ID ACCA_NEIG1 Reviewed; 319 AA. AC Q5F8F5; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=accA {ECO:0000255|HAMAP-Rule:MF_00823}; GN OrderedLocusNames=NGO0821; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89532.1; -; Genomic_DNA. DR RefSeq; WP_003691155.1; NC_002946.2. DR RefSeq; YP_207944.1; NC_002946.2. DR ProteinModelPortal; Q5F8F5; -. DR SMR; Q5F8F5; 5-314. DR EnsemblBacteria; AAW89532; AAW89532; NGO_0821. DR GeneID; 3282210; -. DR KEGG; ngo:NGO0821; -. DR PATRIC; 20334796; VBINeiGon24812_0968. DR HOGENOM; HOG000273832; -. DR KO; K01962; -. DR OMA; HSVYTVA; -. DR OrthoDB; EOG6HQSSF; -. DR BioCyc; NGON242231:GI2G-774-MONOMER; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000535; 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_0000223788. SQ SEQUENCE 319 AA; 35420 MW; 508A824759E89ECB CRC64; MKPVFLDFEQ PIAELTNKID ELRFVQDESA VDISDEIHRL QKKSNDLTKS IFSKLTPAQI SQVSRHPQRP YTLDYIDALF TDFEELHGDR HFADDHAIVG GLARFNGQSV VVVGHQKGRD TKEKIRRNFG MPRPEGYRKA LRLMKTAEKF GLPVMTFIDT PGAYPGIGAE ERGQSEAIGK NLYELTRLRV PVLCTVIGEG GSGGALAVAV GDYVNMLQYS TYSVISPEGC ASILWKTAEK AADAAQALGI TADRLQKLDL VDTVIKEPLG GAHRDFGQTM KNVKAVLEKQ LHEAQSIPLA DLLSRRFDRI MAYGKFSEQ // ID ACPS_NEIG1 Reviewed; 125 AA. AC Q5F6P2; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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}; GN OrderedLocusNames=NGO1507; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90145.1; -; Genomic_DNA. DR RefSeq; WP_003695557.1; NC_002946.2. DR RefSeq; YP_208557.1; NC_002946.2. DR ProteinModelPortal; Q5F6P2; -. DR EnsemblBacteria; AAW90145; AAW90145; NGO_1507. DR GeneID; 3281569; -. DR KEGG; ngo:NGO1507; -. DR PATRIC; 20336488; VBINeiGon24812_1792. DR HOGENOM; HOG000014316; -. DR KO; K00997; -. DR OMA; GHTERGQ; -. DR OrthoDB; EOG6384R9; -. DR BioCyc; NGON242231:GI2G-1411-MONOMER; -. DR Proteomes; UP000000535; 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_0000228292. 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; 13509 MW; 64AD8220BB5AB12E CRC64; MIYGIGTDIV SLKRIIRLNK KFGQAFAGRI LTPEELLEFP QAGKPVNYLA KRFAAKEAFA KAVGTGIRGA VSFCNIGIGH DALGKPEFFY GPALSEWLEE QGISRVSLSM ADEGDTVLAF AVAEK // ID ACP_NEIG1 Reviewed; 78 AA. AC Q5F604; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. 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=NGO1762; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90383.1; -; Genomic_DNA. DR RefSeq; WP_003689968.1; NC_002946.2. DR RefSeq; YP_208795.1; NC_002946.2. DR ProteinModelPortal; Q5F604; -. DR SMR; Q5F604; 2-78. DR EnsemblBacteria; AAW90383; AAW90383; NGO_1762. DR GeneID; 3281138; -. DR KEGG; ngo:NGO1762; -. DR PATRIC; 20337138; VBINeiGon24812_2109. DR HOGENOM; HOG000178184; -. DR KO; K02078; -. DR OMA; IKPESSF; -. DR OrthoDB; EOG6MWNJM; -. DR BioCyc; NGON242231:GI2G-1658-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000535; 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_1000066641. FT MOD_RES 37 37 O-(pantetheine 4'-phosphoryl)serine. FT {ECO:0000255|HAMAP-Rule:MF_01217}. SQ SEQUENCE 78 AA; 8525 MW; 5A3691085515A975 CRC64; MSNIEQQVKK IIAEQLGVNE ADVKNESSFQ DDLGADSLDT VELVMALEEA FGCEIPDEDA EKITTVQLAI DYINAHNG // ID ANMK_NEIG1 Reviewed; 367 AA. AC Q5F6H5; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 2. DT 16-MAR-2016, entry version 66. 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=NGO1583; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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=AAW90212.1; 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; AE004969; AAW90212.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F6H5; -. DR EnsemblBacteria; AAW90212; AAW90212; NGO_1583. DR PATRIC; 20336694; VBINeiGon24812_1893. DR HOGENOM; HOG000256309; -. DR OrthoDB; EOG64N9WW; -. DR BioCyc; NGON242231:GI2G-1480-MONOMER; -. DR UniPathway; UPA00343; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000535; 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_0000250013. FT NP_BIND 13 20 ATP. {ECO:0000255|HAMAP-Rule:MF_01270}. SQ SEQUENCE 367 AA; 39995 MW; 54D01140A93219BD CRC64; MMETQLYIGI MSGTSMDGAD AVLVRMDGGK WLGAEGHAFT PYPDRLRRKL LDLQDTGTDE LHRSRMLSQE LSRLYAQTAA ELLCSQNLAP CDITALGCHG QTVRHAPEHG YSIQLADLPL LAELTRIFTV GDFRSRDLAA GGQGAPLVPA FHEALFRDDR ETRVVLNIGG IANISVLPPG APAFGFDTGP GNMLMDAWTQ AHWQLPYDKN GAKAAQGNIL PQLLGRLLAH PYFSQPHPKS TGRELFALNW LETYLDGGEN RYDVLRTLSR FTAQTVCDAV SHAAADARQM YICGGGIRNP VLMADLAECF GTRVSLHSTA ELNLDPQWVE AAAFAWLAAC WINRIPGSPH KATGASKPCI LGAGYYY // ID ALR_NEIG1 Reviewed; 352 AA. AC Q5F788; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO1295; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89949.1; -; Genomic_DNA. DR RefSeq; WP_010951235.1; NC_002946.2. DR RefSeq; YP_208361.1; NC_002946.2. DR ProteinModelPortal; Q5F788; -. DR SMR; Q5F788; 1-351. DR EnsemblBacteria; AAW89949; AAW89949; NGO_1295. DR GeneID; 3281857; -. DR KEGG; ngo:NGO1295; -. DR PATRIC; 20335935; VBINeiGon24812_1522. DR HOGENOM; HOG000031446; -. DR KO; K01775; -. DR OMA; PSDWVRP; -. DR OrthoDB; EOG6PP9NJ; -. DR BioCyc; NGON242231:GI2G-1207-MONOMER; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000535; 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_1000066015. 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; 38877 MW; CFAAC79B56106B93 CRC64; MRPLNVQIRL GNLRHNYRIL KEMHGGKLLA VVKADAYGHG AVRCAFALAD LADGFAVATI DEGIRLRESG ITHPIVLLEG VFEASEYEAV EQYSLWPAVG NQWQLEALLS RHWKKPVKVW LKMDSGMHRT GFFPHDYTSA YAALKQSEYV DSIVKFSHFS CADEPESGMT EIQMEAFDLG TKGLEGEESL ANSAAILNIP EARRDWGRAG LALYGISPFG GSDDRLKPVM RLSTRIFGER VLQPHSPIGY GATFYTSKST RVGLIACGYA DGYPRRAPSN SPVAVDGKLT RVIGRISMDM MTIELDASQE GLGHEVELWG DTVNINTVAE AAGTIPYELM CNIKRAKFTY IE // ID APAH_NEIG1 Reviewed; 276 AA. AC Q5FA03; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000255|HAMAP-Rule:MF_00199}; DE EC=3.6.1.41 {ECO:0000255|HAMAP-Rule:MF_00199}; DE AltName: Full=Ap4A hydrolase {ECO:0000255|HAMAP-Rule:MF_00199}; DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00199}; DE AltName: Full=Diadenosine tetraphosphatase {ECO:0000255|HAMAP-Rule:MF_00199}; GN Name=apaH {ECO:0000255|HAMAP-Rule:MF_00199}; GN OrderedLocusNames=NGO0231; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to CC yield ADP. {ECO:0000255|HAMAP-Rule:MF_00199}. CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate + CC H(2)O = 2 ADP. {ECO:0000255|HAMAP-Rule:MF_00199}. CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family. CC {ECO:0000255|HAMAP-Rule:MF_00199}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88984.1; -; Genomic_DNA. DR RefSeq; WP_003687564.1; NC_002946.2. DR RefSeq; YP_207396.1; NC_002946.2. DR ProteinModelPortal; Q5FA03; -. DR EnsemblBacteria; AAW88984; AAW88984; NGO_0231. DR GeneID; 3281453; -. DR KEGG; ngo:NGO0231; -. DR PATRIC; 20333407; VBINeiGon24812_0285. DR HOGENOM; HOG000251871; -. DR KO; K01525; -. DR OMA; INAFTRM; -. DR OrthoDB; EOG66B3WP; -. DR BioCyc; NGON242231:GI2G-215-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 2. DR HAMAP; MF_00199; ApaH; 1. DR InterPro; IPR004617; ApaH. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00668; apaH; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 276 Bis(5'-nucleosyl)-tetraphosphatase, FT symmetrical. FT /FTId=PRO_1000012071. SQ SEQUENCE 276 AA; 30879 MW; 4163840FC6E16CF6 CRC64; MAHYAIGDIQ GCFDELTALL GKIGFNHGTD TLWLTGDIVN RGPKSLETLQ FCIRHENSVQ IVLGNHDLYL LAVGCGEGAL KRSDTIEPIL KHPDGGKMLD WLRAQPLLIR EGGRVMIHAG ILPQWRIAKA ESLAGEAEAE LRGKKYVKFF SKMYGNKPAA WDEGLEGYAR LRFIVNAFTR MRALTFKNEL DFDYKSTVKK MPPYLRPWFK APDRQNLDHT IIFGHWSSLG YTNADNVISL DTGALWGGQL TAVNLETEEI TQVQAAGGID WKSFAK // ID ARGJ_NEIG1 Reviewed; 406 AA. AC Q5F7I3; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO1194; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89854.1; -; Genomic_DNA. DR RefSeq; WP_003691802.1; NC_002946.2. DR RefSeq; YP_208266.1; NC_002946.2. DR ProteinModelPortal; Q5F7I3; -. DR MEROPS; T05.001; -. DR EnsemblBacteria; AAW89854; AAW89854; NGO_1194. DR GeneID; 3282038; -. DR KEGG; ngo:NGO1194; -. DR PATRIC; 20335685; VBINeiGon24812_1401. DR HOGENOM; HOG000022798; -. DR KO; K00620; -. DR OMA; ADHSFNS; -. DR OrthoDB; EOG6P8TQQ; -. DR BioCyc; NGON242231:GI2G-1106-MONOMER; -. DR UniPathway; UPA00068; UER00106. DR UniPathway; UPA00068; UER00111. DR Proteomes; UP000000535; 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_0000227234. FT CHAIN 190 406 Arginine biosynthesis bifunctional FT protein ArgJ beta chain. FT {ECO:0000255|HAMAP-Rule:MF_01106}. FT /FTId=PRO_0000227235. 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; 42851 MW; A3F3635905E2C856 CRC64; MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA YAAARSPLVK TAFFASDPNL GRLLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS // ID AROA_NEIG1 Reviewed; 433 AA. AC Q5F889; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 84. 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=NGO0900; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89598.1; -; Genomic_DNA. DR RefSeq; WP_010951148.1; NC_002946.2. DR RefSeq; YP_208010.1; NC_002946.2. DR ProteinModelPortal; Q5F889; -. DR EnsemblBacteria; AAW89598; AAW89598; NGO_0900. DR GeneID; 3281109; -. DR KEGG; ngo:NGO0900; -. DR PATRIC; 20334981; VBINeiGon24812_1060. DR HOGENOM; HOG000247372; -. DR KO; K00800; -. DR OMA; IGRNSVQ; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NGON242231:GI2G-840-MONOMER; -. DR UniPathway; UPA00053; UER00089. DR Proteomes; UP000000535; 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. 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_1000099730. 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; 46744 MW; 5548C56AAD0B5A67 CRC64; MTESVRLPAA SPKPSTVALP GSKSISNRTL LLAALSDNVC EIHSLLKSDD TDRMLEALDK LGVQIEHLAE GRLKVHGTGG RFPNRSADLF LGNAGTAFRP LTAALAVLGG DYHLHGVPRM HERPIGDLVD ALRIAGADVE YLGNEHYPPL HIGKRQDCGE RVIPIKGNVS SQFLTALLMA LPLTGQAFEI RMVGELISKP YIDITLKLMA QFGVQVANEG YRVFKIPADA HYHAPEHLHV EGDASGASYF LAAGLIAATP VRVTGIGANS IQGDVAFARE LEKIGADVVW GENFVEVSRP KGRAVQAFDL DANHIPDAAM TLAIVALATR QTCTLRNIGS WRVKETGRIA AMANELRKLG AKVVEEAEAI HITPPETPTP DAVIDTYDDH RMAMCFSLIS LLGVPVVIND PKCTHKTFPT YFEVFSSLTE TAE // ID ARGB_NEIG1 Reviewed; 298 AA. AC Q5F8D8; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO0844; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89549.1; -; Genomic_DNA. DR RefSeq; WP_003706280.1; NC_002946.2. DR RefSeq; YP_207961.1; NC_002946.2. DR ProteinModelPortal; Q5F8D8; -. DR SMR; Q5F8D8; 9-294. DR EnsemblBacteria; AAW89549; AAW89549; NGO_0844. DR GeneID; 3282514; -. DR KEGG; ngo:NGO0844; -. DR PATRIC; 20334856; VBINeiGon24812_0998. DR HOGENOM; HOG000233259; -. DR KO; K00930; -. DR OMA; PKTECCI; -. DR OrthoDB; EOG6T1WVF; -. DR BioCyc; NGON242231:GI2G-791-MONOMER; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000000535; 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_0000264722. 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; 31417 MW; 4DB408E115F0E29D CRC64; MEFENIISAA DKARILAEAL PYIRRFSGSV AVIKYGGNAM TEPALKEGFA RDVVLLKLVG IHPVIVHGGG PQINAMLEKV GKKGEFVQGM RVTDKETMDI VEMVLGGHVN KEIVSMINTY GGHAVGVSGR DDHFIKAKKL LVDTPEQNSV DIGQVGTVES IDTGLVKGLI ERGCIPVVAP VGVGEKGEAF NINADLVAGK LAEELNAEKL LMMTNIAGVM DKTGNLLTKL TPKRIDGLIA DGTLYGGMLP KIASAVEAAV NGVKATHIID GRLPNALLLE IFTDAGIGSM ILGRGEDA // ID ARGC_NEIG1 Reviewed; 347 AA. AC Q5FAA9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 85. 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=NGO0118; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88878.1; -; Genomic_DNA. DR RefSeq; WP_010950995.1; NC_002946.2. DR RefSeq; YP_207290.1; NC_002946.2. DR ProteinModelPortal; Q5FAA9; -. DR EnsemblBacteria; AAW88878; AAW88878; NGO_0118. DR GeneID; 3282346; -. DR KEGG; ngo:NGO0118; -. DR PATRIC; 20333139; VBINeiGon24812_0153. DR HOGENOM; HOG000254904; -. DR KO; K00145; -. DR OMA; TFVPHLT; -. DR OrthoDB; EOG6XSZS3; -. DR BioCyc; NGON242231:GI2G-107-MONOMER; -. DR UniPathway; UPA00068; UER00108. DR Proteomes; UP000000535; 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_0000112426. FT ACT_SITE 152 152 {ECO:0000255|HAMAP-Rule:MF_00150}. SQ SEQUENCE 347 AA; 37176 MW; 08F4E298D9D0E959 CRC64; MSKKIKAGIV GATGYTGVEL LRLLAAHPDV EVAAVTSRSE AGTAVADYFP SLRGVYGLAF QTPDEAGLEQ CDIVFFATPN GIAMKDAPRL LEQGVRVIDL SADFRIRDIP TWEHWYGMTH AAPGLVSQAV YGLSELNREA VAQARLVANP GCYPTCVSLP LVPLLRQCRL KPGMPLIADC KSGVSGAGRK GNVGSLLCEA GDNFKAYGTA GHRHLPEIRQ TIAGLQDGIA EGFVFTPHLA PMIRGMHATV YLHLSDGSDP ETVLRDYYRD SPFMDILPAG STPETRSVRG ANLCRISIRQ AAQSDVWVVL SVIDNLVKGA AGQAVQNMNI MFGLEETHGL DAIPLLP // ID APT_NEIG1 Reviewed; 188 AA. AC Q5F774; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-MAR-2016, entry version 76. 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=NGO1311; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89963.1; 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; AE004969; AAW89963.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F774; -. DR EnsemblBacteria; AAW89963; AAW89963; NGO_1311. DR PATRIC; 20335983; VBINeiGon24812_1542. DR HOGENOM; HOG000036776; -. DR OrthoDB; EOG6T4S55; -. DR BioCyc; NGON242231:GI2G-1226-MONOMER; -. DR UniPathway; UPA00588; UER00646. DR Proteomes; UP000000535; 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_0000321374. SQ SEQUENCE 188 AA; 20413 MW; 9841E8CB76CFEF5D CRC64; MLVHPEAMSV GALADKIRKI ENWPQKGILF HDITPVLQSA EYFRLLVDLL VYRYMDQKID IVAGLDARGF IIGAALAYQL NVGFVPIRKK GKLPFETVSQ SYALEYGEAA VEIHTDAVKP GSRVLLVDDL VATGGTMLAG LELIRKLGGE IVEAAAILEF TDLQGGKNIR ASGAPLFTLL QNEGCMKG // ID AROB_NEIG1 Reviewed; 359 AA. AC Q5FAD4; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO0092; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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=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 -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={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; AE004969; AAW88853.1; -; Genomic_DNA. DR RefSeq; WP_003690567.1; NC_002946.2. DR RefSeq; YP_207265.1; NC_002946.2. DR ProteinModelPortal; Q5FAD4; -. DR EnsemblBacteria; AAW88853; AAW88853; NGO_0092. DR GeneID; 3282137; -. DR KEGG; ngo:NGO0092; -. DR PATRIC; 20333073; VBINeiGon24812_0120. DR HOGENOM; HOG000007970; -. DR KO; K01735; -. DR OMA; IERSCAA; -. DR OrthoDB; EOG6SJJGD; -. DR BioCyc; NGON242231:GI2G-82-MONOMER; -. DR UniPathway; UPA00053; UER00085. DR Proteomes; UP000000535; 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_0000231100. SQ SEQUENCE 359 AA; 38581 MW; BE705DB9B44DEDBE CRC64; MKTLTVHTPS HSYPIFIGNG LLPQAGSLLK PHLGKRAAII TNETVAPLYL GTLQTALDAA GVSHFSIILP DGEAHKNWQT LNLIFDGLMQ NRAERKTTLI ALGGGVIGDM VGFAAATYQR GAPFIQIPTT LLSQVDSSVG GKTAINHPLG KNMIGAFYQP QAVLADLDTL HTLPARELSA GMAEVIKYGA LGDIGFFEWL EQHMPELMAL ERAPLTQAVY RCCQMKADIV AQDETEQGIR AWLNLGHTFG HAVEAEMGYG VWLHGEAVAA GCVLAARLSE QLGKTSAADT ARLAALLEAA GLPSAPPVFA FEKWLAHMSH DKKVSGGIMR FIGLNRLGEA VITEITDTDI LRRTLQPYL // ID AROE_NEIG1 Reviewed; 269 AA. AC Q5F6F7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO1602; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90230.1; -; Genomic_DNA. DR RefSeq; WP_003689536.1; NC_002946.2. DR RefSeq; YP_208642.1; NC_002946.2. DR ProteinModelPortal; Q5F6F7; -. DR SMR; Q5F6F7; 5-267. DR EnsemblBacteria; AAW90230; AAW90230; NGO_1602. DR GeneID; 3281609; -. DR KEGG; ngo:NGO1602; -. DR PATRIC; 20336740; VBINeiGon24812_1916. DR HOGENOM; HOG000237876; -. DR KO; K00014; -. DR OMA; FGNPIKH; -. DR OrthoDB; EOG6RRKMV; -. DR BioCyc; NGON242231:GI2G-1498-MONOMER; -. DR UniPathway; UPA00053; UER00087. DR Proteomes; UP000000535; 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_1000021311. 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; 28649 MW; 07FFD1FCF1A5FDD9 CRC64; MHALPRYAVF GNPAAHSKSP QIHQQFALQE GVDIEYGRIC ADIGGFAQAV STFFETGGCG ANVTVPFKQE AFHLADEHSD RALAAGAVNT LVWLEDGRIR GDNTDGIGLA NDITQVKNIA IEGKTILLLG AGGAVRGVIP VLKEHRPARI VIANRTRAKA EELARLFGIE AVPMADVNGG FDIIINGTSG GLSGQLPAVS PKIFRDCRLA YDMVYGEAAK PFLDFARQSG AKKTADGLGM LVGQAAASYA LWRGFKPDIR PVIEHMKAL // ID ARLY_NEIG1 Reviewed; 458 AA. AC Q5FA15; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO0219; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88972.1; -; Genomic_DNA. DR RefSeq; WP_003704829.1; NC_002946.2. DR RefSeq; YP_207384.1; NC_002946.2. DR ProteinModelPortal; Q5FA15; -. DR EnsemblBacteria; AAW88972; AAW88972; NGO_0219. DR GeneID; 3281430; -. DR KEGG; ngo:NGO0219; -. DR PATRIC; 20333377; VBINeiGon24812_0271. DR HOGENOM; HOG000242744; -. DR KO; K01755; -. DR OMA; AHHLMAY; -. DR OrthoDB; EOG6P5ZF8; -. DR BioCyc; NGON242231:GI2G-202-MONOMER; -. DR UniPathway; UPA00068; UER00114. DR Proteomes; UP000000535; 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_0000240741. SQ SEQUENCE 458 AA; 51310 MW; 705B0FF8F6B50540 CRC64; MHDKTWSGRF NEPVSELVKQ YTASIGFDQR LAEWDIQGSL AHAQMLTRSG VLSENDLTDI RRGMSEILEE IRSGKIEWPL DLEDVHMNIE RRLTDKIGDA GKRLHTGRSR NDQVATDIRL WLRDQITVIQ NLIQNLQTAL LDLAEQNAEA VMPGFTHLQV AQPVSFGHHM LAYVEMLGRD FERMTDCRKR VNRMPLGAAA LAGTTYPIQR EITAELLGFE QICQNSLDAV SDRDFAIEFT AAASLVMVHL SRLSEELILW MSPRFGFIDI ADRFCTGSSI MPQKKNPDVP ELVRGKSGRV IGHLIGLITL MKSQPLAYNK DNQEDKEPLF DTADTLIDTL RIYADMMRGV TVKPGNMRAA VMQGFATATD LADYLVKKGM PFRDAHEVVA QAVRHADEAG VDLSELPLEA LQGFSKLISD DVYGVLTPEG SLNARNHLGG TAPEQVRLQV KRWREMSA // ID AROD_NEIG1 Reviewed; 254 AA. AC Q5F8N0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO0740; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89457.1; -; Genomic_DNA. DR RefSeq; WP_003688696.1; NC_002946.2. DR RefSeq; YP_207869.1; NC_002946.2. DR ProteinModelPortal; Q5F8N0; -. DR EnsemblBacteria; AAW89457; AAW89457; NGO_0740. DR GeneID; 3281808; -. DR KEGG; ngo:NGO0740; -. DR PATRIC; 20334618; VBINeiGon24812_0881. DR HOGENOM; HOG000105514; -. DR KO; K03785; -. DR OMA; LFTFRSK; -. DR OrthoDB; EOG6P33BK; -. DR BioCyc; NGON242231:GI2G-697-MONOMER; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000000535; 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_1000043177. 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; 27279 MW; 36F76B48397BD872 CRC64; MHTSLTVKNT VIGSGRTKIA VPLVARDAAD LSSVLSQIKN LPFDIVEFRA DFLECAGSIG EVLRHTQAVR DALPDKPLLF TFRRHCEGGS FPCSDDYYFE LLDALIESRL PDIIDIELFS GETAVRRAVA NAQKNGIAAL LCNHEFHRTP PQEEIVCRLK QMEDCGADIC KIAVMPQSSE DVLTLLSATL EAKRLVAKPV ITMSMGQTGA VSRLAGQVFG SSITFGSGTQ NSAPGQIGVS ALRAALDCLE SGAD // ID AROK_NEIG1 Reviewed; 170 AA. AC Q5FAD3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00109}; 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=NGO0093; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88854.1; -; Genomic_DNA. DR RefSeq; WP_003687349.1; NC_002946.2. DR RefSeq; YP_207266.1; NC_002946.2. DR ProteinModelPortal; Q5FAD3; -. DR EnsemblBacteria; AAW88854; AAW88854; NGO_0093. DR GeneID; 3282244; -. DR KEGG; ngo:NGO0093; -. DR PATRIC; 20333075; VBINeiGon24812_0121. DR HOGENOM; HOG000032568; -. DR KO; K00891; -. DR OMA; LYRECAD; -. DR OrthoDB; EOG6SJJGD; -. DR BioCyc; NGON242231:GI2G-83-MONOMER; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000000535; 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 Shikimate kinase. FT /FTId=PRO_0000237897. 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; 9826408AD07A018D CRC64; MKNFNGKLIL IGLMGAGKTT LGRQMAQRLD YRFYDSDHEI AAAAGVPIPT IFEMEGEQGF RSRETAILKK LIVLPHIVLS TGGGAVLKEE NRALIRKSGT VVYLHAPPET LLERTRCDNS RPLLQVADPL AKLRELYAAR DPVYRQTADF TVESANCRET VQTLLKRLSR // ID ASSY_NEIG1 Reviewed; 447 AA. AC Q5F5G5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00581}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00581}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00581}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00581}; GN OrderedLocusNames=NGO1961; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000255|HAMAP- CC Rule:MF_00581}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00581}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00581}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90572.1; -; Genomic_DNA. DR RefSeq; WP_003688135.1; NC_002946.2. DR RefSeq; YP_208984.1; NC_002946.2. DR ProteinModelPortal; Q5F5G5; -. DR SMR; Q5F5G5; 6-445. DR EnsemblBacteria; AAW90572; AAW90572; NGO_1961. DR GeneID; 3282660; -. DR KEGG; ngo:NGO1961; -. DR PATRIC; 20337675; VBINeiGon24812_2364. DR HOGENOM; HOG000230094; -. DR KO; K01940; -. DR OMA; AFHIRSG; -. DR OrthoDB; EOG6K9QCV; -. DR BioCyc; NGON242231:GI2G-1862-MONOMER; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000535; 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_1000025433. FT NP_BIND 20 28 ATP. {ECO:0000255|HAMAP-Rule:MF_00581}. FT BINDING 46 46 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 102 102 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 132 132 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00581}. FT BINDING 134 134 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 134 134 ATP. {ECO:0000255|HAMAP-Rule:MF_00581}. FT BINDING 138 138 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 138 138 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 139 139 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 139 139 ATP. {ECO:0000255|HAMAP-Rule:MF_00581}. FT BINDING 142 142 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 195 195 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 197 197 ATP. {ECO:0000255|HAMAP-Rule:MF_00581}. FT BINDING 204 204 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 206 206 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. FT BINDING 283 283 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00581}. SQ SEQUENCE 447 AA; 49688 MW; 5599BEE27EB3BA46 CRC64; MNQNHTILQN LPVGQKVGIA FSGGLDTSAA LLWMKLKGAL PYAYTANLGQ PDEDDYNAIP KKAMEYGAEN ARLIDCRAQL AHEGIAAIQC GAFHVSTGGI AYFNTTPLGR AVTGTMLVSA MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT NPALKIYKPW LDQQFIDELG GRHEMSEFLI ANGFNYKMSV EKAYSTDSNM LGATHEAKDL EFLNSGIKIV KPIMGVAFWD ENVEIEPEEV SVRFEEGVPV ALNGKEYADP VELFLEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM ALFHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET AQRWVAKAVT GEVTLELRRG NDYSILNTES PNLTYQPERL SMEKVEGAAF TPLDRIGQLT MRNLDITDTR AKLGIYSQSG LLSLGEGSVL PQLGNKQ // ID ATPA_NEIG1 Reviewed; 515 AA. AC Q5F4Z2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO2148; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90745.1; -; Genomic_DNA. DR RefSeq; WP_003687154.1; NC_002946.2. DR RefSeq; YP_209157.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z2; -. DR SMR; Q5F4Z2; 29-511. DR PRIDE; Q5F4Z2; -. DR EnsemblBacteria; AAW90745; AAW90745; NGO_2148. DR GeneID; 3282773; -. DR KEGG; ngo:NGO2148; -. DR PATRIC; 20338149; VBINeiGon24812_2597. DR HOGENOM; HOG000130111; -. DR KO; K02111; -. DR OMA; PVFCIYV; -. DR OrthoDB; EOG67X1S1; -. DR BioCyc; NGON242231:GI2G-2039-MONOMER; -. DR Proteomes; UP000000535; 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_0000238299. 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; 55241 MW; F10EE6F8F7144565 CRC64; MQLNPAEISD LIKAKIENLS VNAEVSTRGT VISVTDGIVR IHGLSDAMQG EMLEFPGNTL GLAMNLERDS VGAVVLGEYE HIKEGDTVTC TGRILEVPVG RELVGRVVDA LGRPIDGKGP INTTLTAPVE KIAPGVIARK SVDQPMQTGL KAIDSMIPVG 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 AROC_NEIG1 Reviewed; 366 AA. AC Q5F756; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO1331; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89981.1; -; Genomic_DNA. DR RefSeq; WP_003701548.1; NC_002946.2. DR RefSeq; YP_208393.1; NC_002946.2. DR ProteinModelPortal; Q5F756; -. DR EnsemblBacteria; AAW89981; AAW89981; NGO_1331. DR GeneID; 3282016; -. DR KEGG; ngo:NGO1331; -. DR PATRIC; 20336031; VBINeiGon24812_1565. DR HOGENOM; HOG000060335; -. DR KO; K01736; -. DR OMA; MLSINAV; -. DR OrthoDB; EOG6WDSHT; -. DR BioCyc; NGON242231:GI2G-1245-MONOMER; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000000535; 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. 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_0000140616. 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; 39334 MW; 167EC75899081287 CRC64; MAGNTFGQIF TVTTFGESHG AGLGCIIDGC PPGLELSEAD IQFDLDRRKP GTSRHVTQRR EADQVEILSG VFEGKTTGTP IALLIRNTDQ RSKDYGNIAT AFRPGHADYT YWHKYGTRDY RGGGRSSARE TAARVAAGAV AKKWLKEKFG TEITAYVTQV GEKKIRFEGS EHISQNPFFA ANQSQIAELE HYMDGVRKSL DSVGAKLHIE AANVPVGLGE PVFDRLDAEI AYAMMGINAV KGVEIGAGFD SVTQRGSEHG DELTPQGFLS NHSGGILGGI STGQDICVNI AIKPTSSIAT PRRSIDIHGN PVELATRGRH DPCVGLRTAP IAEAMLALVL IDHALRHRAQ NADVAADTPD ISRSDK // ID ATPB_NEIG1 Reviewed; 465 AA. AC Q5F4Z0; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 88. 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=NGO2150; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90747.1; -; Genomic_DNA. DR RefSeq; WP_003690451.1; NC_002946.2. DR RefSeq; YP_209159.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z0; -. DR SMR; Q5F4Z0; 2-464. DR PRIDE; Q5F4Z0; -. DR EnsemblBacteria; AAW90747; AAW90747; NGO_2150. DR GeneID; 3282771; -. DR KEGG; ngo:NGO2150; -. DR PATRIC; 20338153; VBINeiGon24812_2599. DR HOGENOM; HOG000009605; -. DR KO; K02112; -. DR OMA; AEFGIYP; -. DR OrthoDB; EOG6HQSP3; -. DR BioCyc; NGON242231:GI2G-2041-MONOMER; -. DR Proteomes; UP000000535; 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_0000254311. FT NP_BIND 148 155 ATP. {ECO:0000255|HAMAP-Rule:MF_01347}. SQ SEQUENCE 465 AA; 50423 MW; 70331857B2149B3F CRC64; MSQGKIVQII GAVVDVEFPR DMIPRVYDAL KLDENGLTLE VQQLLGDGVV RTIAMGSSDG LKRGMTVSNT GSPITVPVGK GTLGRIVDVL GTPVDEAGPI DTDKSRAIHQ AAPKFDELSS TTELLETGIK VIDLLCPFAK GGKVGLFGGA GVGKTVNMME LINNIAKAHS GLSVFSGVGE RTREGNDFYH EMKDSNVLDK VAMVYGQMNE PPGNRLRVAL TGLTMAEYFR DEKDENGKGR DVLFFVDNIY RYTLAGTEVS ALLGRMPSAV GYQPTLAEEM GRLQERITST QTGSITSIQA VYVPADDLTD PSPATTFAHL DATVVLSRDI ASLGIYPAVD PLDSTSRQLD PMVLGQEHYD VARGVQSTLQ KYKELRDIIA ILGMDELSDE DKLAVMRARK IQRFLSQPFH VAEVFTGSPG KYVALRDTIA GFKAILNGEY DHLPEQAFYM VGSIEEAVEK AKTLN // ID ATPF_NEIG1 Reviewed; 156 AA. AC Q5F4Z4; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO2146; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90743.1; -; Genomic_DNA. DR RefSeq; WP_003687152.1; NC_002946.2. DR RefSeq; YP_209155.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z4; -. DR EnsemblBacteria; AAW90743; AAW90743; NGO_2146. DR GeneID; 3282775; -. DR KEGG; ngo:NGO2146; -. DR PATRIC; 20338145; VBINeiGon24812_2595. DR HOGENOM; HOG000015378; -. DR KO; K02109; -. DR OMA; ILVWFTM; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; NGON242231:GI2G-2037-MONOMER; -. DR Proteomes; UP000000535; 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_0000368619. FT TRANSMEM 7 27 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01398}. SQ SEQUENCE 156 AA; 17139 MW; 6DE2BAC3C57874C5 CRC64; MNINATLFAQ IIVFFGLVWF TMKFVWPPIA KALDERAAKI AEGLAAAERG KSDFEQAEKK VAELLAEGRN QVSEMVANAE KRAAKIVEEA KEQASSEAAR IAAQAKADVE QELFRARESL RDQVAVLAVK GAESILRSEV DASKHAKLLD TLKQEL // ID ATPD_NEIG1 Reviewed; 177 AA. AC Q5F4Z3; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO2147; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90744.1; -; Genomic_DNA. DR RefSeq; WP_002214793.1; NC_002946.2. DR RefSeq; YP_209156.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z3; -. DR EnsemblBacteria; AAW90744; AAW90744; NGO_2147. DR GeneID; 3282774; -. DR KEGG; ngo:NGO2147; -. DR PATRIC; 20338147; VBINeiGon24812_2596. DR HOGENOM; HOG000075825; -. DR KO; K02113; -. DR OMA; ITSAFEM; -. DR OrthoDB; EOG6DNTDK; -. DR BioCyc; NGON242231:GI2G-2038-MONOMER; -. DR Proteomes; UP000000535; 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_0000371033. SQ SEQUENCE 177 AA; 19498 MW; 05B7F468BF31CB23 CRC64; MAEFATIARP YAKALFGLAQ EKNQIESWLG GLEKLAAVVQ EGKVASLIDR PETNASEKAD ILIDLVGLKD KELKNFVIVL AGQKRLSILP EVYAQYQDLT LSFNHIKSAV IYSAYPLTDK QVGELAQMLN KRFDSELKIS VEIEPELIGG IKVEVGDQVL DLSVQGKLSA LYTTMTN // ID ATPE_NEIG1 Reviewed; 140 AA. AC Q5F4Y9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO2151; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90748.1; -; Genomic_DNA. DR RefSeq; WP_003687159.1; NC_002946.2. DR RefSeq; YP_209160.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y9; -. DR EnsemblBacteria; AAW90748; AAW90748; NGO_2151. DR GeneID; 3282770; -. DR KEGG; ngo:NGO2151; -. DR PATRIC; 20338155; VBINeiGon24812_2600. DR HOGENOM; HOG000216025; -. DR KO; K02114; -. DR OMA; HHRAEVA; -. DR OrthoDB; EOG690MN9; -. DR BioCyc; NGON242231:GI2G-2042-MONOMER; -. DR Proteomes; UP000000535; 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; PF00401; ATP-synt_DE; 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_0000265844. SQ SEQUENCE 140 AA; 14987 MW; 5E4A3B88B95AA564 CRC64; MSIMQVEVVS GEQKIYSGEA TFIVVPTVQG ELGIYPRHEP IMSLVRPGAL RLTVPGEDKE VLVAVSGGIL EVQPDKVTVL ADVAVRSAEM DRARAEEAKK AAEAGISQAK DDKALAEAHK ALAAAIAQLK TLDYIRSHKK // ID BICOA_NEIG1 Reviewed; 592 AA. AC Q5F5C8; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO2001; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90609.1; -; Genomic_DNA. DR RefSeq; WP_010951380.1; NC_002946.2. DR RefSeq; YP_209021.1; NC_002946.2. DR ProteinModelPortal; Q5F5C8; -. DR EnsemblBacteria; AAW90609; AAW90609; NGO_2001. DR GeneID; 3282623; -. DR KEGG; ngo:NGO2001; -. DR PATRIC; 20337779; VBINeiGon24812_2413. DR HOGENOM; HOG000220772; -. DR KO; K01947; -. DR OMA; RPAGKRY; -. DR OrthoDB; EOG6G20K0; -. DR BioCyc; NGON242231:GI2G-1902-MONOMER; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000000535; 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_0000270882. 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; 64167 MW; 1FEA35BF638D2BF6 CRC64; MTVLKPSHWR VLAELADGLP QHVSQLAREA DMKPQQLNGF WQQMPAHIRG LLRQHDGYWR LVRPLAVFDA EGLRDLGERS GFQTALKHEC ASSNDEILEL ARIAPDKAHK TICVTHLQSK GRGRQGRKWS HRLGECLMFS FGWAFDRPQY ELGSLSPVAA LACRRALGCL GLETQIKWPN DLVVGRDKLG GILIETVRAG GKTVAVVGIG INFVLPKEVE NAASVQSLFQ TASRRGNADA AVLLETLLAE LGAVLEQYAE EGFAPFLNEY ETANRDHGKA VLLLRDGETV CEGTVKGVDG RGVLHLETAE GEQTVVSGEI SLRPDNRSVS VPKRPDSERF LLLEGGNSRL KWAWVENGTF ATVGSAPYRD LSPLGAEWAE KADGNVRIVG CAVCGESKKA QVKEQLARKI EWLPSSAQAL GIRNHYRHPE EHGSDRWFNA LGSRRFSRNA CVVVSCGTAV TVDALTDDGH YLGGTIMPGF HLMKESLAVR TANLNRPAGK RYPFPTTTGN AVASGMMDAV CGSIMMMHGR LKEKNGAGKP VDVIITGGGA AKVAEALPPA FLAENTVRVA DNLVIHGLLN LIAAEGGESE HA // ID ATPG_NEIG1 Reviewed; 291 AA. AC Q5F4Z1; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO2149; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90746.1; -; Genomic_DNA. DR RefSeq; WP_003705028.1; NC_002946.2. DR RefSeq; YP_209158.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z1; -. DR EnsemblBacteria; AAW90746; AAW90746; NGO_2149. DR GeneID; 3282772; -. DR KEGG; ngo:NGO2149; -. DR PATRIC; 20338151; VBINeiGon24812_2598. DR HOGENOM; HOG000215912; -. DR KO; K02115; -. DR OMA; DRGMCGG; -. DR OrthoDB; EOG6R5C97; -. DR BioCyc; NGON242231:GI2G-2040-MONOMER; -. DR Proteomes; UP000000535; 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_0000073327. SQ SEQUENCE 291 AA; 32453 MW; D3D02B7488AC00A1 CRC64; MAVGKEILTK IRSVQNTQKI TKAMQMVSTS KMRKTQERMS LARPYAEKVR MVMSHLAQTN TDHGIPLLES HREIRRVGFI LITSDKGLCG GLNANVLKKF LAQVQEYRNQ GIEEEIVCLG SKGLMACQSI GLNVVASAVN LGDTPKMEML LGPLTELFQR YEKHEIDRIH LVYSGFVNTM RQEPRMEVLL PIGENVIGDS APKSPFSWEY RYEPTALAVL EYLVRRYLES VVYQALSDNM ASEQAARMVA MKAATDNAGN AIKELRLVYN KSRQAAITTE LSEIVAGAAA V // ID BIOB_NEIG1 Reviewed; 350 AA. AC Q5F8G2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=bioB {ECO:0000255|HAMAP-Rule:MF_01694}; GN OrderedLocusNames=NGO0813; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89525.1; -; Genomic_DNA. DR RefSeq; WP_010358160.1; NC_002946.2. DR RefSeq; YP_207937.1; NC_002946.2. DR ProteinModelPortal; Q5F8G2; -. DR SMR; Q5F8G2; 23-330. DR EnsemblBacteria; AAW89525; AAW89525; NGO_0813. DR GeneID; 3281938; -. DR KEGG; ngo:NGO0813; -. DR PATRIC; 20334782; VBINeiGon24812_0961. DR HOGENOM; HOG000239957; -. DR KO; K01012; -. DR OMA; PFDFIRM; -. DR OrthoDB; EOG622PMP; -. DR BioCyc; NGON242231:GI2G-767-MONOMER; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000535; 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_0000381493. 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; 38781 MW; CAD3FC7352529499 CRC64; MTVSPVALRR KTECKPHPTA RYWKKCDVEA LFGLPFLELV YQAAEVHRQN FNPREIQLST LLSIKTGGCP EDCAYCPQSA HHNTNLGKEQ MMDVDEIVEK AKIAKSRGAS RFCMGAAWRG PKPKDVETVS AIIKAVKGLG METCGTFGML EEGMAEDLKE AGLDYYNHNL DTDPDRYNDI IHTRRHEDRM DTLGKVRNAG LKVCCGGIVG MNETRAERAG LIASLANLDP QPESVPINRL VKVEGTPLAD AEDLDWTEFV RTVSVARITM PQSYVRLSAG RSNMPEAMQA MCFMAGANSI FYGDKLLTTG NPDEDGDRIL MEKLNLYPLQ FEPEGEVAEV EKASGIKADY // ID BIOD_NEIG1 Reviewed; 215 AA. AC Q5F9T1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO0309; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89056.1; -; Genomic_DNA. DR RefSeq; WP_003690778.1; NC_002946.2. DR RefSeq; YP_207468.1; NC_002946.2. DR ProteinModelPortal; Q5F9T1; -. DR EnsemblBacteria; AAW89056; AAW89056; NGO_0309. DR GeneID; 3281703; -. DR KEGG; ngo:NGO0309; -. DR PATRIC; 20333601; VBINeiGon24812_0380. DR HOGENOM; HOG000275033; -. DR KO; K01935; -. DR OMA; CINHAVL; -. DR OrthoDB; EOG66B3XT; -. DR BioCyc; NGON242231:GI2G-289-MONOMER; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000535; 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_0000302532. 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; 23676 MW; 48CB57B353B7CD95 CRC64; MKGVYFVSGI DTDIGKTVAT GMLAKQLLQQ GKSVITQKPV QTGCQDIAED IAVHRKIMGI PMQEADEQRL TMPEIFSHPA SPHLAARLDG RGLDLDKIRT ATQELAAQYE VVLVEGAGGL MVPLTEKLLT IDHIQQQAYP VILVTSGRLG SINHTLLSFV VLKQYGIRLH SLVFNHIHDS RDAHVAQDSL NYLQCRLKAD FPEAEWMELA KTGAV // ID BIOF_NEIG1 Reviewed; 380 AA. AC Q5F6R6; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO1483; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90121.1; -; Genomic_DNA. DR RefSeq; WP_010951279.1; NC_002946.2. DR RefSeq; YP_208533.1; NC_002946.2. DR ProteinModelPortal; Q5F6R6; -. DR EnsemblBacteria; AAW90121; AAW90121; NGO_1483. DR GeneID; 3281648; -. DR KEGG; ngo:NGO1483; -. DR PATRIC; 20336415; VBINeiGon24812_1755. DR HOGENOM; HOG000221021; -. DR KO; K00652; -. DR OMA; RDGARKH; -. DR OrthoDB; EOG6PZX7V; -. DR BioCyc; NGON242231:GI2G-1387-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000535; 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_0000381048. 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; 43100 MW; 671FD34280960094 CRC64; MKVFRQQLEQ 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 TQIMPSETCI VPYILGGNEA TLAKAEYLQG QGYYCLPIGP PTVPKNTSRI RLSLTADMTT DEVRQFAACL // ID BIOH_NEIG1 Reviewed; 258 AA. AC Q5F641; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO1725; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90346.1; -; Genomic_DNA. DR RefSeq; WP_010951334.1; NC_002946.2. DR RefSeq; YP_208758.1; NC_002946.2. DR ProteinModelPortal; Q5F641; -. DR ESTHER; neig1-bioh; BioH. DR DNASU; 3281297; -. DR EnsemblBacteria; AAW90346; AAW90346; NGO_1725. DR GeneID; 3281297; -. DR KEGG; ngo:NGO1725; -. DR PATRIC; 20337046; VBINeiGon24812_2063. DR HOGENOM; HOG000028062; -. DR KO; K02170; -. DR OMA; QRERKSM; -. DR OrthoDB; EOG6FJNH9; -. DR BioCyc; NGON242231:GI2G-1621-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. 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_0000204482. 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; 28053 MW; 24DFDB7256026500 CRC64; MRRQQERKFM PDAAKKVYLI HGWGANRHAF DDLMPRLPAT WPVSAVDLPG HGDAPFAQPF DIEAAADGIA AQIDTSADIL GWSLGGLVAL YLAARHPDKV RSLCLTASFA RLTAAEDYPE GLAAPALGKM VGAFRTDYAK HIKQFLQLQL LHTPDAAEII GRILPDLARC GTPQALQEAL DAAERADARH LLDKIDVPVL LVFGGKDAIT PLRMGEYLHR HLKGSRLVVM EKAAHAPFLS HAEAFAALCR DFVEGGLT // ID CAPP_NEIG1 Reviewed; 900 AA. AC Q5F5A9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 16-MAR-2016, entry version 71. 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=NGO2020; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90628.1; -; Genomic_DNA. DR RefSeq; WP_010355840.1; NC_002946.2. DR RefSeq; YP_209040.2; NC_002946.2. DR EnsemblBacteria; AAW90628; AAW90628; NGO_2020. DR GeneID; 3282727; -. DR KEGG; ngo:NGO2020; -. DR PATRIC; 20337823; VBINeiGon24812_2435. DR HOGENOM; HOG000238647; -. DR KO; K01595; -. DR OrthoDB; EOG6TJ7T8; -. DR BioCyc; NGON242231:GI2G-1921-MONOMER; -. DR Proteomes; UP000000535; 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_0000166602. 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; 101122 MW; CB3E85C494759D66 CRC64; MQLHILNNPK DAALAADAEF LKQSLFNLLH EEASPLVVET VKLLSTSDDS AALIEKVLPQ LDERQTYDLT LACGLFAQIL NIAEDVHHER RRQIHEDAGH NAAEGSLTET VRRLKAGKAD GKSVQRQLDN TSVTAVLTAH PTEVQRQTVL NFNRRIRALL PQRERCTNAD ALARLRREID TVLLGLWQTS ETRRHKLSVN DEINNGVSIF PMSFFEALPK LYRKMEHDFQ TAYPDVRVPN ILKIGGWIGG DRDGNPFVSG ETLRFAFRRH ADAVFRFYRS ELDKLYRELP LSIRRVKVND DVMALAALSP DEEIARTEEP YRRAIAYIMA RAMGKARSLG LGMGCKFGFL EPYASAQKFL DDLKKLQRSL IDNGSRLLAE GRLADLIRSV SVFGFHMMPL DLRQHAGKHA DVVAELFQHA GLEDYNSLNE EQKQAALLRE LGHQRPLYSP FITYSDHTRR ELAIFNEARK IKDEFGEDAV TQSIISNCEQ PGDLLALALL LKESGLLAVE NGKPHSRINI VPLFETIEAL ENACPVMETM FRLDWYDALL ESRGNIQEIM LGYSDSNKDG GYVTSSWCLH QAELGLVELF KKYDVRMRLF HGRGGSVGRG GGPSYQAILA QPAGSVAGQI RITEQGEVIT AKYADPGNAQ RNLETLVAAT LEASILPDKK DPDAKLMQAL SDVSFKYYRE LITHPDFIDY FLQTSPIQEI ATLNLGSRPA SRKTLARIQD LRAIPWVFSW MQNRLMLPAW YGFGSAVETL CEGSPETLAA LRGHAQNNPF FQAMLSNMEQ VMAKTDITLA ENYAGLSESP EKAKVIFGMI KEEYRRSRKA LLDLLQTEEL LRDNRSLARS LALRIPYLNA LNGLQVAMLK RLRKEPDNPH ALLMVHLTIN GVAQGLRNTG // ID CCA_NEIG1 Reviewed; 410 AA. AC Q5F8K9; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. 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=NGO0763; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89478.1; -; Genomic_DNA. DR RefSeq; WP_003706239.1; NC_002946.2. DR RefSeq; YP_207890.1; NC_002946.2. DR ProteinModelPortal; Q5F8K9; -. DR EnsemblBacteria; AAW89478; AAW89478; NGO_0763. DR GeneID; 3283071; -. DR KEGG; ngo:NGO0763; -. DR PATRIC; 20334674; VBINeiGon24812_0909. DR HOGENOM; HOG000007368; -. DR KO; K00974; -. DR OMA; APRECQE; -. DR OrthoDB; EOG651SRP; -. DR BioCyc; NGON242231:GI2G-718-MONOMER; -. DR Proteomes; UP000000535; 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 1 410 Multifunctional CCA protein. FT /FTId=PRO_0000138986. 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 410 AA; 45999 MW; 6965E40059C91249 CRC64; MQTYLVGGAV RDYLLGLPVK DRDWVVVGAD AQTMLAQGFQ PVGKDFPVFL HPKTHEEYAL ARTERKTAKG YAGFSFHADK DVTLEQDLMR RDLTINAMAQ DADGKIIDPF GGQRDLAAGI LRHVSPAFAE DPVRILRAAR FAARYGFEIA EETIKLMRQM VENGEADALV AERVWQELAK GLMEKNPRKM IEMLRECGAL QVLLPEVDAL FGVPQRADYH PEIDSGIHTL MTLQRAADMG LSLPERYAAL LHDLGKAKTP PDILPRHHGH DINGVEPVRE VNQRLRAPRQ CAELAELVCR WHIIFHQVGQ LKSQTILNVL KKTDAFRRPE RFQTALNVCI ADTQGRLNRE HTPYPQRAHW LALLEAANQA DSGKIAAECR AQGKAHFIAE QIDRARLAQI APLQKTFRGA // ID CH10_NEIG1 Reviewed; 96 AA. AC Q5F542; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. 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=NGO2094; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90695.1; -; Genomic_DNA. DR RefSeq; WP_003687059.1; NC_002946.2. DR RefSeq; YP_209107.1; NC_002946.2. DR ProteinModelPortal; Q5F542; -. DR SMR; Q5F542; 1-95. DR EnsemblBacteria; AAW90695; AAW90695; NGO_2094. DR GeneID; 3282823; -. DR KEGG; ngo:NGO2094; -. DR PATRIC; 20338023; VBINeiGon24812_2534. DR HOGENOM; HOG000133897; -. DR KO; K04078; -. DR OMA; DTGKEKP; -. DR OrthoDB; EOG6GFGSD; -. DR BioCyc; NGON242231:GI2G-1989-MONOMER; -. DR Proteomes; UP000000535; 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_1000025309. SQ SEQUENCE 96 AA; 10287 MW; A244C8E34BD1C5A4 CRC64; MTIRPLHDRV VVKRLEAEEK TASGIVLPGA AAEKPDMGEV IAVGAGKIGK DGARRPLDVK AGDKIIFGKY SGQTVKADGE ELLVMREEDI FGIVEK // ID CLPS_NEIG1 Reviewed; 100 AA. AC Q5F9I5; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. 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=NGO0409; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89152.1; -; Genomic_DNA. DR RefSeq; WP_010951037.1; NC_002946.2. DR RefSeq; YP_207564.1; NC_002946.2. DR ProteinModelPortal; Q5F9I5; -. DR EnsemblBacteria; AAW89152; AAW89152; NGO_0409. DR GeneID; 3282076; -. DR KEGG; ngo:NGO0409; -. DR PATRIC; 20333829; VBINeiGon24812_0492. DR HOGENOM; HOG000247049; -. DR KO; K06891; -. DR OMA; TENTTKM; -. DR OrthoDB; EOG67Q9F2; -. DR BioCyc; NGON242231:GI2G-387-MONOMER; -. DR Proteomes; UP000000535; 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_0000215727. SQ SEQUENCE 100 AA; 11385 MW; FDAE2256D5F36DEC CRC64; MTAQHQSDTL LHRLNTLPPK RYGVFLLNDD YTTMEFVVEI LTEIFMLGQE QAVAVMLSVH HEGKGLCGTY TRDIAQTKQQ QVMQRAKAEG HPLQCIVEEI // ID CH60_NEIG1 Reviewed; 544 AA. AC Q5F541; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=GroEL protein {ECO:0000255|HAMAP-Rule:MF_00600}; 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}; GN OrderedLocusNames=NGO2095; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90696.1; -; Genomic_DNA. DR RefSeq; WP_003694628.1; NC_002946.2. DR RefSeq; YP_209108.1; NC_002946.2. DR ProteinModelPortal; Q5F541; -. DR SMR; Q5F541; 2-525. DR PRIDE; Q5F541; -. DR EnsemblBacteria; AAW90696; AAW90696; NGO_2095. DR GeneID; 3282822; -. DR KEGG; ngo:NGO2095; -. DR PATRIC; 20338025; VBINeiGon24812_2535. DR HOGENOM; HOG000076290; -. DR KO; K04077; -. DR OMA; SNAMKKV; -. DR OrthoDB; EOG6JDWBZ; -. DR BioCyc; NGON242231:GI2G-1990-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 544 60 kDa chaperonin. FT /FTId=PRO_0000063458. SQ SEQUENCE 544 AA; 57351 MW; 8F8F7C967495EE2F CRC64; MAAKDVQFGN EVRQKMVNGV NILANAVRVT LGPKGRNVVV DRAFGGPHIT KDGVTVAKEI ELKDKFENMG AQMVKEVASK TNDVAGDGTT TATVLAQSIV AEGMKYVTAG MNPTDLKRGI DKAVAALVEE LKNIAKPCDT SKEIAQVGSI SANSDEQVGA IIAEAMEKVG KEGVITVEDG KSLENELDVV EGMQFDRGYL SPYFINDAEK QIAGLDNPFV LLFDKKISNI RDLLPVLEQV AKASRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKAMLQ DIAILTGGVV ISEEVGLSLE KATLDDLGQA KRIEIGKENT TVIDGFGDAA QIEARVAEIR QQIETATSDY DKEKLQERVA KLAGGVAVIK VGAATEVEMK EKKDRVEDAL HATRAAVEEG VVAGGGVALL RARAALENLH TGNADQDAGV QIVLRAVESP LRQIVANAGG EPSVVVNKVL EGKGNYGYNA GSGEYGDMIG MGVLDPAKVT RSALQHAASI AGLMLTTDCM IAEIPEEKPA VPDMGGMGGM GGMM // ID COAE_NEIG1 Reviewed; 210 AA. AC Q5F691; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 16-MAR-2016, entry version 76. 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=NGO1671; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW90296.1; 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; AE004969; AAW90296.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F691; -. DR EnsemblBacteria; AAW90296; AAW90296; NGO_1671. DR PATRIC; 20336894; VBINeiGon24812_1992. DR HOGENOM; HOG000020769; -. DR OrthoDB; EOG6HTP3H; -. DR BioCyc; NGON242231:GI2G-1565-MONOMER; -. DR UniPathway; UPA00241; UER00356. DR Proteomes; UP000000535; 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_0000243307. 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; 22950 MW; 1443ED0A3D4057B5 CRC64; MTAWVGLTGG IGSGKSAAAQ YFADLGVPRI DADAAAHSLT ASDGIALPEI RRLFGDTVFD TQGLLRRDIL RKEIFASPSR KALLESVMLP LIFSEIKKQQ ETFTDAVYGI VEIPLLTEKR QFISLIRRVL TISAPLEKRI GRVMARSGLT RGEVADIISH QASESERLLL ADDVLLNDGS LKSLREKTML LHAFYSGIFA SKPTQGKHNG // ID CLPP_NEIG1 Reviewed; 204 AA. AC Q5F914; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. 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=NGO0593; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89323.1; -; Genomic_DNA. DR RefSeq; WP_003688955.1; NC_002946.2. DR RefSeq; YP_207735.1; NC_002946.2. DR ProteinModelPortal; Q5F914; -. DR SMR; Q5F914; 7-199. DR MEROPS; S14.001; -. DR EnsemblBacteria; AAW89323; AAW89323; NGO_0593. DR GeneID; 3282554; -. DR KEGG; ngo:NGO0593; -. DR PATRIC; 20334260; VBINeiGon24812_0702. DR HOGENOM; HOG000285833; -. DR KO; K01358; -. DR OMA; TAGAKGH; -. DR OrthoDB; EOG6Z3KQ0; -. DR BioCyc; NGON242231:GI2G-563-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; KW Serine protease. FT CHAIN 1 204 ATP-dependent Clp protease proteolytic FT subunit. FT /FTId=PRO_0000179600. FT ACT_SITE 102 102 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00444}. FT ACT_SITE 127 127 {ECO:0000255|HAMAP-Rule:MF_00444}. SQ SEQUENCE 204 AA; 22606 MW; A624FA653575E375 CRC64; MSFDNHLVPT VIEQSGRGER AFDIYSRLLK ERIVFLVGPV TDESANLVVA QLLFLESENP DKDIFFYINS PGGSVTAGMS IYDTMNFIKP DVSTLCLGQA ASMGAFLLSA GEKGKRFALP NSRIMIHQPL ISGGLGGQAS DIEIHARELL KIKEKLNRLM AKHCGRDLAD LERDTDRDNF MSAEEAKEYG LIDQVLENRA SLRL // ID COAD_NEIG1 Reviewed; 171 AA. AC Q5F551; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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}; GN OrderedLocusNames=NGO2085; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90686.1; -; Genomic_DNA. DR RefSeq; WP_003692360.1; NC_002946.2. DR RefSeq; YP_209098.1; NC_002946.2. DR ProteinModelPortal; Q5F551; -. DR EnsemblBacteria; AAW90686; AAW90686; NGO_2085. DR GeneID; 3282832; -. DR KEGG; ngo:NGO2085; -. DR PATRIC; 20338003; VBINeiGon24812_2524. DR HOGENOM; HOG000006518; -. DR KO; K00954; -. DR OMA; RHKQKLG; -. DR OrthoDB; EOG6MH5J7; -. DR BioCyc; NGON242231:GI2G-1980-MONOMER; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000000535; 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 1 171 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_1000011185. SQ SEQUENCE 171 AA; 19600 MW; F0890AE943134989 CRC64; MLPNTPRRAV YAGSFDPPTL GHLWMIRQAQ SMFDELIVAI GINPDKRNTY TVAERQDMLC AITDNFPNVR IEVFQNRFLV HYAREVDAGF IVRGIRSTSD YEYERSMRHI NSDLAPEIST VFLMPPREIA EVSSTMIKGL VGPEGWMETV KRYVPPAVYQ KMIAEHHNNN A // ID CLPX_NEIG1 Reviewed; 414 AA. AC Q5F8W5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 83. 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=NGO0645; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89372.1; -; Genomic_DNA. DR RefSeq; WP_003706165.1; NC_002946.2. DR RefSeq; YP_207784.1; NC_002946.2. DR ProteinModelPortal; Q5F8W5; -. DR SMR; Q5F8W5; 7-41. DR PRIDE; Q5F8W5; -. DR EnsemblBacteria; AAW89372; AAW89372; NGO_0645. DR GeneID; 3281483; -. DR KEGG; ngo:NGO0645; -. DR PATRIC; 20334376; VBINeiGon24812_0760. DR HOGENOM; HOG000010093; -. DR KO; K03544; -. DR OMA; HYKRVQA; -. DR OrthoDB; EOG625JZK; -. DR BioCyc; NGON242231:GI2G-612-MONOMER; -. DR Proteomes; UP000000535; 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_1000024595. 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; 44832 MW; 32CE2097591BA4BC CRC64; MSNENRTCSF CGKSKSHAKH LIEGKNAYIC DECVANCLEI LYEGDNGGTP PENAGGEPEE SGKLPTPAEI VANLDDYVIG QGQAKKALAV AVYNHYKRLR HPKADGGVEL SKSNILLIGP TGSGKTLLAQ SLARKLDVPF VMADATTLTE AGYVGEDVEQ IITKLLGKCD FDVEKARHGI VYIDEIDKIS RKSDNPSITR DVSGEGVQQA LLKLIEGTVA SVPPQGGRKH PNQEFINVDT ANILFICGGA FAGLEKVIRQ RTEKGGIGFG ASVHSKDENA GITKLFGIVE PEDLIKFGLI PELIGRLPVI ATLEELDEDA LINILTEPKN ALVKQYQALF GIENVGLEFE EGALRSIARQ AMERKTGARG LRSIVERCLL DTMYRLPDLQ GLKKVVVGKA VIEEGREPEL VFES // ID CRCB_NEIG1 Reviewed; 119 AA. AC Q5F8D0; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0853; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89557.1; -; Genomic_DNA. DR RefSeq; WP_003688548.1; NC_002946.2. DR RefSeq; YP_207969.1; NC_002946.2. DR EnsemblBacteria; AAW89557; AAW89557; NGO_0853. DR GeneID; 3282247; -. DR KEGG; ngo:NGO0853; -. DR PATRIC; 20334876; VBINeiGon24812_1008. DR HOGENOM; HOG000052572; -. DR KO; K06199; -. DR OMA; IPWGTLA; -. DR OrthoDB; EOG6HXJC8; -. DR BioCyc; NGON242231:GI2G-799-MONOMER; -. DR Proteomes; UP000000535; 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_0000110139. 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 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. SQ SEQUENCE 119 AA; 12535 MW; 7079C6DC19EFC441 CRC64; MLSNILPLSI GAIFGTTARW LLNLAVPASL SPATGNLFAN WTGALLIGIF AETVSHPQWK LLLITGFFGS LTTLSGFSLE TVTLLQSNRP ASALANIFLH TAGSLLLTWL GLKIGTAVK // ID CYAY_NEIG1 Reviewed; 107 AA. AC Q5F536; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE RecName: Full=Protein CyaY {ECO:0000255|HAMAP-Rule:MF_00142}; GN Name=cyaY {ECO:0000255|HAMAP-Rule:MF_00142}; GN OrderedLocusNames=NGO2100; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the frataxin family. {ECO:0000255|HAMAP- CC Rule:MF_00142}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90701.1; -; Genomic_DNA. DR RefSeq; WP_002226758.1; NC_002946.2. DR RefSeq; YP_209113.1; NC_002946.2. DR ProteinModelPortal; Q5F536; -. DR EnsemblBacteria; AAW90701; AAW90701; NGO_2100. DR GeneID; 3282817; -. DR KEGG; ngo:NGO2100; -. DR PATRIC; 20338037; VBINeiGon24812_2541. DR HOGENOM; HOG000190728; -. DR KO; K06202; -. DR OMA; LHQIWVA; -. DR OrthoDB; EOG6GXTXM; -. DR BioCyc; NGON242231:GI2G-1995-MONOMER; -. DR Proteomes; UP000000535; 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_0000193944. SQ SEQUENCE 107 AA; 11996 MW; 182AE37D244CDD81 CRC64; MMTESEFIRA SEALFEHIED QIDENGWDFD CRFAGNVLTI EAGDGTQIIV NRHTPNQELW IAAKSGGYHF AEQNGKWLAT RDSRDFYDVL NEALSAASGE AVEIAEL // ID DAPB_NEIG1 Reviewed; 269 AA. AC Q5F5Y7; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO1781; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90400.1; -; Genomic_DNA. DR RefSeq; WP_003689993.1; NC_002946.2. DR RefSeq; YP_208812.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y7; -. DR SMR; Q5F5Y7; 4-268. DR EnsemblBacteria; AAW90400; AAW90400; NGO_1781. DR GeneID; 3282515; -. DR KEGG; ngo:NGO1781; -. DR PATRIC; 20337204; VBINeiGon24812_2138. DR HOGENOM; HOG000227153; -. DR KO; K00215; -. DR OMA; EAHHRMK; -. DR OrthoDB; EOG6SV5DS; -. DR BioCyc; NGON242231:GI2G-1679-MONOMER; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000535; 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_0000228364. 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; 28269 MW; 22CFE3A65AD0FDE0 CRC64; MIPLKIAIAG ANGRMGRVLV EAVNNHPDTV LSGALEHSGS EALGLDAGYA VGLKTGIAIS DDVDAVLAQS DVLIDFTRPE PTLKHLQKCV EKQVNIIIGT TGFDDAGKAA IRAAAEKTGI VFAANFSVGV NLTFHILDTV ARVLNEGYDI EIIEGHHRHK VDAPSGTALR MGEVIAGALG RDLKQCAVYG REGHTGPRDP STIGFATVRA GDIVGDHTAL FATDGERVEI THKAGSRMTF AAGAVRAAVW VNGKTGLYDM QDVLGLNNR // ID DAPA_NEIG1 Reviewed; 291 AA. AC Q5F849; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. 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=NGO0947; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418}. 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 -!- 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; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00418}. 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; AE004969; AAW89638.1; -; Genomic_DNA. DR RefSeq; WP_003706330.1; NC_002946.2. DR RefSeq; YP_208050.1; NC_002946.2. DR ProteinModelPortal; Q5F849; -. DR EnsemblBacteria; AAW89638; AAW89638; NGO_0947. DR GeneID; 3281803; -. DR KEGG; ngo:NGO0947; -. DR PATRIC; 20335077; VBINeiGon24812_1108. DR HOGENOM; HOG000173604; -. DR KO; K01714; -. DR OMA; GMDACVP; -. DR OrthoDB; EOG6W7235; -. DR BioCyc; NGON242231:GI2G-880-MONOMER; -. DR UniPathway; UPA00034; UER00017. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; KW Reference proteome; Schiff base. FT CHAIN 1 291 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_0000103129. 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}. SQ SEQUENCE 291 AA; 30751 MW; 688CD59FCEAF9882 CRC64; MLQGSLVALI TPMNQDGSIH YDQLRQLIDW HIENGTDGIV AAGTTGESAT LSVEEHLSVI EETVKHVAKR VPVIAGTGAN NTVEAIALSQ AAEKAGADYT LSVVPYYNKP SQEGMYRHFK AVAEAAAIPM ILYNVPGRTV VSMNNETILR LAEIPNIVGV KEASGNVGSN IELINRAPEG FAVLSGDDHT ALPFMLCGGH GVITVAANAA PKLFADMCRA ALQGDIALAR ELNDRLIPIY DTMFCEPSPA APKWAVSALG RCGPHVRLPL VPLTEGGQAK VRAALKASGQ L // ID DAPD_NEIG1 Reviewed; 273 AA. AC Q5F695; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO1667; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90292.1; -; Genomic_DNA. DR RefSeq; WP_003689804.1; NC_002946.2. DR RefSeq; YP_208704.1; NC_002946.2. DR ProteinModelPortal; Q5F695; -. DR SMR; Q5F695; 3-273. DR EnsemblBacteria; AAW90292; AAW90292; NGO_1667. DR GeneID; 3281268; -. DR KEGG; ngo:NGO1667; -. DR PATRIC; 20336884; VBINeiGon24812_1987. DR HOGENOM; HOG000003295; -. DR KO; K00674; -. DR OMA; QVPCALI; -. DR OrthoDB; EOG68H8BV; -. DR BioCyc; NGON242231:GI2G-1561-MONOMER; -. DR UniPathway; UPA00034; UER00019. DR Proteomes; UP000000535; 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; PF00132; Hexapep; 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_0000196950. 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; 29305 MW; 762DD5A632781146 CRC64; MSLQNIIETA FENRADITPT TVAPEVKEAV LETIRQLDSG KLRVAERLGV GEWKVNEWAK KAVLLSFRIQ DNEVLNDGVN KYFDKVPTKF ADWSEDEFKN AGFRAVPGAV ARRGSFVAKN AVLMPSYVNI GAYVDEGAMV DTWATVGSCA QIGKNVHLSG GVGIGGVLEP LQAAPTIIED NCFIGARSEI VEGAIVEEGS VISMGVFIGQ STKIFDRTTG EIYQGRVPAG SVVVSGSLPS KDGSHSLYCA VIVKRVDAQT RAKTSVNELL RGI // ID DAPE_NEIG1 Reviewed; 381 AA. AC Q5F812; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690}; DE Short=SDAP desuccinylase {ECO:0000255|HAMAP-Rule:MF_01690}; DE EC=3.5.1.18 {ECO:0000255|HAMAP-Rule:MF_01690}; DE AltName: Full=N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase {ECO:0000255|HAMAP-Rule:MF_01690}; GN Name=dapE {ECO:0000255|HAMAP-Rule:MF_01690}; GN OrderedLocusNames=NGO0991; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP- CC Rule:MF_01690}. CC -!- CATALYTIC ACTIVITY: N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O CC = succinate + LL-2,6-diaminoheptanedioate. {ECO:0000255|HAMAP- CC Rule:MF_01690}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01690}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01690}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01690}; CC Note=Binds 1 Co(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01690}; 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. {ECO:0000255|HAMAP-Rule:MF_01690}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01690}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. DapE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01690}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89675.1; -; Genomic_DNA. DR RefSeq; WP_003688278.1; NC_002946.2. DR RefSeq; YP_208087.1; NC_002946.2. DR ProteinModelPortal; Q5F812; -. DR SMR; Q5F812; 2-376. DR MEROPS; M20.010; -. DR EnsemblBacteria; AAW89675; AAW89675; NGO_0991. DR GeneID; 3281244; -. DR KEGG; ngo:NGO0991; -. DR PATRIC; 20335186; VBINeiGon24812_1161. DR HOGENOM; HOG000243770; -. DR KO; K01439; -. DR OMA; QNDPFDA; -. DR OrthoDB; EOG60651W; -. DR BioCyc; NGON242231:GI2G-918-MONOMER; -. DR UniPathway; UPA00034; UER00021. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW 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_0000375621. FT ACT_SITE 70 70 {ECO:0000255|HAMAP-Rule:MF_01690}. FT ACT_SITE 135 135 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 68 68 Cobalt or zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 101 101 Cobalt or zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 101 101 Cobalt or zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 136 136 Cobalt or zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 164 164 Cobalt or zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01690}. FT METAL 350 350 Cobalt or zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01690}. SQ SEQUENCE 381 AA; 41469 MW; 5B2F544275BE9C99 CRC64; MTETQSLELA KALISRPSVT PDDRDCQKLL AERLHKIGFA AEELHFGDTK NIWLRRGTKA PVVCFAGHTD VVPTGPVEKW DSPPFEPTER DGRLYGRGAA DMKTSIACFV TACERFVAEH PDHQGSIALL ITSDEEGDAL DGTTKVVDVL KARGELIDYC IVGEPTAVDK LGDMIKNGRR GSLSGSLTVK GKQGHIAYPH LAVNPIHTFA PALLELTQEI WDEGNEYFPP TSFQISNING GTGATNVIPG ELNVKFNFRF STESTETGLK QRVHAILDKH GVQYDLQWSC SGQPFLTHAG KLTDVARTAI AETCGVEAEL STTGGTSDGR FIKAIAKELI ELGPSNATIH QINENVRLDD IPKLSAVYER ILARLLAEKA V // ID DADA_NEIG1 Reviewed; 419 AA. AC Q5F5W1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1808; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and CC pyruvate from D-alanine: step 1/1. 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; AE004969; AAW90426.1; -; Genomic_DNA. DR RefSeq; WP_003690316.1; NC_002946.2. DR RefSeq; YP_208838.1; NC_002946.2. DR ProteinModelPortal; Q5F5W1; -. DR EnsemblBacteria; AAW90426; AAW90426; NGO_1808. DR GeneID; 3282307; -. DR KEGG; ngo:NGO1808; -. DR PATRIC; 20337268; VBINeiGon24812_2169. DR HOGENOM; HOG000217450; -. DR KO; K00285; -. DR OMA; NDLYPRG; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NGON242231:GI2G-1706-MONOMER; -. DR UniPathway; UPA00043; UER00498. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0055130; P:D-alanine catabolic process; IEA:UniProtKB-UniPathway. 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 1 419 D-amino acid dehydrogenase. FT /FTId=PRO_1000066100. FT NP_BIND 3 17 FAD. {ECO:0000255|HAMAP-Rule:MF_01202}. SQ SEQUENCE 419 AA; 46845 MW; F435775806AABDE3 CRC64; MKVLVLGAGV AGVSSVWYLA EAGHEVTVID RTEGVAMETS FANAGQLSYG YTTPWAAPGI PTKALKRLFK SHPPLLFRPD GGLYQIEWLW RMLQNCTATR YQINKERMVR ISEYSREMFR RFEAQTDMNF EGRKKGTLQI FRQTEEVEAA KQDIAVLERY GVPYRRLKPE ECAEFEPALA RVTAKIVGGL HLPADATGDC RLFTENLYKL CQEKGVRFYF NQTISRIDHN GLRIKAVETE TGRFETDAVV CALGCFSRTV LAQLDLNLPI YPVKGYSLTL PVTNSDGAPV STVLDESYKV AITRFDNRIR VGGMAELSGY ETKLPEKRRE TLALVVNDLF PEGGDLSQAL SWSGLRPMTP DSTPLIGRTR FENLFLNTGH GTLGWTMSPG SAKLTADIVS GKDTEIRSDD LSLSRYQKL // ID DCUP_NEIG1 Reviewed; 354 AA. AC Q5F9N1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO0362; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89106.1; -; Genomic_DNA. DR RefSeq; WP_003706638.1; NC_002946.2. DR RefSeq; YP_207518.1; NC_002946.2. DR ProteinModelPortal; Q5F9N1; -. DR EnsemblBacteria; AAW89106; AAW89106; NGO_0362. DR GeneID; 3283028; -. DR KEGG; ngo:NGO0362; -. DR PATRIC; 20333719; VBINeiGon24812_0437. DR HOGENOM; HOG000253896; -. DR KO; K01599; -. DR OMA; GSSKDFR; -. DR OrthoDB; EOG6VXF6H; -. DR BioCyc; NGON242231:GI2G-341-MONOMER; -. DR UniPathway; UPA00251; UER00321. DR Proteomes; UP000000535; 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_1000023927. FT REGION 27 31 Substrate binding. {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; 39017 MW; F3F56687A3D0BE67 CRC64; MTLLKNDTFL RALLKQPVEY TPIWMMRQAG RYLPEYKATR TKAGSFLDLC KNTGLATEVT IQPLERFDLD AAILFSDILT VPDAMGLGLY FAEGEGPKFK RALQHESDIA KLHVPDMEKL QYVFDAVTSI RKALDGRVPL IGFSGSPFTL ACYMVEGGGS KEFRTIKTMM YSRPDLLYKI LDTNAQAVTA YLNAQIDAGA QAVQIFDTWG GVLSDAAFKE FSLKYIRQIV AGLKRESEGR RVPVIVFAKG GGLWLESMAQ IGADALGLDW TCNIGEARRR VGNQVALQGN FDPSALFGTP ESIRTEVARI LTGYGHGSGH VFNLGHGINQ HADPEHAKIL VDTVHELSRQ YHGG // ID DDL_NEIG1 Reviewed; 304 AA. AC Q5F6M0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO1531; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90167.1; -; Genomic_DNA. DR RefSeq; WP_003689437.1; NC_002946.2. DR RefSeq; YP_208579.1; NC_002946.2. DR ProteinModelPortal; Q5F6M0; -. DR EnsemblBacteria; AAW90167; AAW90167; NGO_1531. DR GeneID; 3281512; -. DR KEGG; ngo:NGO1531; -. DR PATRIC; 20336558; VBINeiGon24812_1827. DR HOGENOM; HOG000011592; -. DR KO; K01921; -. DR OMA; NREIRFR; -. DR OrthoDB; EOG6ND0KB; -. DR BioCyc; NGON242231:GI2G-1433-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_1000030472. 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; 32678 MW; D80E1AADD9CEBBA3 CRC64; MQNFGKVAVL MGGFSSEREI SLDSGTAILN ALKSKGIDAY AFDPKETPLS ELKERGFQTA FNILHGTYGE DGAVQGALEL LGIPYTGSGV AASAIGMDKY RCKLIWQALG LPVPEFAVLY DDTDFDAVEE KLGLPMFVKP AAEGSSVGVV KVKEKGRLKS VYEELKHLQG EIIAERFIGG GEYSCPVLNG KGLPGIHIIP ATEFYDYEAK YNRDDTIYQC PSEDLTEAEE SLMRELAVRG AQAIGAEGCV RVDFLKDTDG KLYLLEINTL PGMTGHSLVP KSAAVTGVGF ADLCIEILKA AHVG // ID DER_NEIG1 Reviewed; 485 AA. AC O87407; Q5F9H0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 20-JAN-2016, entry version 103. DE RecName: Full=GTPase Der; DE AltName: Full=GTP-binding protein EngA; GN Name=der; Synonyms=engA; OrderedLocusNames=NGO0424; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RX PubMed=10655208; RA Mehr I.J., Long C.D., Serkin C.D., Seifert H.S.; RT "A homologue of the recombination-dependent growth gene, rdgC, is RT involved in gonococcal pilin antigenic variation."; RL Genetics 154:523-532(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis. {ECO:0000250}. CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Essential. {ECO:0000269|PubMed:10655208}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngA (Der) GTPase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 EngA-type G (guanine nucleotide-binding) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH-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; AF058711; AAC63508.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89167.1; -; Genomic_DNA. DR RefSeq; WP_010951041.1; NC_002946.2. DR RefSeq; YP_207579.1; NC_002946.2. DR ProteinModelPortal; O87407; -. DR EnsemblBacteria; AAW89167; AAW89167; NGO_0424. DR GeneID; 3282582; -. DR KEGG; ngo:NGO0424; -. DR PATRIC; 20333861; VBINeiGon24812_0508. DR HOGENOM; HOG000242862; -. DR KO; K03977; -. DR OMA; DVMGTPI; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; NGON242231:GI2G-402-MONOMER; -. DR Proteomes; UP000000535; 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_0000179019. FT DOMAIN 3 167 EngA-type G 1. FT DOMAIN 176 349 EngA-type G 2. FT DOMAIN 350 434 KH-like. FT NP_BIND 9 16 GTP 1. {ECO:0000255}. FT NP_BIND 56 60 GTP 1. {ECO:0000255}. FT NP_BIND 119 122 GTP 1. {ECO:0000255}. FT NP_BIND 182 189 GTP 2. {ECO:0000255}. FT NP_BIND 229 233 GTP 2. {ECO:0000255}. FT NP_BIND 294 297 GTP 2. {ECO:0000255}. SQ SEQUENCE 485 AA; 54028 MW; 19161A08B63857FC CRC64; MKPTIALIGR PNVGKSTLFN RLTRTKDALV HDLPGLTRDR HYGHGKVGSK PYFVIDTGGF EPVVDSGILH EMAKQTLQAV DEADAVVFLV DGRTGLTPQD KIIADRLRQS PRPVYLAVNK GEGGDRAVLA AEFYELALGE PHVISGAHGD GVYYLIEEIL ENFPEPEAEE ADAKHPVFAV IGRPNVGKST LVNAILGEKR VIAFDMAGTT RDSIHIDFER EGKPFTIIDT AGVRRRGKVD EAVEKFSVIK AMQAVEAANV AVLVLDAQQD IADQDATIAG FALEAGRALV VAVNKWDGIS EERREQVKRD ISRKLYFLDF AKFHFISALK ERGIDGLFES IQAAYNAAMI KMPTPKITRV LQTAVERQQP PRAGLVRPKM RYAHQGGMNP PVIVVHGNSL HAISDSYTRY LTQTFRKAFN LQGTPLRIQY NVSENPYENA EDKPKKKPLR RVSLSNRIEK REGRKEEKNR FKKKTKVSVK KQFSK // ID DCD_NEIG1 Reviewed; 188 AA. AC Q5F9H3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. 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=NGO0421; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89164.1; -; Genomic_DNA. DR RefSeq; WP_003687863.1; NC_002946.2. DR RefSeq; YP_207576.1; NC_002946.2. DR ProteinModelPortal; Q5F9H3; -. DR EnsemblBacteria; AAW89164; AAW89164; NGO_0421. DR GeneID; 3282995; -. DR KEGG; ngo:NGO0421; -. DR PATRIC; 20333855; VBINeiGon24812_0505. DR HOGENOM; HOG000228600; -. DR KO; K01494; -. DR OMA; MEYFRIP; -. DR OrthoDB; EOG67DPKR; -. DR BioCyc; NGON242231:GI2G-399-MONOMER; -. DR UniPathway; UPA00610; UER00665. DR Proteomes; UP000000535; 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_1000009767. SQ SEQUENCE 188 AA; 21281 MW; 7D5FFADBB092BC5A CRC64; MSIKSDKWIR RMSEEFGMID PFEPNQIKEA DGQRIISYGT SSYGYDIRCA NEFKIFTNIN STIVDPKNFD PKNFVTVEDD CCIIPPNSFA LARTVEYFRI PRNVLTVCLG KSTYARCGII VNVTPFEPEW EGYVTLEFSN TTPLPAKIYA GEGVAQVLFF ESDEVCETSY KDRNGKYMGQ TGVTLPKA // ID DEF_NEIG1 Reviewed; 167 AA. AC Q5F5P6; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1871; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90491.1; -; Genomic_DNA. DR RefSeq; WP_003690288.1; NC_002946.2. DR RefSeq; YP_208903.1; NC_002946.2. DR ProteinModelPortal; Q5F5P6; -. DR SMR; Q5F5P6; 2-165. DR EnsemblBacteria; AAW90491; AAW90491; NGO_1871. DR GeneID; 3282344; -. DR KEGG; ngo:NGO1871; -. DR PATRIC; 20337436; VBINeiGon24812_2249. DR HOGENOM; HOG000243509; -. DR KO; K01462; -. DR OMA; FDTMYEE; -. DR OrthoDB; EOG664CMF; -. DR BioCyc; NGON242231:GI2G-1775-MONOMER; -. DR Proteomes; UP000000535; 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_0000301066. 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; 19071 MW; 9BB11DB3BAC71BD3 CRC64; MALLNILQYP DERLHTVAKP VEQVDERIRK LVADMFETMY ESRGIGLAAT QVDVHERVVV MDLTEDRSEP RVFINPVIVE KDGETTYEEG CLSVPGIYDA VTRAERVKVE ALNEKGEKFT LEADGLLAIC VQHELDHLMG IVFVERLSQL KQGRIKTKLK KRQKHTI // ID DNAA_NEIG1 Reviewed; 518 AA. AC Q5FAJ2; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377}; GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; GN OrderedLocusNames=NGO0001; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP- CC Rule:MF_00377}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88774.1; -; Genomic_DNA. DR RefSeq; WP_003687194.1; NC_002946.2. DR RefSeq; YP_207186.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ2; -. DR EnsemblBacteria; AAW88774; AAW88774; NGO_0001. DR GeneID; 3283049; -. DR KEGG; ngo:NGO0001; -. DR PATRIC; 20332830; VBINeiGon24812_0001. DR HOGENOM; HOG000235659; -. DR KO; K02313; -. DR OMA; AVGNSIM; -. DR OrthoDB; EOG689HR1; -. DR BioCyc; NGON242231:GI2G-1-MONOMER; -. DR Proteomes; UP000000535; 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_0000114219. FT NP_BIND 222 229 ATP. {ECO:0000255|HAMAP-Rule:MF_00377}. SQ SEQUENCE 518 AA; 58057 MW; 3D55B19A2E4EE565 CRC64; MTLAEFWPLC LRRLHDMLPH GQFAQWIAPL TVGEEGGVWV VYGKNQFACN MLKSQFAGKI EAVREELAAG RPAFVFKPGE GVRYEMAAVE GAVEPAEPSL HAGSEEMPVQ EVLLDELPSE KPVKPAASKT AADILAERMK NLPHEPRQAA GPASRPESAA VAKARTDAQR DAEEARYEQT NLSPDYTFDT LVEGKGNRLA AAAAQAIAEN 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 DNAK_NEIG1 Reviewed; 642 AA. AC Q5F6W5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332}; DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332}; DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332}; DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332}; GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; GN OrderedLocusNames=NGO1429; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}. CC -!- INDUCTION: By stress conditions e.g. heat shock. CC {ECO:0000255|HAMAP-Rule:MF_00332}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000255|HAMAP-Rule:MF_00332}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90072.1; -; Genomic_DNA. DR RefSeq; WP_003689283.1; NC_002946.2. DR RefSeq; YP_208484.1; NC_002946.2. DR ProteinModelPortal; Q5F6W5; -. DR SMR; Q5F6W5; 1-606. DR PRIDE; Q5F6W5; -. DR EnsemblBacteria; AAW90072; AAW90072; NGO_1429. DR GeneID; 3281746; -. DR KEGG; ngo:NGO1429; -. DR PATRIC; 20336277; VBINeiGon24812_1687. DR HOGENOM; HOG000228136; -. DR KO; K04043; -. DR OMA; EKMAPPQ; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; NGON242231:GI2G-1337-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Stress response. FT CHAIN 1 642 Chaperone protein DnaK. FT /FTId=PRO_0000225984. FT MOD_RES 200 200 Phosphothreonine; by autocatalysis. FT {ECO:0000255|HAMAP-Rule:MF_00332}. SQ SEQUENCE 642 AA; 68863 MW; 6BC051EC0E5334CB CRC64; MAKVIGIDLG TTNSCLAISE NGQTKVIENA EGARTTPSII AYLDGGEILV GAPAKRQAVT NAKNTIYAAK RLIGHKFEDK EVQRDIESMP FEIIKADNGD AWVKAQGKEL SPPQISAEVL RKMKEAAEAY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG MDKGDNKDRK IAVYDLGGGT FDISIIEIAN LDGDKQFEVL ATNGDTFLGG EDFDQRLIDY IIDEFKKEQG IDLKQDVMAL QRLKEAAEKA KIELSSGQQT EINLPYITMD ATGPKHLAMK ITRAKFESLV EDLIARSIEP CRTALKDAGL STGDIDDVIL VGGQSRMPKV QEAVKDFFGK EPRKDVNPDE AVAVGAAIQG EVLSGGRSDV LLLDVTPLSL GIETMGGVMT KLIQKNTTIP TKASQVFSTA EDNQSAVTIH VLQGERERAS ANKSLGQFNL GDIAPAPRGM PQIEVTFDID ANGILHVSAK DKGTGKAANI TIQGSSGLSE EEIERMVKDA EANAEEDKKL TELVASRNQA EALIHSVKKS LADYGDKLDA AEKEKIEAAL KEAEEAVKGD DKTAIDAKAE ALGTASQKLG EMVYAQAQAE AQAGEGAQAN ASAKKDDDVV DADFEEVKDD KK // ID DNAJ_NEIG1 Reviewed; 373 AA. AC Q5F5M1; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=NGO1901; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90516.1; -; Genomic_DNA. DR RefSeq; WP_010951367.1; NC_002946.2. DR RefSeq; YP_208928.1; NC_002946.2. DR ProteinModelPortal; Q5F5M1; -. DR SMR; Q5F5M1; 2-78, 134-208. DR EnsemblBacteria; AAW90516; AAW90516; NGO_1901. DR GeneID; 3282302; -. DR KEGG; ngo:NGO1901; -. DR PATRIC; 20337506; VBINeiGon24812_2284. DR HOGENOM; HOG000226717; -. DR KO; K03686; -. DR OMA; IKDPCNS; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; NGON242231:GI2G-1800-MONOMER; -. DR Proteomes; UP000000535; 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_0000070838. 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 78 117 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; 40602 MW; BB8B6BD02D9FE318 CRC64; MSNQDFYATL GVARAATDDE IKKAYRKLAM KYHPDRNPDN KEAEEKFKEV QKAYETLSDK EKRAMYDQYG HAAFEGGGQG GFGGFGGFGG AQGFDFGDIF SQMFGGGSGR AQPDYQGEDV QVGIEITLEE AAKGVKKRIN IPTYEACDVC NGSGAKPGAS PETCPTCKGS GTVHIQQAIF RMQQTCPTCR GAGKHIKEPC VKCRGVGRNK AVKTVEVNIP AGIDDGQRIR LSGEGGPGMH GAPAGDLYVT VRIRAHKIFQ RDGLDLHCEL PISFAMAALG GELEVPTLDG KVKLTVPKET QTGRRMRVKG KGVKSLRSSA TGDLYCHIVV ETPVNLTDRQ KELLEEFERI STGLENQTPR KKSFLDKLRD LFD // ID DPO4_NEIG1 Reviewed; 352 AA. AC Q5F8N2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO0738; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89455.1; -; Genomic_DNA. DR RefSeq; WP_003695315.1; NC_002946.2. DR RefSeq; YP_207867.1; NC_002946.2. DR ProteinModelPortal; Q5F8N2; -. DR EnsemblBacteria; AAW89455; AAW89455; NGO_0738. DR GeneID; 3281904; -. DR KEGG; ngo:NGO0738; -. DR PATRIC; 20334614; VBINeiGon24812_0879. DR HOGENOM; HOG000082707; -. DR KO; K02346; -. DR OMA; WIAQEIR; -. DR OrthoDB; EOG6FZ4D8; -. DR BioCyc; NGON242231:GI2G-695-MONOMER; -. DR Proteomes; UP000000535; 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; IPR001126; UmuC. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 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 1 352 DNA polymerase IV. FT /FTId=PRO_1000084903. 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 352 AA; 39538 MW; 0B5BDD2E883543E7 CRC64; MSLRKIIHID MDAFYASVEL REQPHLKGRP VVVAWEGARS VICAASYEAR QFGLHSAMSV ATVKRLCPQA VYVPPHFDLY RQVSAQIHAV FRRYTDLIEP LSLDEAYLDV TRNFKNIPYA GEVAKEIRAA IFAETGLTAS AGIAPNKFLA KIASDWRKPN GQFVLPPHKV MAFLETLPLG KIPGAGKVTL KKMQSLGMRT AGDLRRFERG ELLNHFGRYG YRLYDLARGT DEHPVKAERE RLQISTEITL PEDLPLGQAA GHLPHLAEDL WRQITRKNVE AQSVTLKLKT YDFRIITRTL TYSSVLPDCA ALLQAAQMLM ARVPPQTEDA FRLIGIGVGR LVPKNQQQDL WA // ID DNLJ_NEIG1 Reviewed; 823 AA. AC Q5F9Z9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. 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=NGO0235; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88988.1; -; Genomic_DNA. DR RefSeq; WP_010951014.1; NC_002946.2. DR RefSeq; YP_207400.1; NC_002946.2. DR ProteinModelPortal; Q5F9Z9; -. DR SMR; Q5F9Z9; 5-327. DR EnsemblBacteria; AAW88988; AAW88988; NGO_0235. DR GeneID; 3281488; -. DR KEGG; ngo:NGO0235; -. DR PATRIC; 20333419; VBINeiGon24812_0291. DR HOGENOM; HOG000218459; -. DR KO; K01972; -. DR OMA; IEIHETV; -. DR OrthoDB; EOG6TTVM9; -. DR BioCyc; NGON242231:GI2G-219-MONOMER; -. DR Proteomes; UP000000535; 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 1 823 DNA ligase. FT /FTId=PRO_0000313330. FT DOMAIN 746 823 BRCT. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 32 36 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT NP_BIND 81 82 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT ACT_SITE 123 123 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 449 449 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 452 452 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 467 467 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT METAL 473 473 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 121 121 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 144 144 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 181 181 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 299 299 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. FT BINDING 323 323 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}. SQ SEQUENCE 823 AA; 90204 MW; 17FB1EA154269C85 CRC64; MNPTAQRIHE LTDLLNRYAY EYYTLDAPSI PDAEYDRLFR ELEALERNHP ELKLPDSPTQ RVGGEPLAGF AEVRHEVPML SLTNAFSPQD ENGVFDHAEM YAFDQRVRDG LDGGNPEYVI EPKFDGLAIS LLYRDGVLVQ AATRGDGTTG EDVTRNVKTV SNIPLRLHGE NVPELIEVRG EVLMLKADFA ALNQRQTENG QKPFANPRNA AAGSLRQLDS RITAQRKLHF FPYSVARQQG GLIAEEHIQE LAYFQALGFS LPNGNFGCFK NIGEVLAFYE HMQQKRPELP YEIDGTVVKV NSLAQQHELG FISRAPRWAV AHKFPAEEAL TIVEAIDVQI GRTGAVTPVA RLQPVFVGGV TVTNATLHNQ DEVSRKDVRV GDTVVVRRAG DVIPEVVRVI FERRPMQETA VAVSDGIGHQ QDDLFAETPS AKQTESVPLH KPYRLPARCP ICRSEIEREE GEAVARCSGG MLCQAQRAQG LIHFASRKAM DIDGLGEKQI EQLVAQDLVR HFADLYRIDI PTLQKMKETA DKGSSENENG DAETVSGDLS KYNTQNGKKQ PTKWAQNILA GIESGKTPEL ARFLFALGIR HVGERTAKTL AQAFGTLERV RRAPEPVLAC LPDIGTVVAR SIAHFFAQAE QQAMIDELLA AGVAPQAQAV SLPAAQYAGP QRWITRLPGF KISENKAQAL WELAGQSIEG LQNDKALPAD WQAWRSKAQN TALLENLKTF FAQMPSEDEA AQGSDGINKA VAGKTFVLTG TLPTFKRDQA QALIEAAGGK VSGSVSKKTD YVVAGETAGS KLEKANALGV SVLSEAELLT LLC // ID DTD_NEIG1 Reviewed; 163 AA. AC Q5F6A6; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO1654; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90281.1; -; Genomic_DNA. DR RefSeq; WP_003689787.1; NC_002946.2. DR RefSeq; YP_208693.1; NC_002946.2. DR ProteinModelPortal; Q5F6A6; -. DR EnsemblBacteria; AAW90281; AAW90281; NGO_1654. DR GeneID; 3281339; -. DR KEGG; ngo:NGO1654; -. DR PATRIC; 20336854; VBINeiGon24812_1972. DR HOGENOM; HOG000113982; -. DR KO; K07560; -. DR OMA; VFGADMK; -. DR OrthoDB; EOG6C2WM2; -. DR BioCyc; NGON242231:GI2G-1550-MONOMER; -. DR Proteomes; UP000000535; 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_0000164563. FT ACT_SITE 84 84 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00518}. SQ SEQUENCE 163 AA; 17667 MW; 6D06C989927A130F CRC64; MRAVIQKTVG AKVDVVSEAG TETCGKIDGG FVVLLGVTHS DTEKDARYIA DKIAHLRVFE DEAGKLNLSL KDVGGAVLLV SQFTLYADAA SGRRPSFSQA APAEQAQRLY LRTAELLRGH GIHVETGRFR THMQVSLCND GPVTILLDSF MTRISPKMKV VPD // ID DSBB_NEIG1 Reviewed; 162 AA. AC Q5F791; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO1292; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89946.1; -; Genomic_DNA. DR RefSeq; WP_010951234.1; NC_002946.2. DR RefSeq; YP_208358.1; NC_002946.2. DR ProteinModelPortal; Q5F791; -. DR EnsemblBacteria; AAW89946; AAW89946; NGO_1292. DR GeneID; 3282107; -. DR KEGG; ngo:NGO1292; -. DR PATRIC; 20335927; VBINeiGon24812_1518. DR HOGENOM; HOG000027866; -. DR KO; K03611; -. DR OMA; PLFDWFE; -. DR OrthoDB; EOG615VM4; -. DR BioCyc; NGON242231:GI2G-1204-MONOMER; -. DR Proteomes; UP000000535; 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_0000298371. 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; 17338 MW; 81BB104A3121ED43 CRC64; MTPLFRKAVW LLFAVSVCAF AGSLAAQYVL GMEPCVLCIS QRLCVLATAL CAAVVLACKP KGRVGGLSGA VFISIPAVTG ISVAAYQLWL QSLPPGAAPS CGAPWTFRLK GWPLFDWFEP VVRGFGNCAE PDYLLGVALP VWSAAYFLAV VLTVWWAWAR AK // ID EFP_NEIG1 Reviewed; 186 AA. AC Q5F856; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. 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=NGO0936; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89631.1; -; Genomic_DNA. DR RefSeq; WP_002219406.1; NC_002946.2. DR RefSeq; YP_208043.1; NC_002946.2. DR ProteinModelPortal; Q5F856; -. DR EnsemblBacteria; AAW89631; AAW89631; NGO_0936. DR GeneID; 23783072; -. DR GeneID; 3281711; -. DR KEGG; ngo:NGO0936; -. DR PATRIC; 20335057; VBINeiGon24812_1098. DR HOGENOM; HOG000010047; -. DR KO; K02356; -. DR OMA; DRRDYQY; -. DR OrthoDB; EOG6JQH6Q; -. DR BioCyc; NGON242231:GI2G-873-MONOMER; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000000535; 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_0000094293. 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 DXR_NEIG1 Reviewed; 394 AA. AC Q5F5X0; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1799; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90417.1; -; Genomic_DNA. DR RefSeq; WP_010951350.1; NC_002946.2. DR RefSeq; YP_208829.1; NC_002946.2. DR ProteinModelPortal; Q5F5X0; -. DR SMR; Q5F5X0; 4-393. DR EnsemblBacteria; AAW90417; AAW90417; NGO_1799. DR GeneID; 3282430; -. DR KEGG; ngo:NGO1799; -. DR PATRIC; 20337248; VBINeiGon24812_2159. DR HOGENOM; HOG000007221; -. DR KO; K00099; -. DR OMA; GFCPLSE; -. DR OrthoDB; EOG6R2H04; -. DR BioCyc; NGON242231:GI2G-1697-MONOMER; -. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000000535; 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 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_0000163681. 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; 42023 MW; 096A4A10FD3F5D92 CRC64; MTPQVLTILG STGSIGESTL DVVSRHPEKF RVFALAGHKQ VEKLAAQCQT FRPEYAVVAD AEHAARLEAL LKRDGTATQV LHGAQALVDV ASADEVSGVM CAIVGAAGLP SALAAAQKGK TIYLANKETL VVSGALFMET ARANGAAVLP VDSEHNAIFQ VLPRDYTDRL NEHGIDSIIL TASGGPFLTT DLSTFDSITP EQAVKHPNWR MGRKISVDSA TMANKGLELI EAHWLFNCPP DKLEVVIHPQ SVIHSMVRYR DGSVLAQLGN PDMRTPIAYC LGLPERIDSG VGKLDFGALS ALTFQKPDFG RFPCLKFAYE TINAGGAAPC VLNAANETAV AAFLDGQIKF TDIAKTVAHC LAQDFSNGMG DIEGLLAQDA RTRAQARAFI GTLR // ID DXS_NEIG1 Reviewed; 637 AA. AC Q5FAI2; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. 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=NGO0036; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88805.1; -; Genomic_DNA. DR RefSeq; WP_003696634.1; NC_002946.2. DR RefSeq; YP_207217.1; NC_002946.2. DR ProteinModelPortal; Q5FAI2; -. DR SMR; Q5FAI2; 1-630. DR EnsemblBacteria; AAW88805; AAW88805; NGO_0036. DR GeneID; 3281875; -. DR KEGG; ngo:NGO0036; -. DR PATRIC; 20332902; VBINeiGon24812_0036. DR HOGENOM; HOG000012988; -. DR KO; K01662; -. DR OMA; HAVGPFD; -. DR OrthoDB; EOG6BKJ6P; -. DR BioCyc; NGON242231:GI2G-33-MONOMER; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000000535; 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_0000256442. 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; 68812 MW; 6EFC18E52C5ECD71 CRC64; MNPSPLLHLI DSPQDLRRLD KKQLPRLAGE LRAFLLESVG QTGGHFASNL GAVELTIALH YVYDTPEDKL VWDVGHQSYP HKILTGRKNQ MHTMRQYGGL AGFPKRCESE YDAFGVGHSS TSIGAALGMA AADKLLGGDR RSVAIIGDGA MTAGQAFEAL NCAGDMDVDL LVVLNDNEMS ISPNVGALPK YLASNVVRDM HGLLSTVKAQ TGKVLDKIPG AMEFAQKVEH KIKTLAEEAE HAKQSLSLFE NFGFRYTGPV DGHNVENLVD VLKDLRSRKG PQLLHVITKK GNGYKLAEND PVKYHAVANL PKEGGAQMPS EKEPKPAAKP TYTQVFGKWL CDRAAADSRL VAITPAMREG SGLVEFEQRF PDRYFDVGIA EQHAVTFAGG LACEGMKPVV AIYSTFLQRA YDQLVHDIAL QNLPVLFAVD RAGIVGADGP THAGLYDLSF LRCVPNMIVA APSDENECRL LLSTCYQADA PAAVRYPRGT GTGAPVSDGM ETVEIGKGII RREGEKTAFI AFGSMVATAL AVAEKLNATV ADMRFVKPID EELIVRLARS HDRIVTLEEN AEQGGAGGAV LEVLAKHGIC KPVLLLGVAD TVTEHGDPKK LLDDLGLSAE AVERRVREWL PDRDAAN // ID EFTS_NEIG1 Reviewed; 284 AA. AC Q5F5F4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-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=NGO1974; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90583.1; -; Genomic_DNA. DR RefSeq; WP_003686860.1; NC_002946.2. DR RefSeq; YP_208995.1; NC_002946.2. DR ProteinModelPortal; Q5F5F4; -. DR SMR; Q5F5F4; 2-283. DR PRIDE; Q5F5F4; -. DR EnsemblBacteria; AAW90583; AAW90583; NGO_1974. DR GeneID; 3282649; -. DR KEGG; ngo:NGO1974; -. DR PATRIC; 20337713; VBINeiGon24812_2383. DR HOGENOM; HOG000220986; -. DR KO; K02357; -. DR OMA; FIMEPKK; -. DR OrthoDB; EOG66B42N; -. DR BioCyc; NGON242231:GI2G-1873-MONOMER; -. DR Proteomes; UP000000535; 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_0000241497. FT REGION 80 83 Involved in Mg(2+) ion dislocation from FT EF-Tu. {ECO:0000255|HAMAP-Rule:MF_00050}. SQ SEQUENCE 284 AA; 30359 MW; 29501A19F66D0227 CRC64; MAEITAKMVA DLRAATGLGM MECKKALVEA EGNFDKAEEI LRIKSGAKAG KLAGRTAAEG VLAYAINGNV GALVEVNCET DFVAKDAGFV EFANFVAKTA AEKKPASVEE LSELVESERK AIIAKLGENM SVRRFQVIDT ANQLVAYIHG ALATEGVLVE YKGSEDVARK IGMHIVAAKP QCVSEAEVDA ETVEKERHIY TEQAIASGKP ADIAAKMVEG RIRKFLAEIT LNGQAFVMNP DQTVAQFAKE NDTEVVSFIR YKVGDGIEKA VVDYAAEVAA AAKV // ID DUT_NEIG1 Reviewed; 150 AA. AC Q5F9E0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0459; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89197.1; -; Genomic_DNA. DR RefSeq; WP_010951049.1; NC_002946.2. DR RefSeq; YP_207609.1; NC_002946.2. DR ProteinModelPortal; Q5F9E0; -. DR SMR; Q5F9E0; 1-134. DR EnsemblBacteria; AAW89197; AAW89197; NGO_0459. DR GeneID; 3282986; -. DR KEGG; ngo:NGO0459; -. DR PATRIC; 20333952; VBINeiGon24812_0550. DR HOGENOM; HOG000028968; -. DR KO; K01520; -. DR OMA; MVSAWNR; -. DR OrthoDB; EOG689HXK; -. DR BioCyc; NGON242231:GI2G-435-MONOMER; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000535; 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_0000231413. 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; 16103 MW; FDCF309CC0012614 CRC64; MNIEVEMKVL DERMADFIPA YATEGSAGLD LRACLDEEVV LQPGETFLVP TGLAIYLANP AYAAVLLPRS GLGHKHGIVL GNLVGLIDSD YQGELKVSLW NRGSEPFAVK PFERIAQMVI VPVVQAGFKR VEEFVGSSRG EGGFGSTGSH // ID ENGB_NEIG1 Reviewed; 209 AA. AC Q5FAC6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 13-APR-2016, entry version 71. 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=NGO0100; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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=AAW88861.1; 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; AE004969; AAW88861.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003687358.1; NC_002946.2. DR RefSeq; YP_207273.2; NC_002946.2. DR ProteinModelPortal; Q5FAC6; -. DR EnsemblBacteria; AAW88861; AAW88861; NGO_0100. DR GeneID; 3282443; -. DR KEGG; ngo:NGO0100; -. DR PATRIC; 20333097; VBINeiGon24812_0132. DR HOGENOM; HOG000009832; -. DR KO; K03978; -. DR OrthoDB; EOG6ND0NG; -. DR BioCyc; NGON242231:GI2G-90-MONOMER; -. DR Proteomes; UP000000535; 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_0000266903. 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; 23600 MW; 79742D484A0A1ABF CRC64; MNLFQNAKFF TTVNHLKDLP DTPLEIAFVG RSNAGKSSAI NTLTNHVRLA YVSKTPGRTQ HINFFELQNG NFMVDLPGYG YAQVPEAVRA HWVNLLGDYL RHRKQLIGLV LIMDARHPLK ELDIRMLDFF HTTGRPVHIL LSKADKLSKN EQIKTLSQVK KLLKPYSDRQ NISVQLFSSL KKQGIDEANR TVGSWFDAAD AAASSPEEN // ID EFTU_NEIG1 Reviewed; 394 AA. AC Q5F5Q8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=NGO1842; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=NGO1858; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90463.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90479.1; -; Genomic_DNA. DR RefSeq; WP_003690212.1; NC_002946.2. DR RefSeq; YP_208875.1; NC_002946.2. DR RefSeq; YP_208891.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q8; -. DR SMR; Q5F5Q8; 2-394. DR PRIDE; Q5F5Q8; -. DR EnsemblBacteria; AAW90463; AAW90463; NGO_1842. DR EnsemblBacteria; AAW90479; AAW90479; NGO_1858. DR GeneID; 3282353; -. DR GeneID; 3282355; -. DR KEGG; ngo:NGO1842; -. DR KEGG; ngo:NGO1858; -. DR PATRIC; 20337358; VBINeiGon24812_2214. DR HOGENOM; HOG000229290; -. DR KO; K02358; -. DR OMA; GMVICKP; -. DR OrthoDB; EOG6R5C6X; -. DR BioCyc; NGON242231:GI2G-1743-MONOMER; -. DR BioCyc; NGON242231:GI2G-1760-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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_0000337440. 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}. SQ SEQUENCE 394 AA; 42938 MW; 0C57A62C3A6B5854 CRC64; MAKEKFERSK PHVNVGTIGH VDHGKTTLTA ALTTILAKKF GGAAKAYDQI DNAPEEKARG ITINTSHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLARQVGVPY IIVFMNKCDM VDDAELLELV EMEIRDLLSS YDFPGDDCPI VQGSALKALE GDAAYEEKIF ELATALDSYI PTPERAVDKP FLLPIEDVFS ISGRGTVVTG RVERGIIHVG DEIEIVGLKE TQKTTCTGVE MFRKLLDEGQ AGDNVGVLLR GTKREDVERG QVLAKPGTIT PHTKFKAEVY VLSKEEGGRH TPFFANYRPQ FYFRTTDVTG AVTLEKGVEM VMPGENVTIT VELIAPIAME EGLRFAIREG GRTVGAGVVS SVIA // ID EFG_NEIG1 Reviewed; 701 AA. AC Q5F5S3; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1843; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90464.1; -; Genomic_DNA. DR RefSeq; WP_003690097.1; NC_002946.2. DR RefSeq; YP_208876.1; NC_002946.2. DR ProteinModelPortal; Q5F5S3; -. DR PRIDE; Q5F5S3; -. DR EnsemblBacteria; AAW90464; AAW90464; NGO_1843. DR GeneID; 3282145; -. DR KEGG; ngo:NGO1843; -. DR PATRIC; 20337360; VBINeiGon24812_2215. DR HOGENOM; HOG000231585; -. DR KO; K02355; -. DR OMA; GDTFCDP; -. DR OrthoDB; EOG6X6RBF; -. DR BioCyc; NGON242231:GI2G-1744-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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_0000225220. 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; 77173 MW; 8F4667449376CED7 CRC64; MARKTPISLY RNIGISAHID AGKTTTTERI LFYTGLTHKL GEVHDGAATT DYMEQEQERG ITITSAAVTS YWSGMAKQFP EHRFNIIDTP GHVDFTVEVE RSMRVLDGAV MVYCAVGGVQ PQSETVWRQA NKYQVPRLAF VNKMDRQGAN FFRVVEQMKT RLRANPVPIV IPVGAEDSFT GVVDLLKMKS IIWNEADKGT TFTYGDIPAE LVETAEEWRQ NMIEAAAEAS EELMDKYLGG EDLAEEEIVG 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 ENO_NEIG1 Reviewed; 428 AA. AC Q5F8Z2; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. 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=NGO0617; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89345.1; -; Genomic_DNA. DR RefSeq; WP_003691316.1; NC_002946.2. DR RefSeq; YP_207757.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z2; -. DR SMR; Q5F8Z2; 2-426. DR PRIDE; Q5F8Z2; -. DR EnsemblBacteria; AAW89345; AAW89345; NGO_0617. DR GeneID; 3282141; -. DR KEGG; ngo:NGO0617; -. DR PATRIC; 20334318; VBINeiGon24812_0731. DR HOGENOM; HOG000072174; -. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR OrthoDB; EOG65J589; -. DR BioCyc; NGON242231:GI2G-585-MONOMER; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000000535; 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_0000133933. 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; 46112 MW; FE51A36498843F4B CRC64; MSAIVDIFAR EILDSRGNPT VECDVLLESG VMGRAAVPSG ASTGQKEALE LRDGDKSRYS GKGVLKAVEH VNNQIAQALI GIDANEQSYI DQIMIELDGT ENKGNLGANA TLAVSMAVAR AAAEDSGLPL YRYLGGAGPM SLPVPMMNVI NGGEHANNSL NIQEFMIMPV GAKSFREALR CGAEIFHALK KLCDSKGFPT TVGDEGGFAP NLNSHKEALQ LMVEAAEAAG YKAGEDVLFA LDCASSEFYK DGKYHLEAEG RSYTNAEFAE YLEGLVNEFP IISIEDGMDE NDWEGWKLLT EKLGKKVQLV GDDLFVTNPK ILAEGIEKGV ANALLVKVNQ IGTLSETLKA VDLAKCNRYA SVMSHRSGET EDSTIADLAV ATNCMQIKTG SLSRSDRMAK YNQLLRIEEE LAEAAYYPGK AAFYQLGK // ID ERPA_NEIG1 Reviewed; 112 AA. AC Q5F6W8; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO1426; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90069.1; -; Genomic_DNA. DR RefSeq; WP_002219692.1; NC_002946.2. DR RefSeq; YP_208481.1; NC_002946.2. DR ProteinModelPortal; Q5F6W8; -. DR SMR; Q5F6W8; 6-112. DR EnsemblBacteria; AAW90069; AAW90069; NGO_1426. DR GeneID; 3281776; -. DR KEGG; ngo:NGO1426; -. DR PATRIC; 20336271; VBINeiGon24812_1684. DR HOGENOM; HOG000228313; -. DR KO; K15724; -. DR OMA; FDENVND; -. DR OrthoDB; EOG6VXF8J; -. DR BioCyc; NGON242231:GI2G-1334-MONOMER; -. DR Proteomes; UP000000535; 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_0000311507. 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 EX7L_NEIG1 Reviewed; 451 AA. AC Q5F8V5; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0655; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89382.1; -; Genomic_DNA. DR RefSeq; WP_003688847.1; NC_002946.2. DR RefSeq; YP_207794.1; NC_002946.2. DR ProteinModelPortal; Q5F8V5; -. DR EnsemblBacteria; AAW89382; AAW89382; NGO_0655. DR GeneID; 3282507; -. DR KEGG; ngo:NGO0655; -. DR PATRIC; 20334400; VBINeiGon24812_0772. DR HOGENOM; HOG000229265; -. DR KO; K03601; -. DR OMA; PFMPKVI; -. DR OrthoDB; EOG64R65J; -. DR BioCyc; NGON242231:GI2G-622-MONOMER; -. DR Proteomes; UP000000535; 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_0000273671. SQ SEQUENCE 451 AA; 49798 MW; 4040CED8CE88A526 CRC64; MSDFFHSDVL SVSELNAFAK SILENHLAGL WIAGEVSNLT RAASGHYYFS LKDSRAQVRC AMFKGAAARL AQPLKEGDHI EVAGKISIYE ARGEFQITVN EVRLKGLGQL YEAYERLKAQ LQAEGAFAAE RKKPLPVRPQ CIGIVTSLAA AALRDVVTTL KRRAPEIPVI VYPAAVQGAG SGFQIAQAIK TASQRAECDV LIVCRGGGSI EDLRAFNEEP VVRAIEACTI PVVSGVGHET DFTLADFVAD VRAPTPTGAA ELVSPNRQES LHRLVQAQGR LKTVLEQRYF DASQKLDWLA RQIRHPRQKL DEQRASIGKL AQTLSYSMTQ NLRAHTARFE RQTQALQHCR PDVSVYRQDI VRLQTALPAA FSRLLARRRQ SLTAQAALLE AVSPQHILER GFSVVKNTRG QVIRNADVLK QGQKLHITFS DGETDVRVSK EQGQQDLFDC I // ID EX7S_NEIG1 Reviewed; 74 AA. AC Q5F632; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000255|HAMAP-Rule:MF_00337}; DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00337}; DE AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337}; DE Short=Exonuclease VII small subunit {ECO:0000255|HAMAP-Rule:MF_00337}; GN Name=xseB {ECO:0000255|HAMAP-Rule:MF_00337}; GN OrderedLocusNames=NGO1734; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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_00337}. 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_00337}. CC -!- SUBUNIT: Heterooligomer composed of large and small subunits. CC {ECO:0000255|HAMAP-Rule:MF_00337}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337}. CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000255|HAMAP- CC Rule:MF_00337}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90355.1; -; Genomic_DNA. DR RefSeq; WP_003689929.1; NC_002946.2. DR RefSeq; YP_208767.1; NC_002946.2. DR ProteinModelPortal; Q5F632; -. DR EnsemblBacteria; AAW90355; AAW90355; NGO_1734. DR GeneID; 3281259; -. DR KEGG; ngo:NGO1734; -. DR PATRIC; 20337066; VBINeiGon24812_2073. DR HOGENOM; HOG000228798; -. DR KO; K03602; -. DR OMA; ESIVLEM; -. DR OrthoDB; EOG69KV31; -. DR BioCyc; NGON242231:GI2G-1630-MONOMER; -. DR Proteomes; UP000000535; 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_0000206976. SQ SEQUENCE 74 AA; 8363 MW; 57EF38B47AAA198F CRC64; MKKNTPKSFE EALSRLESLT QSMQGEMPLE DALAAYQEGN ELVRYCQTKL AQVEQKLQVL DADGTKELNL ESDE // ID F16PA_NEIG1 Reviewed; 324 AA. AC Q5F8C3; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. 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=NGO0862; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89564.1; -; Genomic_DNA. DR RefSeq; WP_003691115.1; NC_002946.2. DR RefSeq; YP_207976.1; NC_002946.2. DR ProteinModelPortal; Q5F8C3; -. DR EnsemblBacteria; AAW89564; AAW89564; NGO_0862. DR GeneID; 3282373; -. DR KEGG; ngo:NGO0862; -. DR PATRIC; 20334894; VBINeiGon24812_1017. DR HOGENOM; HOG000191264; -. DR KO; K03841; -. DR OMA; YTTRYIG; -. DR OrthoDB; EOG6X10TR; -. DR BioCyc; NGON242231:GI2G-806-MONOMER; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000535; 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_0000364605. 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; 35474 MW; 013500A67852B411 CRC64; MDTLTRFLPE HLQQNQLPEA LGGVLLSVVS ACTEINAKVR LGALAGVLGM AGTGNIQGED QKKLDVIANN IMIDTLKANP AVAGLASEEE DTFVSAGENG RYLVLFDPLD GSSNIDVNIS VGTIFSILAK PEGALATESF LQTGRQQLAA GYVLYGPQTQ LVFTFGHGVY VFTLNAENEF VLTKENPKVP ESTKEFAINM SNRRHWLPPV QQYVDELLAG ETGTRGKNYN MRWVASMVAE IHRILMRGGV FMYLQDKRDP SKPGKLRLMY EANPMALILE QAGASASNAY QAMLDIQPES LHQRVAVIMG SSEEVDYLNR LHSK // ID FABH_NEIG1 Reviewed; 320 AA. AC Q5F4X5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO2168; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90762.1; -; Genomic_DNA. DR RefSeq; WP_003687179.1; NC_002946.2. DR RefSeq; YP_209174.1; NC_002946.2. DR ProteinModelPortal; Q5F4X5; -. DR SMR; Q5F4X5; 3-320. DR EnsemblBacteria; AAW90762; AAW90762; NGO_2168. DR GeneID; 3282756; -. DR KEGG; ngo:NGO2168; -. DR PATRIC; 20338192; VBINeiGon24812_2618. DR HOGENOM; HOG000246674; -. DR KO; K00648; -. DR OMA; ESGMYEN; -. DR OrthoDB; EOG6J74XN; -. DR BioCyc; NGON242231:GI2G-2056-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000535; 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_1000056381. 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; 34002 MW; 000E4939D5ECD119 CRC64; MQYAKISGTG SYLPANRVSN DDLAQKVDTS DEWITARTGI KFRHIAAENE KTSDLAAEAA RRALADAKLN INDIDLIIVA TATPDMQFPS TATIVQQKLG ITNGCPAFDV QAVCAGFMYA LTTANAYIKS GMAKNALVIG AETFSRIVDW NDRTTCVLFG DGAGAVVLSA SDKPGIIHSK LKADGNYLKL LNVPGQIACG KVSGSPYISM DGPGVFKFAV KMLSKIADDV IEEAGYTAEQ IDWIVPHQAN RRIIESTAKH LGLSMDKVVL TVQDHGNTSA ASIPLALDAG IRSGQIKRGQ NLLLEGIGGG FAWGAVLLQY // ID FETP_NEIG1 Reviewed; 88 AA. AC Q5F553; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE RecName: Full=Probable Fe(2+)-trafficking protein {ECO:0000255|HAMAP-Rule:MF_00686}; GN OrderedLocusNames=NGO2083; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90684.1; -; Genomic_DNA. DR RefSeq; WP_002214948.1; NC_002946.2. DR RefSeq; YP_209096.1; NC_002946.2. DR ProteinModelPortal; Q5F553; -. DR EnsemblBacteria; AAW90684; AAW90684; NGO_2083. DR GeneID; 3282834; -. DR KEGG; ngo:NGO2083; -. DR PATRIC; 20337999; VBINeiGon24812_2522. DR HOGENOM; HOG000137239; -. DR OMA; SKQTMLI; -. DR OrthoDB; EOG654P6H; -. DR BioCyc; NGON242231:GI2G-1978-MONOMER; -. DR Proteomes; UP000000535; 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_0000214491. SQ SEQUENCE 88 AA; 10180 MW; EBC6F2FBF097F2F1 CRC64; MARMVFCVKL NKEAEGMKFP PLPNELGKRI FENVSQEAWA AWTRHQTMLI NENRLSLADP RAREYLAQQM EQYFFGDGAD AVQGYVPQ // ID FITA_NEIG1 Reviewed; 78 AA. AC Q5F881; Q9RF92; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Antitoxin FitA; DE AltName: Full=Trafficking protein A; GN Name=fitA; Synonyms=vapB; OrderedLocusNames=NGO0908; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 700825 / FA 1090, and MS11A; RX PubMed=10639460; DOI=10.1128/IAI.68.2.896-905.2000; RA Hopper S., Wilbur J.S., Vasquez B.L., Larson J., Clary S., Mehr I.J., RA Seifert H.S., So M.; RT "Isolation of Neisseria gonorrhoeae mutants that show enhanced RT trafficking across polarized T84 epithelial monolayers."; RL Infect. Immun. 68:896-905(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP DNA-BINDING, SUBUNIT, AND MUTAGENESIS OF ARG-7. RC STRAIN=ATCC 700825 / FA 1090; RX PubMed=16156663; DOI=10.1021/bi0511080; RA Wilbur J.S., Chivers P.T., Mattison K., Potter L., Brennan R.G., RA So M.; RT "Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through RT its ribbon-helix-helix motif."; RL Biochemistry 44:12515-12524(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-78 IN COMPLEX WITH FITB RP BOUND TO DNA, SUBUNIT, AND DNA-BINDING. RC STRAIN=ATCC 700825 / FA 1090; RX PubMed=16982615; DOI=10.1074/jbc.M605198200; RA Mattison K., Wilbur J.S., So M., Brennan R.G.; RT "Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a RT tetramer of toxin-antitoxin heterodimers containing pin domains and RT ribbon-helix-helix motifs."; RL J. Biol. Chem. 281:37942-37951(2006). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Plays a role in the speed with which bacteria traverse human CC epithelial cells; disruption of the locus increases the speed of CC trafficking about 2-4-fold. Binds to its own promoter, binding CC affinity of the FitAB complex is 20-30-fold higher than FitA CC alone. No nuclease activity was observed for the FitAB complex, CC perhaps because FitA (the antitoxin) prevents metal binding and CC thus catalysis by FitB. {ECO:0000269|PubMed:10639460}. CC -!- SUBUNIT: Homodimer in the absence of FitB; forms a heterodimer CC with FitB; 4 FitAB heterodimers form a complex that binds to fitAB CC promoter DNA. The complex is also seen in solution. CC {ECO:0000269|PubMed:16156663, ECO:0000269|PubMed:16982615}. CC -!- DISRUPTION PHENOTYPE: Disruption of the fitAB operon leads to CC faster transepithelial cell trafficking of the bacterium; mutants CC adhere to and invade cells normally. Mutants grow normally in CC liquid culture but much faster within human cell lines A431 and CC T84; these latter 2 phenotypes were observed using MS11A bacteria CC with a disrupted fitAB locus. {ECO:0000269|PubMed:10639460}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF200716; AAF19188.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89606.1; -; Genomic_DNA. DR RefSeq; WP_003688410.1; NC_002946.2. DR RefSeq; YP_208018.1; NC_002946.2. DR PDB; 2BSQ; X-ray; 3.00 A; E/F/G/H=2-78. DR PDB; 2H1C; X-ray; 1.80 A; B=46-64. DR PDB; 2H1O; X-ray; 3.00 A; E/F/G/H=2-69. DR PDBsum; 2BSQ; -. DR PDBsum; 2H1C; -. DR PDBsum; 2H1O; -. DR ProteinModelPortal; Q5F881; -. DR SMR; Q5F881; 2-69. DR EnsemblBacteria; AAW89606; AAW89606; NGO_0908. DR GeneID; 3281660; -. DR KEGG; ngo:NGO0908; -. DR PATRIC; 20334997; VBINeiGon24812_1068. DR HOGENOM; HOG000142203; -. DR OMA; CIMPVIT; -. DR OrthoDB; EOG6HQSV9; -. DR BioCyc; NGON242231:GI2G-848-MONOMER; -. DR EvolutionaryTrace; Q5F881; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0044001; P:migration in host; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR SUPFAM; SSF47598; SSF47598; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 78 Antitoxin FitA. FT /FTId=PRO_0000408086. FT MUTAGEN 7 7 R->A: Loss of DNA-binding, still binds FT FitB. {ECO:0000269|PubMed:16156663}. FT STRAND 4 6 {ECO:0000244|PDB:2BSQ}. FT HELIX 11 23 {ECO:0000244|PDB:2BSQ}. FT HELIX 28 43 {ECO:0000244|PDB:2BSQ}. FT HELIX 48 59 {ECO:0000244|PDB:2H1C}. SQ SEQUENCE 78 AA; 8434 MW; 29CC28FF3DCD9C73 CRC64; MASVVIRNLS EATHNAIKFR ARAAGRSTEA EIRLILDNIA KAQQTVRLGS MLASIGQEIG GVELEDVRGR NTDNEVSL // ID FABZ_NEIG1 Reviewed; 149 AA. AC Q5F5W5; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO1804; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90422.1; -; Genomic_DNA. DR RefSeq; WP_002231544.1; NC_002946.2. DR RefSeq; YP_208834.1; NC_002946.2. DR ProteinModelPortal; Q5F5W5; -. DR EnsemblBacteria; AAW90422; AAW90422; NGO_1804. DR GeneID; 3282334; -. DR KEGG; ngo:NGO1804; -. DR PATRIC; 20337258; VBINeiGon24812_2164. DR HOGENOM; HOG000277829; -. DR KO; K02372; -. DR OMA; AMIKDKS; -. DR OrthoDB; EOG6JTCGM; -. DR BioCyc; NGON242231:GI2G-1702-MONOMER; -. DR Proteomes; UP000000535; 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_0000230818. FT ACT_SITE 53 53 {ECO:0000255|HAMAP-Rule:MF_00406}. SQ SEQUENCE 149 AA; 16613 MW; 939E7B544D56C10E CRC64; MDVQLPIEAK DIQKLIPHRY PFLQLDRITA FEPMKTLTAI KNVTINEPQF QGHFPDLPVM PGVLIIEAMA QACGTLAILS EGGRKENEFF FFAGIDEARF KRQVIPGDQL VFEVELLTSR RGIGKFNAVA KVDGQVAVEA VIMCAKRVV // ID FBPC_NEIG1 Reviewed; 352 AA. AC Q5FA19; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 86. 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=NGO0215; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88968.1; -; Genomic_DNA. DR RefSeq; WP_003687540.1; NC_002946.2. DR RefSeq; YP_207380.1; NC_002946.2. DR PDB; 3FVQ; X-ray; 1.90 A; A/B=1-352. DR PDBsum; 3FVQ; -. DR ProteinModelPortal; Q5FA19; -. DR EnsemblBacteria; AAW88968; AAW88968; NGO_0215. DR GeneID; 3281434; -. DR KEGG; ngo:NGO0215; -. DR PATRIC; 20333369; VBINeiGon24812_0267. DR KO; K02010; -. DR OMA; AINICID; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-198-MONOMER; -. DR EvolutionaryTrace; Q5FA19; -. DR Proteomes; UP000000535; 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; 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. DR PROSITE; PS51242; FBPC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Hydrolase; Ion transport; Iron; Iron transport; KW Membrane; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 352 Fe(3+) ions import ATP-binding protein FT FbpC. FT /FTId=PRO_0000272040. 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}. FT STRAND 5 14 {ECO:0000244|PDB:3FVQ}. FT STRAND 17 27 {ECO:0000244|PDB:3FVQ}. FT STRAND 32 38 {ECO:0000244|PDB:3FVQ}. FT HELIX 43 50 {ECO:0000244|PDB:3FVQ}. FT STRAND 57 63 {ECO:0000244|PDB:3FVQ}. FT STRAND 66 72 {ECO:0000244|PDB:3FVQ}. FT HELIX 77 79 {ECO:0000244|PDB:3FVQ}. FT STRAND 83 85 {ECO:0000244|PDB:3FVQ}. FT HELIX 97 102 {ECO:0000244|PDB:3FVQ}. FT HELIX 113 125 {ECO:0000244|PDB:3FVQ}. FT HELIX 129 131 {ECO:0000244|PDB:3FVQ}. FT HELIX 136 138 {ECO:0000244|PDB:3FVQ}. FT HELIX 141 153 {ECO:0000244|PDB:3FVQ}. FT STRAND 158 164 {ECO:0000244|PDB:3FVQ}. FT TURN 165 168 {ECO:0000244|PDB:3FVQ}. FT HELIX 171 187 {ECO:0000244|PDB:3FVQ}. FT STRAND 191 195 {ECO:0000244|PDB:3FVQ}. FT HELIX 199 205 {ECO:0000244|PDB:3FVQ}. FT STRAND 207 213 {ECO:0000244|PDB:3FVQ}. FT STRAND 216 221 {ECO:0000244|PDB:3FVQ}. FT HELIX 223 228 {ECO:0000244|PDB:3FVQ}. FT HELIX 233 239 {ECO:0000244|PDB:3FVQ}. FT STRAND 243 249 {ECO:0000244|PDB:3FVQ}. FT STRAND 251 257 {ECO:0000244|PDB:3FVQ}. FT STRAND 260 265 {ECO:0000244|PDB:3FVQ}. FT STRAND 273 278 {ECO:0000244|PDB:3FVQ}. FT HELIX 280 282 {ECO:0000244|PDB:3FVQ}. FT STRAND 283 287 {ECO:0000244|PDB:3FVQ}. FT STRAND 292 304 {ECO:0000244|PDB:3FVQ}. FT STRAND 306 315 {ECO:0000244|PDB:3FVQ}. FT STRAND 318 326 {ECO:0000244|PDB:3FVQ}. FT STRAND 335 340 {ECO:0000244|PDB:3FVQ}. FT STRAND 344 348 {ECO:0000244|PDB:3FVQ}. SQ SEQUENCE 352 AA; 37902 MW; 2EB9713C445BA3C0 CRC64; MTAALHIGHL SKSFQNTPVL NDISLSLDPG EILFIIGASG CGKTTLLRCL AGFEQPDSGE ISLSGKTIFS KNTNLPVRER RLGYLVQEGV LFPHLTVYRN IAYGLGNGKG RTAQERQRIE AMLELTGISE LAGRYPHELS GGQQQRVALA RALAPDPELI LLDEPFSALD EQLRRQIRED MIAALRANGK SAVFVSHDRE EALQYADRIA VMKQGRILQT ASPHELYRQP ADLDAALFIG EGIVFPAALN ADGTADCRLG RLPVQSGAPA GTRGTLLIRP EQFSLHPHSA PAASIHAVVL KTTPKARHTE ISLRAGQTVL TLNLPSAPTL SDGISAVLHL DGPALFFPGN TL // ID FMT_NEIG1 Reviewed; 308 AA. AC Q5F5P7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. 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=NGO1870; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90490.1; -; Genomic_DNA. DR RefSeq; WP_003697690.1; NC_002946.2. DR RefSeq; YP_208902.1; NC_002946.2. DR ProteinModelPortal; Q5F5P7; -. DR EnsemblBacteria; AAW90490; AAW90490; NGO_1870. DR GeneID; 3282345; -. DR KEGG; ngo:NGO1870; -. DR PATRIC; 20337434; VBINeiGon24812_2248. DR HOGENOM; HOG000261177; -. DR KO; K00604; -. DR OMA; GCINSHA; -. DR OrthoDB; EOG6B09WV; -. DR BioCyc; NGON242231:GI2G-1774-MONOMER; -. DR Proteomes; UP000000535; 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_0000083002. FT REGION 110 113 Tetrahydrofolate (THF) binding. FT {ECO:0000255|HAMAP-Rule:MF_00182}. SQ SEQUENCE 308 AA; 32827 MW; 0DDF7EC6EC4852B5 CRC64; MKVIFAGTPD FAAAALKAVA AAGFEIPLVL TQPDRPKGRG MQLTAPPVKQ AALELGLRVA QPEKLRNNAE ALQMLKEVEA DVMVVAAYGL ILPQEVLDTP KHGCLNIHAS LLPRWRGAAP IQRAIEAGDA ETGVCIMQMD IGLDTGDVVS EHRYAIQPTD TANEVHDALM EIGAAAVVAD LQQLQSKGRL NAVKQPEEGV TYAQKLSKEE ARIDWSESAD IIERKIRAFN PVPAAWVEYQ GKPMKIRRAE VVAQQGTAGE VLSCSADGLV VACGESALKI TELQPAGGRR MNIAAFAAGR SIEAGAKL // ID FITB_NEIG1 Reviewed; 139 AA. AC Q5F882; Q9RF91; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Toxin FitB; DE AltName: Full=Ribonuclease FitB; DE Short=RNase FitB; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Trafficking protein B; GN Name=fitB; Synonyms=vapC; OrderedLocusNames=NGO0907; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 700825 / FA 1090, and MS11A; RX PubMed=10639460; DOI=10.1128/IAI.68.2.896-905.2000; RA Hopper S., Wilbur J.S., Vasquez B.L., Larson J., Clary S., Mehr I.J., RA Seifert H.S., So M.; RT "Isolation of Neisseria gonorrhoeae mutants that show enhanced RT trafficking across polarized T84 epithelial monolayers."; RL Infect. Immun. 68:896-905(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP DNA-BINDING, AND SUBUNIT. RC STRAIN=ATCC 700825 / FA 1090; RX PubMed=16156663; DOI=10.1021/bi0511080; RA Wilbur J.S., Chivers P.T., Mattison K., Potter L., Brennan R.G., RA So M.; RT "Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through RT its ribbon-helix-helix motif."; RL Biochemistry 44:12515-12524(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-138 IN COMPLEX WITH FITA RP BOUND TO DNA, AND SUBUNIT. RC STRAIN=ATCC 700825 / FA 1090; RX PubMed=16982615; DOI=10.1074/jbc.M605198200; RA Mattison K., Wilbur J.S., So M., Brennan R.G.; RT "Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a RT tetramer of toxin-antitoxin heterodimers containing pin domains and RT ribbon-helix-helix motifs."; RL J. Biol. Chem. 281:37942-37951(2006). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Plays CC a role in the speed with which bacteria traverse human epithelial CC cells; disruption of the locus increases the speed of trafficking CC about 2-4-fold. FitAB binds to its own promoter better than FitA CC alone. The expected nuclease activity was not observed for the CC FitAB complex, perhaps because FitA (the antitoxin) prevents metal CC binding and thus catalysis by FitB. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SUBUNIT: Forms a heterodimer with FitA, 4 FitAB heterodimers form CC a complex that binds to promoter DNA. The complex is also seen in CC solution. This protein does not actually contact DNA. CC {ECO:0000269|PubMed:16156663, ECO:0000269|PubMed:16982615}. CC -!- DISRUPTION PHENOTYPE: Disruption of the fitAB locus leads to CC faster transepithelial cell trafficking of the bacterium; mutants CC adhere to and invade cells normally. Mutants grow normally in CC liquid culture but much faster within human cell lines A431 and CC T84; these latter 2 phenotypes were observed using MS11A bacteria CC with a disrupted fitAB locus. {ECO:0000269|PubMed:10639460}. CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF200716; AAF19189.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89605.1; -; Genomic_DNA. DR RefSeq; WP_003691083.1; NC_002946.2. DR RefSeq; YP_208017.1; NC_002946.2. DR PDB; 2BSQ; X-ray; 3.00 A; A/B/C/D=1-139. DR PDB; 2H1C; X-ray; 1.80 A; A=1-138. DR PDB; 2H1O; X-ray; 3.00 A; A/B/C/D=1-138. DR PDBsum; 2BSQ; -. DR PDBsum; 2H1C; -. DR PDBsum; 2H1O; -. DR ProteinModelPortal; Q5F882; -. DR SMR; Q5F882; 1-138. DR EnsemblBacteria; AAW89605; AAW89605; NGO_0907. DR GeneID; 3281212; -. DR KEGG; ngo:NGO0907; -. DR PATRIC; 20334995; VBINeiGon24812_1067. DR HOGENOM; HOG000121275; -. DR KO; K07062; -. DR OMA; NVISEPW; -. DR OrthoDB; EOG6CVVD1; -. DR BioCyc; NGON242231:GI2G-847-MONOMER; -. DR EvolutionaryTrace; Q5F882; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR GO; GO:0044001; P:migration in host; IMP:UniProtKB. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome; Toxin. FT CHAIN 1 139 Toxin FitB. FT /FTId=PRO_0000407900. FT DOMAIN 2 123 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 5 5 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 104 104 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT STRAND 2 4 {ECO:0000244|PDB:2H1C}. FT HELIX 6 9 {ECO:0000244|PDB:2H1C}. FT HELIX 11 13 {ECO:0000244|PDB:2H1C}. FT STRAND 14 16 {ECO:0000244|PDB:2H1C}. FT HELIX 19 27 {ECO:0000244|PDB:2H1C}. FT HELIX 30 32 {ECO:0000244|PDB:2H1C}. FT STRAND 33 36 {ECO:0000244|PDB:2H1C}. FT HELIX 37 48 {ECO:0000244|PDB:2H1C}. FT HELIX 53 65 {ECO:0000244|PDB:2H1C}. FT HELIX 68 71 {ECO:0000244|PDB:2H1C}. FT HELIX 80 94 {ECO:0000244|PDB:2H1C}. FT TURN 95 97 {ECO:0000244|PDB:2H1C}. FT HELIX 102 114 {ECO:0000244|PDB:2H1C}. FT STRAND 117 119 {ECO:0000244|PDB:2H1C}. FT HELIX 124 128 {ECO:0000244|PDB:2H1C}. SQ SEQUENCE 139 AA; 15307 MW; AE12B8DF0E8427F4 CRC64; MILLDTNVIS EPLRPQPNER VVAWLDSLIL EDVYLSAITV AELRLGVALL LNGKKKNVLH ERLEQSILPL FAGRILPFDE PVAAIYAQIR SYAKTHGKEI AAADGYIAAT AKQHSLTVAT RDTGSFFAAD VAVFNPWHD // ID FPG_NEIG1 Reviewed; 275 AA. AC Q5F8Z9; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 83. DE RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103}; DE Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103}; DE EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103}; DE Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103}; GN Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103}; GN Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103}; GN OrderedLocusNames=NGO0610; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_00103}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7- CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N- CC methyl)formamidopyrimidine. {ECO:0000255|HAMAP-Rule:MF_00103}. 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:0000255|HAMAP-Rule:MF_00103}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00103}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00103}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP- CC Rule:MF_00103}. CC -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000255|HAMAP- CC Rule:MF_00103}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89338.1; -; Genomic_DNA. DR RefSeq; WP_003688927.1; NC_002946.2. DR RefSeq; YP_207750.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z9; -. DR SMR; Q5F8Z9; 2-275. DR EnsemblBacteria; AAW89338; AAW89338; NGO_0610. DR GeneID; 3281724; -. DR KEGG; ngo:NGO0610; -. DR PATRIC; 20334300; VBINeiGon24812_0722. DR HOGENOM; HOG000020881; -. DR KO; K10563; -. DR OMA; CQKENYE; -. DR OrthoDB; EOG6QP131; -. DR BioCyc; NGON242231:GI2G-578-MONOMER; -. DR Proteomes; UP000000535; 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_0000228450. FT ZN_FING 241 275 FPG-type. {ECO:0000255|HAMAP- FT Rule:MF_00103}. FT ACT_SITE 2 2 Schiff-base intermediate with DNA. FT {ECO:0000255|HAMAP-Rule:MF_00103}. FT ACT_SITE 3 3 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00103}. FT ACT_SITE 58 58 Proton donor; for beta-elimination FT activity. {ECO:0000255|HAMAP- FT Rule:MF_00103}. FT ACT_SITE 265 265 Proton donor; for delta-elimination FT activity. {ECO:0000255|HAMAP- FT Rule:MF_00103}. FT BINDING 95 95 DNA. {ECO:0000255|HAMAP-Rule:MF_00103}. FT BINDING 114 114 DNA. {ECO:0000255|HAMAP-Rule:MF_00103}. SQ SEQUENCE 275 AA; 30856 MW; 687127ACD3A9EEA9 CRC64; MPELPEVETT LRGIAPHIEG KTVEAVILRQ LKLRWQINPD LGEILSGRQV LSCGRRAKYL IVRFQTGILL IHLGMSGSLR IFTPSDGRIG RPDRHDHVDI VFSDGTVMRY RDPRKFGAIL WYEGIEERHP LLEKLGPEPL SEAFCTDYLY AGLKAQKRAV KLALMDNTVV VGVGNIYANE SLFRAGISPH RPANRLKKKE CAVLVETVKA VLQRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC LRCGGLVVKE TLGQRGTFYC TNCQK // ID FOLD_NEIG1 Reviewed; 284 AA. AC Q5F5D0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO1999; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90607.1; -; Genomic_DNA. DR RefSeq; WP_003686899.1; NC_002946.2. DR RefSeq; YP_209019.1; NC_002946.2. DR ProteinModelPortal; Q5F5D0; -. DR SMR; Q5F5D0; 2-282. DR EnsemblBacteria; AAW90607; AAW90607; NGO_1999. DR GeneID; 3282625; -. DR KEGG; ngo:NGO1999; -. DR PATRIC; 20337767; VBINeiGon24812_2410. DR HOGENOM; HOG000218242; -. DR KO; K01491; -. DR OMA; AHERPGX; -. DR OrthoDB; EOG6K6VBB; -. DR BioCyc; NGON242231:GI2G-1897-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000535; 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_0000268414. 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; 30001 MW; 7898CC784E944ED7 CRC64; MSAQLINGKE VSQKHLQAIA EAVAQRQQDN LHTPCLAVVL VGGDPAGAVY VRNKKTACQK CGIKSLSYEL PESTSQEELL ALVDRLNADS EVDGILVQLP LPKHLDSQAI LERISPDKDV DGFHPYNVGR LAVKMPLMRP CTPKGVMTLL EAYGIDPKGK KAVVVGASNI VGRPQALELL LARATVTVCH SATENLADEV AAADILVVGV GIPNFVKGGW IKPGAVVIDV GINRLDDGSL CGDVEFETAK ERAAMITPVP GGVGPMTIAT LMENTLHAAS LHDA // ID G6PI1_NEIG1 Reviewed; 548 AA. AC Q5F8P8; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Glucose-6-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=GPI 1 {ECO:0000255|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphoglucose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PGI 1 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase 1 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PHI 1 {ECO:0000255|HAMAP-Rule:MF_00473}; GN Name=pgi1 {ECO:0000255|HAMAP-Rule:MF_00473}; GN OrderedLocusNames=NGO0719; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP- CC Rule:MF_00473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89439.1; -; Genomic_DNA. DR RefSeq; WP_003688725.1; NC_002946.2. DR RefSeq; YP_207851.1; NC_002946.2. DR ProteinModelPortal; Q5F8P8; -. DR SMR; Q5F8P8; 3-545. DR PRIDE; Q5F8P8; -. DR EnsemblBacteria; AAW89439; AAW89439; NGO_0719. DR GeneID; 3282106; -. DR KEGG; ngo:NGO0719; -. DR PATRIC; 20334568; VBINeiGon24812_0856. DR HOGENOM; HOG000261370; -. DR KO; K01810; -. DR OMA; CETQAML; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; NGON242231:GI2G-679-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000535; 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_0000180689. FT ACT_SITE 353 353 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00473}. FT ACT_SITE 384 384 {ECO:0000255|HAMAP-Rule:MF_00473}. FT ACT_SITE 512 512 {ECO:0000255|HAMAP-Rule:MF_00473}. SQ SEQUENCE 548 AA; 62117 MW; 704E606E2895007B CRC64; MKHLHDLPAW SKLWNHFDDS KTLHMREMFE QDPQRAERYW LQVGGLTLDY SKNRINDETM SLLFELAREA GVPERMRQMF HGEKINTTEN RAVLHVALRN RTNSPIMVDG EDVMPKVNRV LQRMGEFAHE VRSGSWLGYT NQVITDVVNI GIGGSDLGPL TMCTALKPFG HPRLNMHFVS NVDGSQLRDV LSKVHPETTL FIIASKTFTT QETLTNALTA REWFLNHAGD EEAVAKHFAA VSTNRKAVAE FGIDIANMFE FWDWVGGRYS LWSAIGLPIM LYLGEENFIE MLNGAHLMDQ HFINTPLERN LPVILALIGI WYINYYGGGS HVIAPYDQHL HRLPKFIQQL DMESNGKQVT LDGKAVGHET SPIIWGETGI NGQHAFFQLL HQGTHITPID LIASLEKRSN LPGHHEILLA NVFAQAEAFM CGKTPDEVRA ELKAQGMDEA RIEELVPHKT FSGNRPTNLI LMDKVNPRNM GSLIAMYEHK TFVQGIIWGI NSFDQWGVEL GKQLAKTILG ELTGETEPQK HDSSTERLIN LYLQTNRK // ID FTHS_NEIG1 Reviewed; 558 AA. AC Q5FAG1; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0062; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88826.1; -; Genomic_DNA. DR RefSeq; WP_003698015.1; NC_002946.2. DR RefSeq; YP_207238.1; NC_002946.2. DR ProteinModelPortal; Q5FAG1; -. DR SMR; Q5FAG1; 8-556. DR EnsemblBacteria; AAW88826; AAW88826; NGO_0062. DR GeneID; 3282323; -. DR KEGG; ngo:NGO0062; -. DR PATRIC; 20332976; VBINeiGon24812_0072. DR HOGENOM; HOG000040280; -. DR KO; K01938; -. DR OMA; CGEIMTM; -. DR OrthoDB; EOG6PCPSP; -. DR BioCyc; NGON242231:GI2G-55-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000535; 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_0000199363. FT NP_BIND 66 73 ATP. {ECO:0000255|HAMAP-Rule:MF_01543}. SQ SEQUENCE 558 AA; 59140 MW; 47D2FCC1282133B6 CRC64; MSFKTDAETA QSSTMRPIGE IAAKLGLNVD NIEPYGHYKA KINPAEAFKL PQKQGRLILV TAINPTPAGE GKTTVTIGLA DALRHIGKDS VIALREPSLG PVFGVKGGAA GGGYAQVLPM EDINLHFTGD FHAIGAANNL LAAMLDNHIY QGNELNIDPK RVLWRRVVDM NDRQLRNIID GMGKPVDGVM RPDGFDITVA SEVMAVFCLA KDISDLKERF GNILVAYAKD GSPVYAKDLK AHGAMAALLK DAIKPNLVQT IEGTPAFVHG GPFANIAHGC NSVTATRLAK HLADYAVTEA GFGADLGAEK FCDIKCRLAG LKPDAAVVVA TVRALKYNGG VERANLGEEN LEALAKGLPN LLKHISNLKN VFGLPVVVAL NRFVSDSDAE LAMIEKACAE HGVEVSLTEV WGKGGAGGAD LARKVVNAID NQPNNFGFAY DVELGIKDKI RAIAQKVYGA EDVDFSAEAS AEIASLEKLG LDKMPICMAK TQYSLSDNAK LLGCPEGFRI AVRGITVSAG AGFIVALCGN MMKMPGLPKV PAAEKIDVDE HGVIHGLF // ID FTSQ_NEIG1 Reviewed; 242 AA. AC Q5F6M1; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE RecName: Full=Cell division protein FtsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN Name=ftsQ {ECO:0000255|HAMAP-Rule:MF_00911}; GN OrderedLocusNames=NGO1530; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90166.1; -; Genomic_DNA. DR RefSeq; WP_003689436.1; NC_002946.2. DR RefSeq; YP_208578.1; NC_002946.2. DR ProteinModelPortal; Q5F6M1; -. DR EnsemblBacteria; AAW90166; AAW90166; NGO_1530. DR GeneID; 3281504; -. DR KEGG; ngo:NGO1530; -. DR PATRIC; 20336556; VBINeiGon24812_1826. DR HOGENOM; HOG000255873; -. DR KO; K03589; -. DR OMA; WHATLGN; -. DR OrthoDB; EOG6XM7B0; -. DR BioCyc; NGON242231:GI2G-1432-MONOMER; -. DR Proteomes; UP000000535; 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 1 242 Cell division protein FtsQ. FT /FTId=PRO_0000414681. FT TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TRANSMEM 13 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT TOPO_DOM 33 242 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00911}. FT DOMAIN 37 106 POTRA. {ECO:0000255|PROSITE- FT ProRule:PRU01115}. SQ SEQUENCE 242 AA; 27908 MW; A2940C637C2FEE35 CRC64; MWDNAEAMER LTRWLLVMMA MLLAASGLVW FYNSNHLPVK QVSLKGNLVY SDKKALGSLA KEYIHGNILR TDINGAQEAY RRYPWIASVM VRRRFPDTVE VVLTERKPVA RWGDHALVDG EGNVFEARLD RPGMPVFRGA EGTSAEMLRR YDEFSTVLAK QGLGIKEMTY TARSAWNVVL DNGITVRLGR ENEMKRLRLF TEAWQHLLRK NKNRLSYVDM RYKDGFSVRH APDGLPEKES EE // ID FTSB_NEIG1 Reviewed; 92 AA. AC Q5F8Z3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=Cell division protein FtsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN Name=ftsB {ECO:0000255|HAMAP-Rule:MF_00599}; GN OrderedLocusNames=NGO0616; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89344.1; -; Genomic_DNA. DR RefSeq; WP_002213385.1; NC_002946.2. DR RefSeq; YP_207756.1; NC_002946.2. DR EnsemblBacteria; AAW89344; AAW89344; NGO_0616. DR GeneID; 3281228; -. DR KEGG; ngo:NGO0616; -. DR PATRIC; 20334316; VBINeiGon24812_0730. DR HOGENOM; HOG000262021; -. DR KO; K05589; -. DR OMA; DYVRVKD; -. DR OrthoDB; EOG6P5ZC4; -. DR BioCyc; NGON242231:GI2G-584-MONOMER; -. DR Proteomes; UP000000535; 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_1000025709. 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 FTSL_NEIG1 Reviewed; 87 AA. AC Q5F6K8; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE RecName: Full=Cell division protein FtsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN Name=ftsL {ECO:0000255|HAMAP-Rule:MF_00910}; GN OrderedLocusNames=NGO1543; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90179.1; -; Genomic_DNA. DR RefSeq; WP_003689461.1; NC_002946.2. DR RefSeq; YP_208591.1; NC_002946.2. DR EnsemblBacteria; AAW90179; AAW90179; NGO_1543. DR GeneID; 3281486; -. DR KEGG; ngo:NGO1543; -. DR PATRIC; 20336584; VBINeiGon24812_1840. DR HOGENOM; HOG000219098; -. DR OrthoDB; EOG6WQD9T; -. DR BioCyc; NGON242231:GI2G-1445-MONOMER; -. DR Proteomes; UP000000535; 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 87 Cell division protein FtsL. FT /FTId=PRO_0000414563. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TRANSMEM 7 23 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT TOPO_DOM 24 87 Periplasmic. {ECO:0000255|HAMAP- FT Rule:MF_00910}. FT COILED 31 71 {ECO:0000255}. SQ SEQUENCE 87 AA; 9991 MW; 66666B15CB80E5B8 CRC64; MNKSNFFLLL AVCVSAFSVV MQQNQYRLNF TALDKAKKQE IALEQDYAQM RLQQARLANH EAIRAAAEKQ NLHPPVSGNT FMVEHQR // ID G6PI2_NEIG1 Reviewed; 547 AA. AC Q5F694; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Glucose-6-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=GPI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphoglucose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PGI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE AltName: Full=Phosphohexose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00473}; DE Short=PHI 2 {ECO:0000255|HAMAP-Rule:MF_00473}; GN Name=pgi2 {ECO:0000255|HAMAP-Rule:MF_00473}; GN OrderedLocusNames=NGO1668; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP- CC Rule:MF_00473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90293.1; -; Genomic_DNA. DR RefSeq; WP_010951319.1; NC_002946.2. DR RefSeq; YP_208705.1; NC_002946.2. DR ProteinModelPortal; Q5F694; -. DR EnsemblBacteria; AAW90293; AAW90293; NGO_1668. DR GeneID; 3281318; -. DR KEGG; ngo:NGO1668; -. DR PATRIC; 20336886; VBINeiGon24812_1988. DR HOGENOM; HOG000261370; -. DR KO; K01810; -. DR OMA; EQPAVEW; -. DR OrthoDB; EOG64R61J; -. DR BioCyc; NGON242231:GI2G-1562-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000535; 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_0000180690. FT ACT_SITE 351 351 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00473}. FT ACT_SITE 382 382 {ECO:0000255|HAMAP-Rule:MF_00473}. FT ACT_SITE 508 508 {ECO:0000255|HAMAP-Rule:MF_00473}. SQ SEQUENCE 547 AA; 60317 MW; FAD6BFEE1FD7D6F3 CRC64; MDAFTRAWYA LERHYQDTCH ILLRDRFAAE PDRFERMHER LDGMLFDYSK NRFGEDTLQL LCRLAETADL EGKMRALRTG AKVNGSEGRA ALHTALRLPD GADAVYADGR DVLPEIRREL NRALKFAHSL DDGLYQGITG KRIADFVHIG IGGSDLGPAM CVQALEPFRR QISVHFVSNA DPACLDEVLC RLNPETTMFC VASKSFKTPE TLLNAEAVKA WYRGAGFSES ETAHHFCAVS ADTEAAQSFG IAAERVFAMY DWVGGRYSVW SPVGLPVMVA VGGARFRELL AGAHAMDSHF FHTPPRRNIP VLMALIAVWY NNFQHADGQT AVPYSHNLRL LPAWLNQLDM ESLGKSRASD GSPAACKTGG IVFGGEGVNC QHAYFQLLHQ GTRLIPCDFI VPMTAQGAED GRSRFTVANA FAQAEALMKG KTLDEARAEL ADLPEAERER LAPHKEFPGN RPSNSILLDR LTPCNLGMLM AAYEHKTFVQ GAIWNVNPFD QWGVEYGKQL AKTIIGELEG GTSVHDASTE GLMAFYRECR LKGGGAA // ID GCSP_NEIG1 Reviewed; 950 AA. AC Q5F761; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711}; DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711}; DE AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711}; DE AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711}; DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711}; GN Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; GN OrderedLocusNames=NGO1325; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. The P protein binds the alpha-amino group of glycine CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein. {ECO:0000255|HAMAP- CC Rule:MF_00711}. CC -!- CATALYTIC ACTIVITY: Glycine + [glycine-cleavage complex H CC protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H CC protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00711}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00711}; CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}. CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP- CC Rule:MF_00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89976.1; -; Genomic_DNA. DR RefSeq; WP_003705868.1; NC_002946.2. DR RefSeq; YP_208388.1; NC_002946.2. DR ProteinModelPortal; Q5F761; -. DR EnsemblBacteria; AAW89976; AAW89976; NGO_1325. DR GeneID; 3281818; -. DR KEGG; ngo:NGO1325; -. DR PATRIC; 20336017; VBINeiGon24812_1559. DR HOGENOM; HOG000239369; -. DR KO; K00281; -. DR OMA; MAGMYAV; -. DR OrthoDB; EOG6HMXDX; -. DR BioCyc; NGON242231:GI2G-1239-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 2. DR HAMAP; MF_00711; GcvP; 1. DR InterPro; IPR003437; GcvP. DR InterPro; IPR020580; GDC-P_N. DR InterPro; IPR020581; GDC_P. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR PANTHER; PTHR11773; PTHR11773; 1. DR Pfam; PF02347; GDC-P; 2. DR SUPFAM; SSF53383; SSF53383; 3. DR TIGRFAMs; TIGR00461; gcvP; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 950 Glycine dehydrogenase (decarboxylating). FT /FTId=PRO_0000227108. FT MOD_RES 698 698 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00711}. SQ SEQUENCE 950 AA; 104080 MW; FFD4BDE3B5A7437E CRC64; MKLSELFNPN EFAARHLSFG DEAALLAAVG EKSMDEFVGN TLPQSIRMPS ELDLPEALTE ADALAKLKGI ASKNVINKSY IGLGYYPTRV PNVILRNVLE NPGWYTAYTP YQAEIAQGRL EALLNFQQVC IDLTGFPVAG ASLLDEATAA AEAMAMAHRV GKVKSERFFV DARVYPQTLD VMKTRAKYFG FELVVSDFAQ ADEGEYFGAL FQYVGKDGDV QDLQDVIGRL KAKGTIVAVA ADIMSLVLLK SPAELGADIA LGNTQRFGVP MGFGGPHAAY FAFKDEFKRS APGRIIGVSK DASGKPALRM ALSTREQHIR REKATSNICT AQALLANLAG MYAVYHGPKG VKRIANRIHT LASVFADALV SDGLKVVHEV FFDTVTVDFG SKEKADQVFA AALESGYNLR SVNNTQVAAA FHETSVYEDL ADLYRAFTGK DTFTFADDVK GRLNAELLRQ DDILQHPVYN SYHTEHEMLR YLKKLEDRDL AMNRSMISLG SCTMKLNATA EMLPITWTEF SDIHPYAPEA QTAGYRELLA DMENSLKAIT GFDAISFQPN SGAQGEYSGM LAIRRYQEAQ GEAHRNICLI PKSAHGTNPA TAAMLGLKVV VVDTDEHGNV NIDDLKAKAE QHRDALSAIM ITYPSTHGVY EEGIRDICRI IHENGGQVYM DGANLNAQIG IMQPAEVGAD VLHMNLHKTF CIPHGGGGPG MGPIGLKAHL APFAPGHTLT DTHSASAGQT SVAAAAFGSA SILPITWMYL TMMGKQGMEQ ATRWALLNAN YVAKRLSEDY PILYTGKNGR IAHECIVDLR PLKAESGITE TDIAKRLMDY GFHAPTVSFP VAGTLMIEPT ESESKAELDR FIAALKSIRR EVQKVIDGEW PKDDNPLVNA PHTAADITGE WAHPYSREEA VFPLPFVREH KFWPFVNRVD DVYGDRNLVC SCPPMENYED // ID GATA_NEIG1 Reviewed; 481 AA. AC Q5F8U8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0662; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89389.1; -; Genomic_DNA. DR RefSeq; WP_010951102.1; NC_002946.2. DR RefSeq; YP_207801.1; NC_002946.2. DR ProteinModelPortal; Q5F8U8; -. DR EnsemblBacteria; AAW89389; AAW89389; NGO_0662. DR GeneID; 3282547; -. DR KEGG; ngo:NGO0662; -. DR PATRIC; 20334420; VBINeiGon24812_0782. DR HOGENOM; HOG000116699; -. DR KO; K02433; -. DR OMA; KEYFGAG; -. DR OrthoDB; EOG61P6R9; -. DR BioCyc; NGON242231:GI2G-629-MONOMER; -. DR Proteomes; UP000000535; 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_0000241120. 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; 51306 MW; 9747310A38AF919B CRC64; MTQYTLKQAG SLLQSKQISA VELASAYLAA IAEKNPALNG YITIDQDKTL AEARAADERI AQGNASALTG VPVAYKDIFC QTGWRSACAS KMLDNFIFPY TATVVQNLLD EGMVTLGRTN MDEFAMGSTN ENSFYGAAKN PWNPEHVPGG SSGGSAAVVA ARLAPAALGS DTGGSIRQPA SHCGITGIKP TYGTVSRFGM VAYASSFDQA GPMAQTAEDC AILLNAMAGF DPKDSTSFER EKEDYTRDLD KPLKGVKIGL PKEYFSEGNS TDVQTALQNT IDLLKAQGAE LVEVSLPQTK LSIPAYYVLA SAEAGTNLSR YDGVRYGHRA AQFGDLEEMY GKTRAEGFGS EVKRRIMIGT YVLSHGYYDA YYLKAQKLRR LVADDFQTAF ARCDLILAPT APSAAPKIGA DTSPVETYLS DIYTIAVNLA GLPALTLPAG FSGGGLPVGV QLVGNYFAEA KILGAAHQIQ LNSDWHGKRP E // ID GATC_NEIG1 Reviewed; 96 AA. AC Q5F8U7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 60. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C {ECO:0000255|HAMAP-Rule:MF_00122}; DE Short=Asp/Glu-ADT subunit C {ECO:0000255|HAMAP-Rule:MF_00122}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00122}; GN Name=gatC {ECO:0000255|HAMAP-Rule:MF_00122}; GN OrderedLocusNames=NGO0663; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89390.1; -; Genomic_DNA. DR RefSeq; WP_003688831.1; NC_002946.2. DR RefSeq; YP_207802.1; NC_002946.2. DR ProteinModelPortal; Q5F8U7; -. DR EnsemblBacteria; AAW89390; AAW89390; NGO_0663. DR GeneID; 3281108; -. DR KEGG; ngo:NGO0663; -. DR PATRIC; 20334422; VBINeiGon24812_0783. DR HOGENOM; HOG000017522; -. DR KO; K02435; -. DR OMA; SVTPMAM; -. DR OrthoDB; EOG61S35Z; -. DR BioCyc; NGON242231:GI2G-630-MONOMER; -. DR Proteomes; UP000000535; 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 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit C. FT /FTId=PRO_1000016156. SQ SEQUENCE 96 AA; 11032 MW; 0915252FAA53042C CRC64; MALTLADVDK IARLSRLQLT AEEKEKSLQE LNDIFTMVEQ MQNINTDGIE PMAHPHEVAL RLREDEVTET DRAAEYQAVA PEVRNRLYIV PQVIEE // ID GATB_NEIG1 Reviewed; 476 AA. AC Q5F8V0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO0660; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89387.1; -; Genomic_DNA. DR RefSeq; WP_003688837.1; NC_002946.2. DR RefSeq; YP_207799.1; NC_002946.2. DR ProteinModelPortal; Q5F8V0; -. DR EnsemblBacteria; AAW89387; AAW89387; NGO_0660. DR GeneID; 3281129; -. DR KEGG; ngo:NGO0660; -. DR PATRIC; 20334416; VBINeiGon24812_0780. DR HOGENOM; HOG000223742; -. DR KO; K02434; -. DR OMA; ESADYRY; -. DR OrthoDB; EOG6RJV5B; -. DR BioCyc; NGON242231:GI2G-627-MONOMER; -. DR Proteomes; UP000000535; 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 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; 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_0000241243. SQ SEQUENCE 476 AA; 51713 MW; 0F861167F5CC9D5E CRC64; MTWETVIGLE IHVQLNTKSK IFSGASTAFG AEPNAHASVV ECALPGVLPV MNREVVEKAI KLGLALDAKI NRKNVFDRKN YFYPDLPKGY QISQLDLPIV EHGKLEIVVG GDVKTINVTR AHMEEDAGKS VHEGLNGATG IDLNRAGTPL LEVVSEPEMR SAAEAVAYAK ALHSLVTWLD ICDGNMAEGS FRIDANVSVR PKGQAEFGTR REIKNLNSFR FLDQAINYEA EAQIEILEDG GTVQQATMLF DPEKGETRVM RLKEDAHDYG YFPDPDLLPV IISDAQMQKA KAEMPELPKE MAARFVADYG VSEYDARLLT ASRVQAAYFE EAAKESGQGK PTANWMNGEL AATLNKEGME LADSPITAPR LAALVGKIAD GTLSGKLAKK AFEAMWAEPE TSIAEIIEKH SLQQMTDTGA VEAMVDEVLA NNAKAVEQFK SGNEKALNAI VGQVMKTSKG KANPAQVQEL IKAKLA // ID GCH4_NEIG1 Reviewed; 257 AA. AC Q5F9K6; DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=GTP cyclohydrolase FolE2; DE EC=3.5.4.16; DE AltName: Full=GTP cyclohydrolase 1B; GN Name=folE2; OrderedLocusNames=NGO0387; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17032654; DOI=10.1074/jbc.M607114200; RA El Yacoubi B., Bonnett S., Anderson J.N., Swairjo M.A., RA Iwata-Reuyl D., de Crecy-Lagard V.; RT "Discovery of a new prokaryotic type I GTP cyclohydrolase family."; RL J. Biol. Chem. 281:37586-37593(2006). CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate. CC {ECO:0000269|PubMed:17032654}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 2-amino-4-hydroxy-6- CC (erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate. CC {ECO:0000269|PubMed:17032654}. CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step CC 1/1. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV 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; AE004969; AAW89131.1; -; Genomic_DNA. DR RefSeq; WP_003687811.1; NC_002946.2. DR RefSeq; YP_207543.1; NC_002946.2. DR PDB; 3D1T; X-ray; 2.20 A; A/B=1-257. DR PDB; 3D2O; X-ray; 2.04 A; A/B=1-257. DR PDBsum; 3D1T; -. DR PDBsum; 3D2O; -. DR ProteinModelPortal; Q5F9K6; -. DR SMR; Q5F9K6; 15-256. DR EnsemblBacteria; AAW89131; AAW89131; NGO_0387. DR GeneID; 3282560; -. DR KEGG; ngo:NGO0387; -. DR PATRIC; 20333781; VBINeiGon24812_0468. DR HOGENOM; HOG000280679; -. DR KO; K09007; -. DR OMA; INMYVDL; -. DR OrthoDB; EOG6X6RBH; -. DR BioCyc; NGON242231:GI2G-366-MONOMER; -. DR BRENDA; 3.5.4.16; 3590. DR UniPathway; UPA00848; UER00151. DR EvolutionaryTrace; Q5F9K6; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 257 GTP cyclohydrolase FolE2. FT /FTId=PRO_0000147714. FT SITE 147 147 May be catalytically important. FT {ECO:0000250}. FT STRAND 18 34 {ECO:0000244|PDB:3D2O}. FT STRAND 37 51 {ECO:0000244|PDB:3D2O}. FT HELIX 61 69 {ECO:0000244|PDB:3D2O}. FT HELIX 76 89 {ECO:0000244|PDB:3D2O}. FT STRAND 93 108 {ECO:0000244|PDB:3D2O}. FT TURN 110 112 {ECO:0000244|PDB:3D2O}. FT STRAND 115 129 {ECO:0000244|PDB:3D2O}. FT STRAND 132 146 {ECO:0000244|PDB:3D2O}. FT HELIX 148 153 {ECO:0000244|PDB:3D2O}. FT STRAND 154 156 {ECO:0000244|PDB:3D2O}. FT STRAND 160 173 {ECO:0000244|PDB:3D2O}. FT HELIX 177 185 {ECO:0000244|PDB:3D2O}. FT STRAND 188 191 {ECO:0000244|PDB:3D2O}. FT HELIX 198 210 {ECO:0000244|PDB:3D2O}. FT HELIX 215 228 {ECO:0000244|PDB:3D2O}. FT STRAND 232 241 {ECO:0000244|PDB:3D2O}. FT STRAND 246 256 {ECO:0000244|PDB:3D2O}. SQ SEQUENCE 257 AA; 28747 MW; A0235399C3EDF2A9 CRC64; MNAIADVQSS RDLRNLPINQ VGIKDLRFPI TLKTAEGTQS TVARLTMTVY LPAEQKGTHM SRFVALMEQH TEVLDFAQLH RLTAEMVALL DSRAGKISVS FPFFRKKTAP VSGIRSLLDY DVSLTGEMKD GAYGHSMKVM IPVTSLCPCS KEISQYGAHN QRSHVTVSLT SDAEVGIEEV IDYVETQASC QLYGLLKRPD EKYVTEKAYE NPKFVEDMVR DVATSLIADK RIKSFVVESE NFESIHNHSA YAYIAYP // ID GLND_NEIG1 Reviewed; 852 AA. AC Q5F8H5; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0798; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89512.1; -; Genomic_DNA. DR RefSeq; WP_010951127.1; NC_002946.2. DR RefSeq; YP_207924.1; NC_002946.2. DR ProteinModelPortal; Q5F8H5; -. DR EnsemblBacteria; AAW89512; AAW89512; NGO_0798. DR GeneID; 3282021; -. DR KEGG; ngo:NGO0798; -. DR PATRIC; 20334744; VBINeiGon24812_0944. DR HOGENOM; HOG000261778; -. DR KO; K00990; -. DR OMA; HTLFWIA; -. DR OrthoDB; EOG6CCH44; -. DR BioCyc; NGON242231:GI2G-752-MONOMER; -. DR Proteomes; UP000000535; 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_0000192746. 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; 96964 MW; 446EC476F5205885 CRC64; MPENLSSALE TFKQQRNAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE HFQNSALCLM AVGGFGRGEP YPCSDVDLAV VSPAPLSDGI QEQIARFIQT LWDCKLMPSV KSGSVDELCE SVRDDITGDT AFLEARFLFG NRQTADELAE KMNVQRNVAA FIEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL LWIAKAQGLA ANLPDLLKQR ILTRAEAGML SHGYRRLAHI RIRLHLNAKR AEDRLLFDLQ PQVAESMGYQ DENRRRQSEE LMRVFYRAVK TVKQLGGILT PMLRSRVSST PVRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRRRFA GFFRSGNGLT QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LAVVRNVRRL ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAVQGIADA RQFAADHFLT EEESDLLAWL VENHLLMSAV AQKEDIQDPG VLDAFCKRVQ THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RCLAGNDGNP HALFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA NLVHDFEPPI VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA ETQSCNRRIS RRSRYMPIAP SITITPEEDY PDRYSVEITA VNRPFLLADM AEVFFAHNVS LRYAKISTLD ERVEDSFTVF SPDLKNPKIQ SSLKQALLEQ LA // ID GLK_NEIG1 Reviewed; 328 AA. AC Q5F8Q0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO0717; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89437.1; -; Genomic_DNA. DR RefSeq; WP_010951113.1; NC_002946.2. DR RefSeq; YP_207849.1; NC_002946.2. DR ProteinModelPortal; Q5F8Q0; -. DR EnsemblBacteria; AAW89437; AAW89437; NGO_0717. DR GeneID; 3282002; -. DR KEGG; ngo:NGO0717; -. DR PATRIC; 20334562; VBINeiGon24812_0853. DR HOGENOM; HOG000274469; -. DR KO; K00845; -. DR OMA; GHADFAP; -. DR OrthoDB; EOG64BQ47; -. DR BioCyc; NGON242231:GI2G-677-MONOMER; -. DR Proteomes; UP000000535; 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_0000268778. FT NP_BIND 16 21 ATP. {ECO:0000255|HAMAP-Rule:MF_00524}. SQ SEQUENCE 328 AA; 35112 MW; 765E9E4DD01AE499 CRC64; MSSTPNKHAD YPRLVADIGG TNARFALETA PCVIEKVAVL PCKEYDTVTD AVRAYLNQSG ATGVRHAAFA IANPILGDWV QMTNHHWAFS IETTRQALGL DTLILLNDFT AQALAVTQTS SKDLMQVGGQ KPVEFAPKAV IGPGTGLGVS GLVHSPAGWV ALAGEGGHTS FPPFDDMEVL IWQYAKNKYR HVSAERFLSG AGLSLIYETL AVKQKAEPAK LMPSEITEKA LNCESPLCRQ ALDIFCAMLG TVASNLALTL GARGGVYLCG GIIPRMLDYF KTSPFRSRFE NKGRFEAYLA AIPVYVVLSE FPGIAGAAAA LGNHLKNV // ID GLMS_NEIG1 Reviewed; 612 AA. AC Q5F584; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 79. 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=NGO2045; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90653.1; -; Genomic_DNA. DR RefSeq; WP_010951391.1; NC_002946.2. DR RefSeq; YP_209065.1; NC_002946.2. DR ProteinModelPortal; Q5F584; -. DR MEROPS; C44.971; -. DR EnsemblBacteria; AAW90653; AAW90653; NGO_2045. DR GeneID; 3282702; -. DR KEGG; ngo:NGO2045; -. DR PATRIC; 20337885; VBINeiGon24812_2465. DR HOGENOM; HOG000258896; -. DR KO; K00820; -. DR OMA; GEFFCAS; -. DR OrthoDB; EOG6KT2Q1; -. DR BioCyc; NGON242231:GI2G-1947-MONOMER; -. DR Proteomes; UP000000535; 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_0000135359. 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; 66488 MW; BB7ACAA1456CB7C0 CRC64; MCGIVGAIRA HHNVVDFLTD GLKRLEYRGY DSSGIAVYSD GKIKRVRRVG RVQLMEDAAR EKGISGGIGI GHTRWATHGG VTEPNAHPHI SGGMIAVVHN GIIENFESER KRLEGLGYRF ESQTDTEVIA HSINHEYAQN GGRLFEAVQE AVKRFHGAYA IAVIAQDKPD ELVVARMGCP LLVALGDDET FIASDVSAVI AFTRRVAYLE DGDIALLASD GIKRLTDKNG LPAERKVKVS ELSPASLEPG PHSHFMQKEI HEQPRAIADT AEVFLDGGFI PENFGKNAKS VFESIRSVKI LACGTSYYAA LTAKYWLESI AKIPADVEIA SEYRYRSVIA DPDQLVITIS QSGETLDTME ALKYAKSLGH RHSLSVCNVM ESALPRESSL VLYTRAGAEI GVASTKAFTT QLVVLFGLAV TLAKVRGVVS GEDEARYTEE LRQLPGSVQH ALNLEPQIAA WAQQFAKKTS ALFLGRGIHY PIALEGALKL KEITYIHAEA YPAGELKHGP LALVDENMPV VVIAPNDSLL DKVKANMQEV GARGGELFVF ADLDSNFNAT EGVHVIRAPR HVGELSPVVH TVPVQLLAYH TALARGTDVD KPRNLAKSVT VE // ID GCSH_NEIG1 Reviewed; 128 AA. AC Q5F6Y8; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO1404; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90049.1; -; Genomic_DNA. DR RefSeq; WP_003695621.1; NC_002946.2. DR RefSeq; YP_208461.1; NC_002946.2. DR ProteinModelPortal; Q5F6Y8; -. DR EnsemblBacteria; AAW90049; AAW90049; NGO_1404. DR GeneID; 3281213; -. DR KEGG; ngo:NGO1404; -. DR PATRIC; 20336211; VBINeiGon24812_1654. DR HOGENOM; HOG000239392; -. DR KO; K02437; -. DR OMA; NTDPYGE; -. DR OrthoDB; EOG60CWTC; -. DR BioCyc; NGON242231:GI2G-1314-MONOMER; -. DR Proteomes; UP000000535; 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; 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. PE 3: Inferred from homology; KW Complete proteome; Lipoyl; Reference proteome. FT CHAIN 1 128 Glycine cleavage system H protein. FT /FTId=PRO_0000302399. 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; 13613 MW; 646DF0D05E4C1EAF CRC64; MSNNIPTELK YVASHEWLRL EEDGTITVGI THHAQELLGD IVFVELPEVG ANLAAEEQSG VVESVKAASD VYAPIAGEVV AVNDDLPGAP ETANSDPYGA GWFFKIKPAN PADYDGLLTA EQYAGEVD // ID GMHA_NEIG1 Reviewed; 197 AA. AC Q5F5E3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. 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}; GN OrderedLocusNames=NGO1986; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90594.1; -; Genomic_DNA. DR RefSeq; WP_003692028.1; NC_002946.2. DR RefSeq; YP_209006.1; NC_002946.2. DR PDB; 5I01; X-ray; 2.37 A; A/B/C/D=1-197. DR PDBsum; 5I01; -. DR ProteinModelPortal; Q5F5E3; -. DR SMR; Q5F5E3; 4-195. DR EnsemblBacteria; AAW90594; AAW90594; NGO_1986. DR GeneID; 3282638; -. DR KEGG; ngo:NGO1986; -. DR PATRIC; 20337739; VBINeiGon24812_2396. DR HOGENOM; HOG000237572; -. DR KO; K03271; -. DR OMA; QHFRDSA; -. DR OrthoDB; EOG6384PC; -. DR BioCyc; NGON242231:GI2G-1884-MONOMER; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm; KW Isomerase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 197 Phosphoheptose isomerase. FT /FTId=PRO_1000009082. 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}. FT HELIX 4 25 {ECO:0000244|PDB:5I01}. FT HELIX 27 42 {ECO:0000244|PDB:5I01}. FT STRAND 47 50 {ECO:0000244|PDB:5I01}. FT HELIX 54 67 {ECO:0000244|PDB:5I01}. FT STRAND 79 81 {ECO:0000244|PDB:5I01}. FT HELIX 86 95 {ECO:0000244|PDB:5I01}. FT HELIX 98 100 {ECO:0000244|PDB:5I01}. FT HELIX 103 109 {ECO:0000244|PDB:5I01}. FT STRAND 115 123 {ECO:0000244|PDB:5I01}. FT HELIX 126 137 {ECO:0000244|PDB:5I01}. FT STRAND 141 147 {ECO:0000244|PDB:5I01}. FT HELIX 151 156 {ECO:0000244|PDB:5I01}. FT STRAND 161 166 {ECO:0000244|PDB:5I01}. FT HELIX 171 191 {ECO:0000244|PDB:5I01}. SQ SEQUENCE 197 AA; 21093 MW; 1F130C934E07E36D CRC64; MTTLQERVAA HFAESIRAKQ EAEKILVEPT VQAAELMLQC LMNDGKILAC GNGGSAADAQ HFAAEMTGRF EKERMELAAV ALTTDTSALT AIGNDYGFDH VFSKQVRALG RAGDVLVGIS TSGNSANVIE AVKAAHERDM HVIALTGRDG GKIAAMLKDT DVLLNVPHPR TARIQENHIL LIHAMCDCID SVLLEGM // ID GLMM_NEIG1 Reviewed; 445 AA. AC Q5F746; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO1341; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89991.1; -; Genomic_DNA. DR RefSeq; WP_003705855.1; NC_002946.2. DR RefSeq; YP_208403.1; NC_002946.2. DR ProteinModelPortal; Q5F746; -. DR EnsemblBacteria; AAW89991; AAW89991; NGO_1341. DR GeneID; 3282056; -. DR KEGG; ngo:NGO1341; -. DR PATRIC; 20336053; VBINeiGon24812_1576. DR HOGENOM; HOG000268678; -. DR KO; K03431; -. DR OMA; FNLGGEQ; -. DR OrthoDB; EOG6TN467; -. DR BioCyc; NGON242231:GI2G-1255-MONOMER; -. DR Proteomes; UP000000535; 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 1 445 Phosphoglucosamine mutase. FT /FTId=PRO_0000147919. FT ACT_SITE 105 105 Phosphoserine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 105 105 Magnesium; via phosphate group. FT {ECO:0000255|HAMAP-Rule:MF_01554}. FT METAL 244 244 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 246 246 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT METAL 248 248 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01554}. FT MOD_RES 105 105 Phosphoserine. {ECO:0000255|HAMAP- FT Rule:MF_01554}. SQ SEQUENCE 445 AA; 47954 MW; E2E8DF7E5519469E CRC64; MMAKKYFGTD GVRGEVGQFP ITPDFVLKLG YAAGQVLVQH DTDQKPTVLI GKDTRISGYM LEAALVAGFT AAGVNVVQTG PLPTPGVAYL TRALRLSAGV MISASHNTYS DNGIKFFAEG GVKLSDEVEL EIEAKIDEEM KTQPSARLGR ARRISGADDR YIEFCKSTFP GHSDLRGLKL VIDTANGAGY GVAPKVFHEL GAQVVSIGNE PNGYNINEKC GATHTKTLQA AVLQNEADYG IALDGDGDRL MMVDKNRQVY DGDSLIYVIA KARAREGINI GGVVGTVMTN MAMEIALKEQ GVDFCRAKVG DRYVLEQLNQ RGWLIGGEAS GHILCMDKHN TGDGIISALQ VLAALQILNQ DLATVCADWQ PYPQTMINVR IQKGQKWQEA SKDVLAEVEK ELEGKGRVVL RASGTEPVVR VMVEARQADW ARDGAERIAA AIGGI // ID GLMU_NEIG1 Reviewed; 456 AA. AC Q5F577; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 81. 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=NGO2053; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90660.1; -; Genomic_DNA. DR RefSeq; WP_003686996.1; NC_002946.2. DR RefSeq; YP_209072.1; NC_002946.2. DR ProteinModelPortal; Q5F577; -. DR SMR; Q5F577; 6-450. DR EnsemblBacteria; AAW90660; AAW90660; NGO_2053. DR GeneID; 3282732; -. DR KEGG; ngo:NGO2053; -. DR PATRIC; 20337907; VBINeiGon24812_2476. DR HOGENOM; HOG000283476; -. DR KO; K04042; -. DR OMA; SITANYD; -. DR OrthoDB; EOG6Z6FQZ; -. DR BioCyc; NGON242231:GI2G-1954-MONOMER; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR UniPathway; UPA00973; -. DR Proteomes; UP000000535; 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_0000233803. 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; 48873 MW; 29440787F023A3BD CRC64; MPQNTLNTVI LAAGKGTRMY SQMPKVLHCI GGKPMVERVI DTAAALNPQN ICVVVGHGKE QVLDTVKRDA VWVEQTEQLG TGHAVKTALP HLASEGRTLV LYGDVPLIDV ETLETLLEAA GNEVGLLTDV PADPAGLGRI IRDGSGSVTA IVEEKDASAT QKTIREINTG ILVLPNAKLE NWLNSLSSNN AQGEYYLTDL IAKAVADGIK VRPVRVRASH LAAGVNNKRQ LAELERIFQT EQAQELLKAG VTLRDPARFD LRGRLKHGQD VVIDVNVVIE GEVELGDNVE IGANCVIKNA KIGANSKIAP FSHLEGCEVG ENNRIGPYAR LRPQAKLADN VHVGNFVEIK NAAIGKGTKA NHLTYIGDAE VGSKTNFGAG TIIANYDGVH KHKTVIGDEV RIGSNCVLVA PVTLGNKVTT GAGSTITRNI EDNKLALARA RQTVIEGWMR PEKDKQ // ID GLO2_NEIG1 Reviewed; 250 AA. AC Q5F7J0; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO1187; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89847.1; -; Genomic_DNA. DR RefSeq; WP_003689617.1; NC_002946.2. DR RefSeq; YP_208259.1; NC_002946.2. DR ProteinModelPortal; Q5F7J0; -. DR EnsemblBacteria; AAW89847; AAW89847; NGO_1187. DR GeneID; 3281978; -. DR KEGG; ngo:NGO1187; -. DR PATRIC; 20335671; VBINeiGon24812_1394. DR HOGENOM; HOG000058041; -. DR KO; K01069; -. DR OMA; MERSICH; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NGON242231:GI2G-1099-MONOMER; -. DR UniPathway; UPA00619; UER00676. DR Proteomes; UP000000535; 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 1 250 Hydroxyacylglutathione hydrolase. FT /FTId=PRO_0000309662. 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 250 AA; 27810 MW; A7841E49F2F600F5 CRC64; MKITPVKALT DNYIWMIQHG NHAVCVDPSE PSPVLEFLVR NRLMLAQTWV THPHPDHEGG AAALWRGYME SPVYGESDIE AATHTVTAGT RFTFGNGQVT VWATPGHTDR HTSYLLETSD GIHVFCGDTL FSAGCGRVFT GTVEQLYDNF QRFNQLPEGT LFYPAHEYTA ANLRFAAHIE PDNADIQTAL KAAEHTPTLP VTLAHERRVN PFLRTEIPAV RQRAEALVGK TLNSGLEVFA ALRELKNAYR // ID GLUQ_NEIG1 Reviewed; 295 AA. AC Q5F6E8; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1611; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90239.1; -; Genomic_DNA. DR RefSeq; WP_010951304.1; NC_002946.2. DR RefSeq; YP_208651.1; NC_002946.2. DR ProteinModelPortal; Q5F6E8; -. DR EnsemblBacteria; AAW90239; AAW90239; NGO_1611. DR GeneID; 3281447; -. DR KEGG; ngo:NGO1611; -. DR PATRIC; 20336762; VBINeiGon24812_1926. DR HOGENOM; HOG000252723; -. DR KO; K01894; -. DR OMA; WQGVTDI; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NGON242231:GI2G-1508-MONOMER; -. DR Proteomes; UP000000535; 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_0000208306. 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; 33284 MW; 650407D08495E3AA CRC64; MYTGRFAPSP TGLLHIGSLL TAVASYADAR SNGGKWLVRM EDLDPPREMP GAASHILHTL EAFGFKWDGE VTYQSRRYAL YEETLYRLKT AGLVYPCHCN RKDWQAGARR GTDGFVYNGR CRHPGQRPAL QGKQPSWRIR VPDRDIGFSD GIVGSYAQNL ARDIGDFVLF RADGYWAYQL AVVADDAEQG VTHIVRGQDL LVSTPRQIYL QQCLGVPTPQ YAHLPLLTNA QGQKWSKQTL APALDLNRRE QLLRQVFRYL KLPEAPETDR PAELLDWAVA HWDMDKVPKH AITAP // ID GLYA_NEIG1 Reviewed; 416 AA. AC Q5F8C0; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO0866; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10417653; DOI=10.1046/j.1365-2958.1999.01514.x; RA Zhu P., Morelli G., Achtman M.; RT "The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, RT deletions, insertion elements and DNA islands."; RL Mol. Microbiol. 33:635-650(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AJ242839; CAB45001.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89567.1; -; Genomic_DNA. DR RefSeq; WP_010951137.1; NC_002946.2. DR RefSeq; YP_207979.1; NC_002946.2. DR ProteinModelPortal; Q5F8C0; -. DR SMR; Q5F8C0; 1-415. DR PRIDE; Q5F8C0; -. DR EnsemblBacteria; AAW89567; AAW89567; NGO_0866. DR GeneID; 3281886; -. DR KEGG; ngo:NGO0866; -. DR PATRIC; 20334904; VBINeiGon24812_1022. DR HOGENOM; HOG000239404; -. DR KO; K00600; -. DR OMA; VSFTTHK; -. DR OrthoDB; EOG6Z0QB2; -. DR BioCyc; NGON242231:GI2G-809-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000535; 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_0000113620. 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; 44990 MW; F53A0C9274D00219 CRC64; MFSKSVTLAQ YDPDLAAAIA QEDRRQQDHV ELIASENYVS CAVMEAQGSQ LTNKYAEGYP AKRYYGGCEY VDIVEQLAID RVKELFGAAY ANVQPHSGSQ ANQAVYASVL KPGDTILGMS LAHGGHLTHG ASVNISGKLY NAVTYGLDEN EVLDYAEVER LALEHKPKMI VAGASAYALQ IDWAKFREIA DKVGAYLFVD MAHYAGLVAG GEYPNPVPFC DFVTTTTHKT LRGPRGGVIL CRDNTHEKAL NSSIFPSLQG GPLMHVIAAK AVAFKEALQP EFKQYAKQVK INAAVMAEEL VKRGLRIVSG RTESHVFLVD LQPMKITGKA AEAALGKAHI TVNKNAIPND PEKPFVTSGI RIGSAAMTTR GFNETDARVL SNLVADVLAN PEDEANLAKV RGQVTALCDK YPVYGT // ID GPH_NEIG1 Reviewed; 236 AA. AC Q5F7W4; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Phosphoglycolate phosphatase {ECO:0000255|HAMAP-Rule:MF_00495}; DE Short=PGP {ECO:0000255|HAMAP-Rule:MF_00495}; DE Short=PGPase {ECO:0000255|HAMAP-Rule:MF_00495}; DE EC=3.1.3.18 {ECO:0000255|HAMAP-Rule:MF_00495}; GN OrderedLocusNames=NGO1052; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the dephosphorylation of 2- CC phosphoglycolate. Is involved in the dissimilation of the CC intracellular 2-phosphoglycolate formed during the DNA repair of CC 3'-phosphoglycolate ends, a major class of DNA lesions induced by CC oxidative stress. {ECO:0000255|HAMAP-Rule:MF_00495}. CC -!- CATALYTIC ACTIVITY: 2-phosphoglycolate + H(2)O = glycolate + CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00495}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00495}; CC -!- PATHWAY: Organic acid metabolism; glycolate biosynthesis; CC glycolate from 2-phosphoglycolate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00495}. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC CbbY/CbbZ/Gph/YieH family. {ECO:0000255|HAMAP-Rule:MF_00495}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89723.1; -; Genomic_DNA. DR RefSeq; WP_003688188.1; NC_002946.2. DR RefSeq; YP_208135.1; NC_002946.2. DR ProteinModelPortal; Q5F7W4; -. DR EnsemblBacteria; AAW89723; AAW89723; NGO_1052. DR GeneID; 3281802; -. DR KEGG; ngo:NGO1052; -. DR PATRIC; 20335334; VBINeiGon24812_1233. DR HOGENOM; HOG000248344; -. DR KO; K01091; -. DR OMA; AKNAGCA; -. DR OrthoDB; EOG6HB9PJ; -. DR BioCyc; NGON242231:GI2G-968-MONOMER; -. DR UniPathway; UPA00865; UER00834. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0046295; P:glycolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.150.240; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR HAMAP; MF_00495; GPH_hydrolase_bact; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR006346; PGP_bact. DR InterPro; IPR023198; PGP_dom2. 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. DR TIGRFAMs; TIGR01449; PGP_bact; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Hydrolase; Magnesium; KW Metal-binding; Reference proteome. FT CHAIN 1 236 Phosphoglycolate phosphatase. FT /FTId=PRO_0000238161. FT ACT_SITE 14 14 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 14 14 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 16 16 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. FT METAL 177 177 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00495}. SQ SEQUENCE 236 AA; 25654 MW; D819F06CDD85250F CRC64; MNAAIEHVQA VAFDLDGTLC DSVPDLAAAA EAMLEQLGMK PLPAKVVESY VGDGIGKLVH RVLTNDRDRE ADSELWEKGF VSYMKYYRDH LSVFTRPYPE TEAGLALLKS LGIPLVIITN KNEILAAELL KQLGLADYFS LILGGDSLPE KKPSPLPLRH AAEVLGIDAA NMLMVGDSRN DIIAAKAAGC LSVGVTFGYG DMTLLSQDDT TRPDRIIGAL PEIYENLQPQ KNKDEE // ID GSA_NEIG1 Reviewed; 426 AA. AC Q5FAH9; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO0040; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88808.1; -; Genomic_DNA. DR RefSeq; WP_003687258.1; NC_002946.2. DR RefSeq; YP_207220.1; NC_002946.2. DR ProteinModelPortal; Q5FAH9; -. DR SMR; Q5FAH9; 3-419. DR EnsemblBacteria; AAW88808; AAW88808; NGO_0040. DR GeneID; 3282386; -. DR KEGG; ngo:NGO0040; -. DR PATRIC; 20332914; VBINeiGon24812_0042. DR HOGENOM; HOG000020210; -. DR KO; K01845; -. DR OMA; CGHAHPE; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NGON242231:GI2G-36-MONOMER; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000000535; 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 1 426 Glutamate-1-semialdehyde 2,1-aminomutase. FT /FTId=PRO_0000120426. FT MOD_RES 265 265 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00375}. SQ SEQUENCE 426 AA; 45010 MW; 6ECA50AF8BC4B55B CRC64; MNRNEILFDR AKAIIPGGVN SPVRAFGSVG GVPRFIKKAE GAYVWDENGT RYTDYVGSWG PAIVGHAHPE VVEAVREAAL GGLSFGAPTE GEIAIAEQIA EIMPSVERLR LVSSGTEATM TAIRLARGFT GRDKIIKFEG CYHGHSDSLL VKAGSGLLTF GNPSSAGVPA DFTKHTLVLE YNNIAQLEEA FAQSGDEIAC VIVEPFVGNM NLVRPTEAFV KALRGLTEKH GAVLIYDEVM TGFRVALGGA QSLHGITPDL TTMGKVIGGG MPLAAFGGRK DIMECISPLG GVYQAGTLSG NPIAVAAGLK TLEIIQREGF YENLTALTQR LANGIAAAKA HGIEFAADSV GGMFGLYFAA HVPRNYADMA RSNIDAFKRF FHGMLDRGIA FGPSAYEAGF VSAAHTPELI DETVAVAVEV FKAMAA // ID GPDA_NEIG1 Reviewed; 329 AA. AC Q5F5A8; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. 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=NGO2021; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90629.1; -; Genomic_DNA. DR RefSeq; WP_003686938.1; NC_002946.2. DR RefSeq; YP_209041.1; NC_002946.2. DR ProteinModelPortal; Q5F5A8; -. DR EnsemblBacteria; AAW90629; AAW90629; NGO_2021. DR GeneID; 3282726; -. DR KEGG; ngo:NGO2021; -. DR PATRIC; 20337825; VBINeiGon24812_2436. DR HOGENOM; HOG000246853; -. DR KO; K00057; -. DR OMA; VVIMHAS; -. DR OrthoDB; EOG6JDWF4; -. DR BioCyc; NGON242231:GI2G-1922-MONOMER; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000535; 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_0000255334. 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; 35368 MW; 9477E5EDC39B0409 CRC64; MKITVIGAGS WGTALALHFS QHGNRVSLWT RNADQVRQMQ EARENKRGLP GFSFPETLEV CADLAEALKD SGLVLIVTSV AGLRSSAELL KQYGAGHLPV LAACKGFEQD TGLLTFQVLK EVLPDNKKIG VLSGPSFAQE LAKQLPCAVV LASENQEWIE ELVPQLNTTV MRLYGSTDVI GVAVGGSVKN VMAIATGLSD GLEYGLNARA ALVTRGLAEI TRLASAMGAQ PKTMMGLAGI GDLILTCTGA LSRNRRVGLG LAEGKELHQV LVEIGHVSEG VSTIEEVFNT ACKYQIDMPI TQTLLQLIRK EMTPQQVVER LMERSARFE // ID GUAA_NEIG1 Reviewed; 521 AA. AC Q5F4X9; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344}; DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344}; DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344}; DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344}; GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; GN OrderedLocusNames=NGO2164; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. CC {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_00344}. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) CC domain. {ECO:0000255|HAMAP-Rule:MF_00344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90758.1; -; Genomic_DNA. DR RefSeq; WP_003696594.1; NC_002946.2. DR RefSeq; YP_209170.1; NC_002946.2. DR ProteinModelPortal; Q5F4X9; -. DR SMR; Q5F4X9; 3-521. DR MEROPS; C26.957; -. DR EnsemblBacteria; AAW90758; AAW90758; NGO_2164. DR GeneID; 3282760; -. DR KEGG; ngo:NGO2164; -. DR PATRIC; 20338184; VBINeiGon24812_2614. DR HOGENOM; HOG000223964; -. DR KO; K01951; -. DR OMA; MSHGDSV; -. DR OrthoDB; EOG6JHRJV; -. DR BioCyc; NGON242231:GI2G-2052-MONOMER; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000000535; 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_0000229445. FT DOMAIN 5 197 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00344}. FT DOMAIN 198 390 GMPS ATP-PPase. {ECO:0000255|HAMAP- FT Rule:MF_00344}. FT NP_BIND 225 231 ATP. {ECO:0000255|HAMAP-Rule:MF_00344}. FT ACT_SITE 81 81 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00344}. FT ACT_SITE 171 171 {ECO:0000255|HAMAP-Rule:MF_00344}. FT ACT_SITE 173 173 {ECO:0000255|HAMAP-Rule:MF_00344}. SQ SEQUENCE 521 AA; 57626 MW; 38EC28BAA419C93C CRC64; MTQDKILILD FGSQVTRLIA RRVREAHVYC ELHSFDMPLD EIKAFNPKGI ILSGGPNSVY ESDYQADTGI FDLGIPVLGI CYGMQFMAHH LGGEVQPGNQ REFGYAQVKT IDSGLTRGIQ DDAPNTLDVW MSHGDKVSKL PDGFAVIGDT PSCPIAMMEN AEKQFYGIQF HPEVTHTKQG RALLNRFVLD ICGAQPGWTM PNYIEEAVAK IREQVGSDEV ILGLSGGVDS SVAAALIHRA IGDQLTCVFV DHGLLRLNEG KMVMDMFARN LGVKVIHVDA EGQFMAKLAG VTDPEKKRKI IGAEFIEVFD AEEKKLTNAK WLAQGTIYPD VIESAGAKTK KAHAIKSHHN VGGLPENMKL KLLEPLRDLF KDEVRELGVA LGLPREMVYR HPFPGPGLGV RILGEVKKEY ADLLRQADDI FIQELRNTTD ENGTSWYDLT SQAFAVFLPV KSVGVMGDGR TYDYVVALRA VITSDFMTAH WAELPYSLLG RVSNRIINEV KGINRVVYDV SGKPPATIEW E // ID GRPE_NEIG1 Reviewed; 192 AA. AC Q5F6X1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1422; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90066.1; -; Genomic_DNA. DR RefSeq; WP_003689277.1; NC_002946.2. DR RefSeq; YP_208478.1; NC_002946.2. DR ProteinModelPortal; Q5F6X1; -. DR EnsemblBacteria; AAW90066; AAW90066; NGO_1422. DR GeneID; 3281765; -. DR KEGG; ngo:NGO1422; -. DR PATRIC; 20336255; VBINeiGon24812_1676. DR HOGENOM; HOG000252084; -. DR KO; K03687; -. DR OMA; HERHDGA; -. DR OrthoDB; EOG6FJNJ9; -. DR BioCyc; NGON242231:GI2G-1331-MONOMER; -. DR Proteomes; UP000000535; 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_1000137585. SQ SEQUENCE 192 AA; 21350 MW; 8BCC742A29BC338C CRC64; MSEQTQQQNS EEAVENVEAV ETVETVGNAD GVQEQAAAEP AYEDLQARIA ELEAQLKDEQ LRALANEQNL RRRHQQEIAD THKFAGQKFA VEMLPVKDYL EMALLDQSGN FDALKMGVQM TLNELQKAFD ATQIKEINPK AGDKLDPNIH QAMQAVASEQ EPNTVVGVMK KGYTLSDRVL RPAMVTVARK EA // ID GPMA_NEIG1 Reviewed; 227 AA. AC Q5F7C0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 70. 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=NGO1258; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89917.1; -; Genomic_DNA. DR RefSeq; WP_003689726.1; NC_002946.2. DR RefSeq; YP_208329.1; NC_002946.2. DR ProteinModelPortal; Q5F7C0; -. DR SMR; Q5F7C0; 3-227. DR PRIDE; Q5F7C0; -. DR EnsemblBacteria; AAW89917; AAW89917; NGO_1258. DR GeneID; 3282177; -. DR KEGG; ngo:NGO1258; -. DR PATRIC; 20335847; VBINeiGon24812_1478. DR HOGENOM; HOG000221682; -. DR OMA; VKNQGKK; -. DR OrthoDB; EOG6C8N1H; -. DR BioCyc; NGON242231:GI2G-1175-MONOMER; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000535; 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_0000229128. 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; 25929 MW; 0EBB181FF18A1F76 CRC64; MELVFIRHGQ SEWNAKNLFT GWRDVKLSEQ GLAEAAAAGK KLKENGYEFD IAFTSVLTRA IKTCNIVLEE SDQLFVPQIK TWRLNERHYG RLQGLDKKQT AEKYGDEQVR IWRRSYDTLP PLLDKDDAFS AHKDRRYAHL PADVVPDGEN LKVTLERVLP FWEDQIAPAI LSGKRVLVAA HGNSLRALAK HIEGISDEDI MGLEIPTGQP LVYKLDDNLK VIEKFYL // ID HIS2_NEIG1 Reviewed; 107 AA. AC Q5FA47; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020}; DE Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020}; DE EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020}; GN Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020}; GN OrderedLocusNames=NGO0185; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-AMP + diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01020}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC {ECO:0000255|HAMAP-Rule:MF_01020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}. CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP- CC Rule:MF_01020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88940.1; -; Genomic_DNA. DR RefSeq; WP_003687491.1; NC_002946.2. DR RefSeq; YP_207352.1; NC_002946.2. DR ProteinModelPortal; Q5FA47; -. DR SMR; Q5FA47; 5-94. DR EnsemblBacteria; AAW88940; AAW88940; NGO_0185. DR GeneID; 3281511; -. DR KEGG; ngo:NGO0185; -. DR PATRIC; 20333297; VBINeiGon24812_0231. DR HOGENOM; HOG000220965; -. DR KO; K01523; -. DR OMA; EQSWTAK; -. DR OrthoDB; EOG6CGCMH; -. DR BioCyc; NGON242231:GI2G-170-MONOMER; -. DR UniPathway; UPA00031; UER00007. DR Proteomes; UP000000535; 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_0000230179. SQ SEQUENCE 107 AA; 11926 MW; 26994DBA991D189E CRC64; MGDSVLSAIQ QTIIQRKSAD PSESYVAQLL HKGEDKILKK VIEEAGEVLM ASKDKDPSHL VYEVADLWFH TMILLTHHDL KAEDVLDELS RRQGLSGLAE KAARTES // ID H82_NEIG1 Reviewed; 88 AA. AC P11910; Q5F818; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Outer membrane protein H.8; DE Flags: Precursor; GN OrderedLocusNames=NGO0983; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DIACYLGLYCEROL AT CYS-18. RX PubMed=2497298; DOI=10.1111/j.1365-2958.1989.tb00102.x; RA Woods J.P., Spinola S.M., Strobel S.M., Cannon J.G.; RT "Conserved lipoprotein H.8 of pathogenic Neisseria consists entirely RT of pentapeptide repeats."; RL Mol. Microbiol. 3:43-48(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X12627; CAA31145.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89669.1; -; Genomic_DNA. DR PIR; S02720; S02720. DR RefSeq; WP_003688296.1; NC_002946.2. DR RefSeq; YP_208081.1; NC_002946.2. DR EnsemblBacteria; AAW89669; AAW89669; NGO_0983. DR GeneID; 3282867; -. DR KEGG; ngo:NGO0983; -. DR PATRIC; 20335166; VBINeiGon24812_1152. DR OMA; CGRTEAP; -. DR OrthoDB; EOG6VTJX8; -. DR BioCyc; NGON242231:GI2G-911-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW Cell outer membrane; Complete proteome; Lipoprotein; Membrane; KW Palmitate; Reference proteome; Repeat; Signal. FT SIGNAL 1 17 FT CHAIN 18 88 Outer membrane protein H.8. FT /FTId=PRO_0000018024. FT REPEAT 23 27 1. FT REPEAT 28 32 2. FT REPEAT 33 37 3. FT REPEAT 38 42 4. FT REPEAT 43 47 5. FT REPEAT 48 52 6. FT REPEAT 53 57 7. FT REPEAT 58 62 8. FT REPEAT 63 67 9. FT REPEAT 68 72 10. FT REPEAT 73 77 11. FT REPEAT 78 82 12. FT REPEAT 83 87 13. FT REGION 23 87 13 X 5 AA tandem repeats of [AS]-[AT]-E- FT A-[PAS]. FT LIPID 18 18 N-palmitoyl cysteine. {ECO:0000305}. FT LIPID 18 18 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303, FT ECO:0000269|PubMed:2497298}. SQ SEQUENCE 88 AA; 8023 MW; 834DDFAE049FCC21 CRC64; MKKSLFAAAL LSLALAACGG EKAAEAPAAE ASSTEAPAAE APAAEAPAAE AAAAEAPAAE APAAEAPAAE AAATEAPAAE APAAEAAK // ID HFQ_NEIG1 Reviewed; 97 AA. AC Q5F9R5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436}; GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=NGO0326; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89072.1; -; Genomic_DNA. DR RefSeq; WP_003687717.1; NC_002946.2. DR RefSeq; YP_207484.1; NC_002946.2. DR ProteinModelPortal; Q5F9R5; -. DR SMR; Q5F9R5; 5-71. DR EnsemblBacteria; AAW89072; AAW89072; NGO_0326. DR GeneID; 3283044; -. DR KEGG; ngo:NGO0326; -. DR PATRIC; 20333643; VBINeiGon24812_0399. DR HOGENOM; HOG000004931; -. DR KO; K03666; -. DR OMA; RRDGHAQ; -. DR OrthoDB; EOG68SW3W; -. DR BioCyc; NGON242231:GI2G-307-MONOMER; -. DR Proteomes; UP000000535; 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_0000265167. SQ SEQUENCE 97 AA; 10783 MW; AC50A6BD4A76FEA1 CRC64; MTAKGQMLQD PFLNALRKEH VPVSIYLVNG IKLQGQVESF DQYVVLLRNT SVTQMVYKHA ISTIVPARSV NLQHENKPQA APASTLVQVE TVQQPAE // ID HIS3_NEIG1 Reviewed; 131 AA. AC Q5FA24; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. 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=NGO0210; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88963.1; -; Genomic_DNA. DR RefSeq; WP_003687532.1; NC_002946.2. DR RefSeq; YP_207375.1; NC_002946.2. DR ProteinModelPortal; Q5FA24; -. DR EnsemblBacteria; AAW88963; AAW88963; NGO_0210. DR GeneID; 3281419; -. DR KEGG; ngo:NGO0210; -. DR PATRIC; 20333357; VBINeiGon24812_0261. DR HOGENOM; HOG000277504; -. DR KO; K01496; -. DR OMA; GPACHTN; -. DR OrthoDB; EOG6PGKB6; -. DR BioCyc; NGON242231:GI2G-193-MONOMER; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000000535; 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_0000229826. 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; 14818 MW; D7CD56B8308BE218 CRC64; MDKNLLEAVK FDEKGLVCAI AQDAETKRVL MVAWMNAEAL QKTVETGFAH YYSRSRQKQW MKGEESGHTQ KVRELRLDCD GDTIVMLIAQ NGGIACHTGR ESCFYKKWNG GAWETADAVL KDEKEIYGST H // ID HEMH_NEIG1 Reviewed; 336 AA. AC Q5F9U6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Ferrochelatase {ECO:0000255|HAMAP-Rule:MF_00323}; DE EC=4.99.1.1 {ECO:0000255|HAMAP-Rule:MF_00323}; DE AltName: Full=Heme synthase {ECO:0000255|HAMAP-Rule:MF_00323}; DE AltName: Full=Protoheme ferro-lyase {ECO:0000255|HAMAP-Rule:MF_00323}; GN Name=hemH {ECO:0000255|HAMAP-Rule:MF_00323}; GN OrderedLocusNames=NGO0293; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. CC {ECO:0000255|HAMAP-Rule:MF_00323}. CC -!- CATALYTIC ACTIVITY: Protoheme + 2 H(+) = protoporphyrin + Fe(2+). CC {ECO:0000255|HAMAP-Rule:MF_00323}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme CC biosynthesis; protoheme from protoporphyrin-IX: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00323}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323}. CC -!- SIMILARITY: Belongs to the ferrochelatase family. CC {ECO:0000255|HAMAP-Rule:MF_00323}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89041.1; -; Genomic_DNA. DR RefSeq; WP_010359848.1; NC_002946.2. DR RefSeq; YP_207453.1; NC_002946.2. DR ProteinModelPortal; Q5F9U6; -. DR DNASU; 3281650; -. DR EnsemblBacteria; AAW89041; AAW89041; NGO_0293. DR GeneID; 3281650; -. DR KEGG; ngo:NGO0293; -. DR PATRIC; 20333567; VBINeiGon24812_0364. DR HOGENOM; HOG000060730; -. DR KO; K01772; -. DR OMA; WEEGSPL; -. DR OrthoDB; EOG6XHC5H; -. DR BioCyc; NGON242231:GI2G-273-MONOMER; -. DR UniPathway; UPA00252; UER00325. DR Proteomes; UP000000535; 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_1000019328. FT METAL 206 206 Iron. {ECO:0000255|HAMAP-Rule:MF_00323}. FT METAL 287 287 Iron. {ECO:0000255|HAMAP-Rule:MF_00323}. SQ SEQUENCE 336 AA; 38061 MW; 541946E610D9FD01 CRC64; MLPFLPEPSL SYTQQNRTAV LLLNLGTPDA PTAQAVRPYL KSFLTDRRIV ELPKWLWYPI LHGLVLTFRP KKSAHAYEKI WFKEGSPLEV YTARQAAALA ERMPDLIVRH AMTYGNPSIA DVLAELKSQG VGRLLAIPLY PQYAASSSGA AVDKVCEQLL LQRNQMSVRT ISRFYDDAGY IDAMKNHILR YWAEHGRGKK LMLSFHGVPQ KHYDLGDPYP DECRHTAKLL AEALELTEDE YTVSFQSQFG RAKWVTPSTQ DLFGKLPKQG VTELDVFCPG FLADCLETME EIALMGREQF YEAGGKNYRY IPCLNDNPDW IDALVALAEE NLGGWR // ID HIS8_NEIG1 Reviewed; 359 AA. AC Q5F7D7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO1241; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89900.1; -; Genomic_DNA. DR RefSeq; WP_003689699.1; NC_002946.2. DR RefSeq; YP_208312.1; NC_002946.2. DR ProteinModelPortal; Q5F7D7; -. DR EnsemblBacteria; AAW89900; AAW89900; NGO_1241. DR GeneID; 3281832; -. DR KEGG; ngo:NGO1241; -. DR PATRIC; 20335801; VBINeiGon24812_1460. DR HOGENOM; HOG000288510; -. DR KO; K00817; -. DR OMA; CYRIFAK; -. DR OrthoDB; EOG6P5ZBR; -. DR BioCyc; NGON242231:GI2G-1153-MONOMER; -. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000000535; 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 1 359 Histidinol-phosphate aminotransferase. FT /FTId=PRO_0000153398. FT MOD_RES 220 220 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01023}. SQ SEQUENCE 359 AA; 39257 MW; B101CA5C0F324686 CRC64; MKSVRSFIRN DILAMSAYKI TDVPPGFAKL DAMESPAHPF EGHEALMREW RAQLASAPIH LYPNPSGCGL QEALRSAFDI PDCAAVALGN GSDELIQFIT MLTAKPGAAM LAAEPGFIMY RHNAALYGMD YVGVPLNGDF TLNLPAVLEA VRKHRPALTF IAYPNNPTGV CFTRAEIEAA IEASDGIVVV DEAYGAFNGD SFLPQAGRIP NLIVLRTLSK IGFAGLRIGY ATGCPEVIGE LQKILPPYNM NQLSLTTAKL ALQHYGIISA NIDSLKNERE RMFAELGKIC RLNAFPSQAN FITIRVPDAD LLFDTLKQNR ILVKKLHGAH PLLEHCLRIT IGSSAQNDAV LDVIRRLYR // ID HEM1_NEIG1 Reviewed; 415 AA. AC Q9ZHD6; Q5F6Y9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-DEC-2015, entry version 109. 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=NGO1403; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9811666; RA Lewis L.A., Sung M., Gipson M., Hartman K., Dyer D.W.; RT "Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin RT utilization system of Neisseria meningitidis."; RL J. Bacteriol. 180:6043-6047(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AF067426; AAC79428.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90048.1; -; Genomic_DNA. DR RefSeq; WP_003689254.1; NC_002946.2. DR RefSeq; YP_208460.1; NC_002946.2. DR ProteinModelPortal; Q9ZHD6; -. DR EnsemblBacteria; AAW90048; AAW90048; NGO_1403. DR GeneID; 3281230; -. DR KEGG; ngo:NGO1403; -. DR PATRIC; 20336209; VBINeiGon24812_1653. DR HOGENOM; HOG000109650; -. DR KO; K02492; -. DR OMA; NHCPNIK; -. DR OrthoDB; EOG6MWNBM; -. DR BioCyc; NGON242231:GI2G-1313-MONOMER; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000000535; 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_0000114044. 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; 45453 MW; 054D366586CEB32F CRC64; MQLTAVGLNH QTAPLSIREK LAFAAAALPE AVRNLARSNA ATEAVILSTC NRTELYCVGD SEEIIRWLAD YHSLPIEEIR PYLYTLDMQE TVRHAFRVAC GLDSMVLGEP QILGQIKDAV RAAQEQESMG AKLNALFQKT FSVAKEVRTD TAVGENSVSM ASASVKLAEQ IFPDIGDLNV LFIGAGEMIE LVATYFAAKN PRLMTVANRT LARAQELCDK LGVNAEPCLL SDLPAILHDY DVVVSSTASQ LPIVGKGMVE RALKQRQSMP LFMLDLAVPR DIEAEVGDLN DAYLYTVDDM VNIVQSGKEA RQKAAAAAET LVSEKVAEFV RQQQGRQSVP LIKALRDEGE KARKQVLENA MKQLAKGATA EEVLERLSVQ LTNKLLHSPT QTLNKAGEED KDLVHAVAQI YHLDK // ID HIS6_NEIG1 Reviewed; 255 AA. AC Q5FA23; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013}; DE EC=4.1.3.- {ECO:0000255|HAMAP-Rule:MF_01013}; DE AltName: Full=IGP synthase cyclase subunit {ECO:0000255|HAMAP-Rule:MF_01013}; DE AltName: Full=IGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013}; DE AltName: Full=ImGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013}; DE Short=IGPS subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013}; GN Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013}; GN OrderedLocusNames=NGO0211; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_01013}. 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 {ECO:0000255|HAMAP-Rule:MF_01013}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC {ECO:0000255|HAMAP-Rule:MF_01013}. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP- CC Rule:MF_01013}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP- CC Rule:MF_01013}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88964.1; -; Genomic_DNA. DR RefSeq; WP_003690707.1; NC_002946.2. DR RefSeq; YP_207376.1; NC_002946.2. DR ProteinModelPortal; Q5FA23; -. DR SMR; Q5FA23; 2-255. DR EnsemblBacteria; AAW88964; AAW88964; NGO_0211. DR GeneID; 3281422; -. DR KEGG; ngo:NGO0211; -. DR PATRIC; 20333359; VBINeiGon24812_0262. DR HOGENOM; HOG000224612; -. DR KO; K02500; -. DR OMA; KGTNFVN; -. DR OrthoDB; EOG6H1Q3W; -. DR BioCyc; NGON242231:GI2G-194-MONOMER; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000535; 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_0000142186. FT ACT_SITE 12 12 {ECO:0000255|HAMAP-Rule:MF_01013}. FT ACT_SITE 131 131 {ECO:0000255|HAMAP-Rule:MF_01013}. SQ SEQUENCE 255 AA; 27058 MW; E2BBB858DAFF9D9E CRC64; MALAKRIIPC LDVKDGRVVK GVNFIGLRDA GDPVEAAKRY NGEGADELTF LDITASSDNR DTILHIIEEV AGQVFIPLTV GGGVRTVADI RRLLNAGADK VSINTAAVTR PDLINEAAGF FGSQAIVAAV DAKAVNPENT RWEIFTHGGR NPTGLDAVEW AVEMQKRGAG EILLTGMDRD GTKQGFNLPL TRAVAEAVDI PVIASGGVGN VRHLIEGITE GKADAVLAAG IFHFGEIAIR EAKRTMREAG IEVRL // ID HIS7_NEIG1 Reviewed; 303 AA. AC Q5F7D6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 16-MAR-2016, entry version 74. 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=NGO1242; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89901.1; 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; AE004969; AAW89901.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F7D6; -. DR SMR; Q5F7D6; 108-289. DR EnsemblBacteria; AAW89901; AAW89901; NGO_1242. DR PATRIC; 20335803; VBINeiGon24812_1461. DR HOGENOM; HOG000228064; -. DR OrthoDB; EOG60PHGP; -. DR BioCyc; NGON242231:GI2G-1154-MONOMER; -. DR UniPathway; UPA00031; UER00011. DR Proteomes; UP000000535; 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 1 303 Imidazoleglycerol-phosphate dehydratase. FT /FTId=PRO_0000336325. SQ SEQUENCE 303 AA; 33523 MW; 8DA3510FAC5DC1D4 CRC64; MTKTQLHLNN FLTLAQEAGS LPKLAKLCGY RTPVALYKLK QRLEKQAEDP DARGIRPSLM AKLEKHTGKP KGWLDRKHRE RTVPETAAES TGTAETRIAE TASAAGCRSV TVNRNTCETQ ITVSINLDGS GKSRLDTGVP FLEHMIDQIA RHGMIDIDIS CKGDLHIDDH HTAEDIGITL GQAIRQALGD KKGIRRYGHS YVPLDEALSR VVIDLSGRPG LVYNIEFTRT LIGRFDVDLF EEFFHGIVNH SMMTLHIDNL SGKNAHHQAE TVFKAFGRAL RMAVEHDPRM AGQTPSTKGT LTA // ID HIS1_NEIG1 Reviewed; 221 AA. AC Q5F7E0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018}; DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018}; DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018}; DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018}; GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; GN OrderedLocusNames=NGO1238; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000255|HAMAP-Rule:MF_01018}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}. 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:0000255|HAMAP-Rule:MF_01018}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89897.1; -; Genomic_DNA. DR RefSeq; WP_003689692.1; NC_002946.2. DR RefSeq; YP_208309.1; NC_002946.2. DR ProteinModelPortal; Q5F7E0; -. DR EnsemblBacteria; AAW89897; AAW89897; NGO_1238. DR GeneID; 3282595; -. DR KEGG; ngo:NGO1238; -. DR PATRIC; 20335795; VBINeiGon24812_1457. DR HOGENOM; HOG000223248; -. DR KO; K00765; -. DR OMA; VATKFPR; -. DR OrthoDB; EOG66MQT3; -. DR BioCyc; NGON242231:GI2G-1150-MONOMER; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000535; 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 1 221 ATP phosphoribosyltransferase. FT /FTId=PRO_0000229320. SQ SEQUENCE 221 AA; 23776 MW; 74D2248667173BD0 CRC64; MQDNALTIAL SKGRIFEETL PLLAAAGIAP TEEPEKSRKL IIGTNHENIR LVIVRATDVP TYVRYGAADF GIAGKDVLIE HGGTGLYRPL DLEIAKCRMM VAVRKGFDYE AASQPGCRLK IATKYPEIAA SHFAGKGVHV DIIKLYGSME LAPLVGLSDA IVDLVSTGNT LKANGLEAVE HIVDISSYLV VNKAALKTKY ALLEPIIQSF GGAVKAKWAF I // ID HLDD_NEIG1 Reviewed; 334 AA. AC Q5F9J0; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0403; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW89147.1; -; Genomic_DNA. DR RefSeq; WP_003687838.1; NC_002946.2. DR RefSeq; YP_207559.1; NC_002946.2. DR ProteinModelPortal; Q5F9J0; -. DR EnsemblBacteria; AAW89147; AAW89147; NGO_0403. DR GeneID; 3283007; -. DR KEGG; ngo:NGO0403; -. DR PATRIC; 20333815; VBINeiGon24812_0485. DR HOGENOM; HOG000167987; -. DR KO; K03274; -. DR OMA; KGRYQSF; -. DR OrthoDB; EOG6384GP; -. DR BioCyc; NGON242231:GI2G-382-MONOMER; -. DR UniPathway; UPA00356; UER00440. DR Proteomes; UP000000535; 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_0000255733. 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; 38373 MW; 72328515E72FFB89 CRC64; MTIIVTGAAG FIGSNIVKAL NQRGITDIVA VDNLTKGEKF KNLAECEIAH YLDKHEFIRQ VREHILPYQN IEAVFHQGAC SDTMNHDGLY MMENNYQYTL DLLDWCQDER IPFLYASSAA VYGKGEIFRE ERELEKPLNV YGYSKFLFDQ VLRRRMKEGL TAQVVGFRYF NVYGQHEQHK GRMASVAFHH FHQYREHGYV NLFGSNDGYG NGEQTRDFVS VEDVAKINLY FFDHPELSGI YNLGTGRSQQ FNELAAAAVN ACRAAEGKSE LSLKELVEEE LIRYIPFPDA LKGKYQGFTQ ADITKLREAG YKEEFFDVKA GVNRYVKWML ENLA // ID HPRK_NEIG1 Reviewed; 320 AA. AC Q5F9S6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO0314; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89061.1; -; Genomic_DNA. DR RefSeq; WP_003687702.1; NC_002946.2. DR RefSeq; YP_207473.1; NC_002946.2. DR ProteinModelPortal; Q5F9S6; -. DR EnsemblBacteria; AAW89061; AAW89061; NGO_0314. DR GeneID; 3281732; -. DR KEGG; ngo:NGO0314; -. DR PATRIC; 20333609; VBINeiGon24812_0384. DR HOGENOM; HOG000099173; -. DR KO; K06023; -. DR OMA; AVRRKMR; -. DR OrthoDB; EOG6F55HT; -. DR BioCyc; NGON242231:GI2G-294-MONOMER; -. DR Proteomes; UP000000535; 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_1000067161. 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; 35857 MW; C0AAB0414E184D9F CRC64; MPSISVRRLF DDNQYKLQLA WAAGNSGADN RIGVEADKPV LALVGHLNFI HPNQIQVVGL AESEYLNRLE SGETGYQFGD LFDISMSLVI VANDLPVSPG LRDYCHKNDI PLLTSKLESP YLMDVLRIYL QRTLAASSVK HGVFLDVFEI GVLITGHSGL GKSELALELI SRGHSLIADD AVELFRIGPE TLEGRCSPML RDFLEVRGLG ILNIRHIFGE TSIRPKKILQ LIINLVEADD EYMKQLDRLS IRTETESILN VNVRSVTLPV AVGRNLAVLV EAAVRNYILQ LRGKDSTREF LERHQTQLKE NEQNHENRPD // ID HIS4_NEIG1 Reviewed; 245 AA. AC Q5FA22; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; DE EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014}; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014}; GN Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014}; GN OrderedLocusNames=NGO0212; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP- CC Rule:MF_01014}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88965.1; -; Genomic_DNA. DR RefSeq; WP_003687535.1; NC_002946.2. DR RefSeq; YP_207377.1; NC_002946.2. DR ProteinModelPortal; Q5FA22; -. DR EnsemblBacteria; AAW88965; AAW88965; NGO_0212. DR GeneID; 3281397; -. DR KEGG; ngo:NGO0212; -. DR PATRIC; 20333361; VBINeiGon24812_0263. DR HOGENOM; HOG000224614; -. DR KO; K01814; -. DR OMA; EWLHLVD; -. DR OrthoDB; EOG6H1Q3W; -. DR BioCyc; NGON242231:GI2G-195-MONOMER; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000535; 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_0000229062. FT ACT_SITE 8 8 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01014}. FT ACT_SITE 131 131 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01014}. SQ SEQUENCE 245 AA; 25865 MW; C6B9D201BA3E6403 CRC64; MLLIPAIDLK EGRCVRLKQG LMEEATVFSD SPADTALHWF EQGARRLHLV DLNGAFAGVP QNLPAIKDIL AAVAKDIPVQ LGGGMRDLKT IGQYLDLGLN DVIIGTAAVK NPDLVREACK AFPGRIIVGL DAKDGMAAID GWATVTGHHV IDLAKRFEDD GVNSIIYTDI GRDGMMSGVN IDATVKLAQS VRIPVIASGG LTGLDDIRAL CAAEKHGVAG AITGRAIYEG SIDFAQAQQL ADSLD // ID HIS5_NEIG1 Reviewed; 212 AA. AC Q5FA21; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE EC=2.4.2.- {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase glutamine amidotransferase subunit {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=IGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE AltName: Full=ImGP synthase subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; DE Short=IGPS subunit HisH {ECO:0000255|HAMAP-Rule:MF_00278}; GN Name=hisH {ECO:0000255|HAMAP-Rule:MF_00278}; GN OrderedLocusNames=NGO0213; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_00278}. 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 {ECO:0000255|HAMAP-Rule:MF_00278}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC {ECO:0000255|HAMAP-Rule:MF_00278}. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP- CC Rule:MF_00278}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00278}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00278}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88966.1; -; Genomic_DNA. DR RefSeq; WP_003687537.1; NC_002946.2. DR RefSeq; YP_207378.1; NC_002946.2. DR ProteinModelPortal; Q5FA21; -. DR MEROPS; C26.965; -. DR EnsemblBacteria; AAW88966; AAW88966; NGO_0213. DR GeneID; 3281167; -. DR KEGG; ngo:NGO0213; -. DR PATRIC; 20333363; VBINeiGon24812_0264. DR HOGENOM; HOG000025030; -. DR KO; K02501; -. DR OMA; GMQMLLT; -. DR OrthoDB; EOG69KV05; -. DR BioCyc; NGON242231:GI2G-196-MONOMER; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000535; 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_0000231736. FT DOMAIN 2 212 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00278}. FT ACT_SITE 85 85 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00278}. FT ACT_SITE 194 194 {ECO:0000255|HAMAP-Rule:MF_00278}. FT ACT_SITE 196 196 {ECO:0000255|HAMAP-Rule:MF_00278}. SQ SEQUENCE 212 AA; 23570 MW; BDDFE90E1A43ED5A CRC64; MQTAIIDYGM GNLHSVLKSV RTAGQLAGKN TKIFLSGDPD RVSRADKVIF PGQGAMPDCM AALTRGGLDE AVKDALKNKP FFGICVGAQL LFDHSEEGNT DGLGWFGGKV RRFARDLRDP QGCRLKVPHM GWNTVRQTQN HPLFQGIPQN TRFYFVHSYY FAPENPETIL GESDYPSPFA CIVGKDNVFA TQFHTEKSHD AGLTMLKNFL NW // ID HISX_NEIG1 Reviewed; 429 AA. AC Q5F7D8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO1240; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89899.1; -; Genomic_DNA. DR RefSeq; WP_003689697.1; NC_002946.2. DR RefSeq; YP_208311.1; NC_002946.2. DR ProteinModelPortal; Q5F7D8; -. DR EnsemblBacteria; AAW89899; AAW89899; NGO_1240. DR GeneID; 3282462; -. DR KEGG; ngo:NGO1240; -. DR PATRIC; 20335799; VBINeiGon24812_1459. DR HOGENOM; HOG000243914; -. DR KO; K00013; -. DR OMA; TEIYRVG; -. DR OrthoDB; EOG6CVVCR; -. DR BioCyc; NGON242231:GI2G-1152-MONOMER; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000535; 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_0000135800. 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; 46381 MW; 1308394D43951E17 CRC64; MKKLNTQSPD FQAGLKALLA FETAQNPETE RIVADICADV QKRGDAALIE YTNKFDQTNA KSIDDLILTQ ADLNAAFERI PNDVQTALQT AARRVESYHQ RQKMESWSYT DEDGTLLGQQ ITPLDRVGIY VPGGKAAYPS SVIMNAMPAH VAGVKEIIMV VPTPKGERND IVLAAAYVAG VTKVFTVGGA QAIAALAYGT ETIPQVDKIT GPGNAFVAAA KRRVFGVVGI DMVAGPSEIL VIADGTTPAD WVAMDLFSQA EHDEIAQAIL IGTSQAYLDE VEAAMDRLIE TMPRRDIIEA SLGNRGAMIL VKDLNEACEI SNYISPEHLE LSVENPQEWA KKIRHAGAIF MGRYTGESLG DYCAGPNHVL PTSRTARFSS PLGTYDFQKR SSLIQVSEQG AQKLGETASV LAHGESLTAH ARAAEFRMK // ID HISZ_NEIG1 Reviewed; 383 AA. AC Q5F9J6; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125}; GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; GN OrderedLocusNames=NGO0397; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for the first step of histidine biosynthesis. CC May allow the feedback regulation of ATP phosphoribosyltransferase CC activity by histidine. {ECO:0000255|HAMAP-Rule:MF_00125}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC {ECO:0000255|HAMAP-Rule:MF_00125}. CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits. CC {ECO:0000255|HAMAP-Rule:MF_00125}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}. 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:0000255|HAMAP-Rule:MF_00125}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89141.1; -; Genomic_DNA. DR RefSeq; WP_003687826.1; NC_002946.2. DR RefSeq; YP_207553.1; NC_002946.2. DR ProteinModelPortal; Q5F9J6; -. DR EnsemblBacteria; AAW89141; AAW89141; NGO_0397. DR GeneID; 3283012; -. DR KEGG; ngo:NGO0397; -. DR PATRIC; 20333801; VBINeiGon24812_0478. DR HOGENOM; HOG000018074; -. DR KO; K02502; -. DR OMA; RADMTTQ; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; NGON242231:GI2G-376-MONOMER; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000535; 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_0000242842. SQ SEQUENCE 383 AA; 41790 MW; 34107E2534E6CAEF CRC64; MQTWQLPEHI ADVLPTNARQ LESAREQLLA LFRVHGYELV QPPLMEYAHS LLTHIDAGLS LKTILVTDRL SGRQLGIRAD ITPQVARIDA HLLSANQGIN RLCYAGPVLH AQPDGLPNMR EPLQAGAEMY GFADIRGDIE LIDLMLKSMK IADMGKVLLS LGHIGIFRAL SDAAHLDAGQ SAALLALMQD KDTGSVEAQV KAWKLDGMWA KAFSLLPRLY GGREVLSDAR GRLPDLSAVG GALDELQAVC DAFPDNEIHI DLSELRVDNY HTGLLYAAYA ADFHDAVARG GRYDGLGGYF GRARPATGFS FDLRSFIGRL PAVERQPAVL VDAEDAEAAR EAVEALREQG QCVVIDYGIG HNVSEELAGR LKKTDGVWQV VKR // ID HSCA_NEIG1 Reviewed; 620 AA. AC Q5F8E8; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679}; GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; GN OrderedLocusNames=NGO0829; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89539.1; -; Genomic_DNA. DR RefSeq; WP_010951132.1; NC_002946.2. DR RefSeq; YP_207951.1; NC_002946.2. DR ProteinModelPortal; Q5F8E8; -. DR SMR; Q5F8E8; 393-619. DR EnsemblBacteria; AAW89539; AAW89539; NGO_0829. DR GeneID; 3282201; -. DR KEGG; ngo:NGO0829; -. DR PATRIC; 20334816; VBINeiGon24812_0978. DR HOGENOM; HOG000228136; -. DR KO; K04044; -. DR OMA; LRGIPAM; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; NGON242231:GI2G-781-MONOMER; -. DR Proteomes; UP000000535; 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. DR PROSITE; PS01036; HSP70_3; 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_0000078633. SQ SEQUENCE 620 AA; 66421 MW; D442DE26A8679F04 CRC64; MALLQISEPG MSAAPHRHRL AAGIDLGTTN SLVATVRSGS AACLPDADGR VTLPSVVRYL ENGGIEVGKT ALSAQKTDPL NTVSSAKRLI GRTLADLHQN THYLPYRFGD NQRFIELHTR QGVKTPVEVS AEILKTLKLR AEETLGGDLV GVVITVPAYF DDAQRQATKD AARLAGLNVL RLLNEPTAAA IAYGLDNASE GTFVVYDLGG GTFDVSVLQL TKGLFEVKAT GGNSALGGDD FDHRLFCYLL EQNRLSQLNE QDSQLLLSLV RAAKEQLTTQ TEARIQATLS DGMAIDTSIS RAEFHNLTQH LVMKTLEPVK QALKDAGVGK NEVKGVVMVG GSTRMPHVQQ AVATFFGQTP LNNLNPDEVV ALGAAIQANV LAGNKADGEW LLLDVTPLSL GLETYGGLAE KIIPRNSTIP TARAQDFTTF KDGQTAMTIH VVQGERELVS DCRSLAKFTL RGIPPMAAGA ARIRVTFQID ADGLLSVSAQ EQSTGVQAQI EVKPSYGLDD DTITQMLKDS MGNAAEDMAA RARAEAVVEA ESLTDAVNAA LELDSDLLDA EEFAQIQRDI ADLQGRLKDG KAEDIRAAVA KLSRSTDNFA AKRMNRNIQR ALTGQSVDNI // ID HSLO_NEIG1 Reviewed; 302 AA. AC Q5F7I8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO1189; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89849.1; -; Genomic_DNA. DR RefSeq; WP_010951210.1; NC_002946.2. DR RefSeq; YP_208261.1; NC_002946.2. DR ProteinModelPortal; Q5F7I8; -. DR EnsemblBacteria; AAW89849; AAW89849; NGO_1189. DR GeneID; 3281975; -. DR KEGG; ngo:NGO1189; -. DR PATRIC; 20335675; VBINeiGon24812_1396. DR HOGENOM; HOG000261998; -. DR KO; K04083; -. DR OMA; DMQCECC; -. DR OrthoDB; EOG651SSJ; -. DR BioCyc; NGON242231:GI2G-1101-MONOMER; -. DR Proteomes; UP000000535; 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_0000238076. 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; 33077 MW; 03F6C4D7BFF769C8 CRC64; MNQTAINRAD ARTRFIFDDM PVRGLHVRLE NVWHHIVKQK NYPAAIRCAL GELLAAGVLL SGNLKNEGTL IVQVQGQGKL KMLVAEATSD RTVRATARWD ETAEIADDES LGDLLGGNGV FVLTLQPKDG EPWQGVVPLE GGSIAQMLVN YMKRSEQLDT HIALSASDEA AGGLLVQRLP EEVLDEEAWE HVSTLARTLT AEELAELDAQ HVLYRLFHET PPRVFEPETF ESSCTCSRGK VSDMLLMLGG EEVGGVVAEQ GSIEVDCDFC HSKYVFDETD VNALFGEDVV GVAKGLPRHT VQ // ID HTPX_NEIG1 Reviewed; 279 AA. AC Q5F9J4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. 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=NGO0399; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89143.1; -; Genomic_DNA. DR RefSeq; WP_010357358.1; NC_002946.2. DR RefSeq; YP_207555.1; NC_002946.2. DR ProteinModelPortal; Q5F9J4; -. DR SMR; Q5F9J4; 58-158. DR MEROPS; M48.002; -. DR EnsemblBacteria; AAW89143; AAW89143; NGO_0399. DR GeneID; 3283010; -. DR KEGG; ngo:NGO0399; -. DR PATRIC; 20333805; VBINeiGon24812_0480. DR HOGENOM; HOG000227302; -. DR KO; K03799; -. DR OMA; QHNSMAG; -. DR OrthoDB; EOG6F55J5; -. DR BioCyc; NGON242231:GI2G-378-MONOMER; -. DR Proteomes; UP000000535; 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_1000020896. 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; 30172 MW; 913484BD6CADD784 CRC64; MKRIFLFLAT NIAVLVVINI VLAVLGINSR GGAGSLLAYS 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 IF1_NEIG1 Reviewed; 72 AA. AC Q5F5U8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, 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=NGO1821.1; ORFNames=NGO18211; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90439.1; -; Genomic_DNA. DR RefSeq; WP_002215452.1; NC_002946.2. DR RefSeq; YP_208851.1; NC_002946.2. DR ProteinModelPortal; Q5F5U8; -. DR SMR; Q5F5U8; 2-72. DR EnsemblBacteria; AAW90439; AAW90439; NGO_18211. DR GeneID; 23781882; -. DR GeneID; 3282427; -. DR KEGG; ngo:NGO18211; -. DR PATRIC; 20337306; VBINeiGon24812_2188. DR HOGENOM; HOG000221323; -. DR KO; K02518; -. DR OMA; HHITILR; -. DR OrthoDB; EOG6384SC; -. DR BioCyc; NGON242231:GI2G-1719-MONOMER; -. DR Proteomes; UP000000535; 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_0000095831. 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 IF2_NEIG1 Reviewed; 943 AA. AC Q5F797; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO1286; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89940.1; -; Genomic_DNA. DR RefSeq; WP_010951232.1; NC_002946.2. DR RefSeq; YP_208352.1; NC_002946.2. DR ProteinModelPortal; Q5F797; -. DR PRIDE; Q5F797; -. DR EnsemblBacteria; AAW89940; AAW89940; NGO_1286. DR GeneID; 3282010; -. DR KEGG; ngo:NGO1286; -. DR PATRIC; 20335915; VBINeiGon24812_1512. DR HOGENOM; HOG000076907; -. DR KO; K02519; -. DR OMA; KFAVVES; -. DR OrthoDB; EOG67HJSV; -. DR BioCyc; NGON242231:GI2G-1198-MONOMER; -. DR Proteomes; UP000000535; 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 1 943 Translation initiation factor IF-2. FT /FTId=PRO_0000228216. FT DOMAIN 443 612 tr-type G. FT NP_BIND 452 459 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT NP_BIND 498 502 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT NP_BIND 552 555 GTP. {ECO:0000255|HAMAP-Rule:MF_00100}. FT REGION 452 459 G1. {ECO:0000250}. FT REGION 477 481 G2. {ECO:0000250}. FT REGION 498 501 G3. {ECO:0000250}. FT REGION 552 555 G4. {ECO:0000250}. FT REGION 588 590 G5. {ECO:0000250}. SQ SEQUENCE 943 AA; 101018 MW; 5658682DFF512CC2 CRC64; MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KNSGSDSLTL DDKQLLNAYL TKKNGSNGGT ISIRRTKTEV STVDGVKVET RKRGRTVNIP SAEELAAQVK AAQTQAAPVQ PEQTAEDAVK ARAEAAARAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEPKEK AVKPKHERNG KGKDAKKPAK PAAPAVPQPV VSAEEQAQRD EEARRAAALR AHQEALLKEK QERQARREAM KQQAEQQAKA AQEAKTGRQR PAKPAEKPQA AAPAVENKPV NPAKAKKEDR RNRDDEGQGR NAKGKGAKGG RDRNNARNGG DERVRGGKKG KKLKLEPNQH AFQAPTEPVV HEVLVPETIT VADLAHKMAV KGVEMVKALM KKGMMVTINQ SIDQDTALIV VKKLGHIGKP AAADDPEAFL GEGAEAEEAE ALPRPPVVTV MGHVDHGKTS LLDYIRRAKV VQGEAGGITQ HIGAYHVKTP RGVITFLDTP GHEAFTAMRA RGAKATDIVI LVVAADDGVM PQTIEAIAHA KAAGVPIVVA VNKIDKDTAN PERIRQELTQ HEVIPDDWGG TVQFIDVSAK KGTNIDALLE AVLLEAEVLE LTAPVDAPAK GIIVEARLDK GRGAVATLLV QNGTLKKGDM LLAGTAFGKI RAMVDENGKS ITEAGPSIPV EILGLSDVPN AGEDAMVLAD EKKAREIALF RQGKYRDVRL AKQQAAKLEN MFNNMGETQA QSLSVIIKAD VQGSYEALAG SLKKLSADEV KVNVLHSGVG GITESDVNLA IASGAFIIGF NVRADASSRK LAENENVEIR YYNIIYDAID DVKAAMSGML SPEKKEQVTG TVEIRQVISV SKVGNIAGCM VTDGVVKRDS HIRLIRNNVV IHTGELASLK RYKDDVKEVR MGFECGLMLK GYNEIMEGDQ LECFDIVEVA RTL // ID ILVC_NEIG1 Reviewed; 337 AA. AC Q5F7E5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Ketol-acid reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435}; DE EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435}; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435}; GN Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435}; GN OrderedLocusNames=NGO1233; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP- CC Rule:MF_00435}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00435}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89892.1; -; Genomic_DNA. DR RefSeq; WP_003689683.1; NC_002946.2. DR RefSeq; YP_208304.1; NC_002946.2. DR ProteinModelPortal; Q5F7E5; -. DR SMR; Q5F7E5; 1-326. DR EnsemblBacteria; AAW89892; AAW89892; NGO_1233. DR GeneID; 3282497; -. DR KEGG; ngo:NGO1233; -. DR PATRIC; 20335783; VBINeiGon24812_1450. DR HOGENOM; HOG000016230; -. DR KO; K00053; -. DR OMA; EPNIKQG; -. DR OrthoDB; EOG625K07; -. DR BioCyc; NGON242231:GI2G-1144-MONOMER; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000535; 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_0000226183. FT ACT_SITE 106 106 {ECO:0000255|HAMAP-Rule:MF_00435}. SQ SEQUENCE 337 AA; 36417 MW; 51CF40175F6B2F5C CRC64; MQVYYDKDAD LSLIKGKTVA IIGYGSQGHA HAANLKDSGV NVVIGLRHGS SWKKAEAAGH VVKTVAEATK EADVVMLLLP DETMPAVYHA EVAANLKEGA TLAFAHGFNV HYNQIVPRAD LDVIMVAPKG PGHTVRSEYK RGGGVPSLIA VYQDNSGKAK DIALSYAAAN GGTKGGVIET TFREETETDL FGEQAVLCGG VAELIKAGFE TLTEAGYAPE MAYFECLHEM KLIVDLIFEG GIANMNYSIS NNAEYGEYVT GPEVVNASSK EAMRNALKRI QTGEYAKMFI QEGNVNYASM TARRRLNADH QVEKVGARLR AMMPWITANK LVDQDKN // ID IF3_NEIG1 Reviewed; 173 AA. AC Q5F9U3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO0296; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89044.1; -; Genomic_DNA. DR RefSeq; WP_010951024.1; NC_002946.2. DR RefSeq; YP_207456.1; NC_002946.2. DR ProteinModelPortal; Q5F9U3; -. DR SMR; Q5F9U3; 6-81, 86-173. DR EnsemblBacteria; AAW89044; AAW89044; NGO_0296. DR GeneID; 3281674; -. DR KEGG; ngo:NGO0296; -. DR PATRIC; 20333575; VBINeiGon24812_0367. DR HOGENOM; HOG000035157; -. DR KO; K02520; -. DR OMA; HDFNVKV; -. DR OrthoDB; EOG63JRGJ; -. DR BioCyc; NGON242231:GI2G-277-MONOMER; -. DR Proteomes; UP000000535; 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_1000004546. 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 ILVD_NEIG1 Reviewed; 619 AA. AC Q5F8G6; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; GN OrderedLocusNames=NGO0809; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89521.1; -; Genomic_DNA. DR RefSeq; WP_003688598.1; NC_002946.2. DR RefSeq; YP_207933.1; NC_002946.2. DR EnsemblBacteria; AAW89521; AAW89521; NGO_0809. DR GeneID; 3281902; -. DR KEGG; ngo:NGO0809; -. DR PATRIC; 20334776; VBINeiGon24812_0958. DR HOGENOM; HOG000173155; -. DR KO; K01687; -. DR OMA; QGRNMAG; -. DR OrthoDB; EOG6MSS24; -. DR BioCyc; NGON242231:GI2G-763-MONOMER; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000000535; 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_0000225398. 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; 66842 MW; CE3227FFF3065E8E 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 EQDDETVLPR SIATKKAFEN AMTMDIAMGG STNTILHLLA VANEAGVDFK MADIDRLSRV VPCICKTAPN NHDYYMEDVH RAGGIFAILK ELDKAGKLHT DVYTIHAPTL KDAIEKWDVT NPENTRAIER FKAAPGGVRT TQAFSQNRIW KTLDLDREKG CIRDVAHAYS QDGGLAVLFG NIAERGCVVK TAGVDESILK FTGRARVFES QEAAVEGILG NQIVAGNIVI IRYEGPKGGP GMQEMLYPTS YLKSKGLGKA CALLTDGRFS GGTSGLSIGH ASPEAAEGGA IGLVHEGDTI EIDIPKRSIR LVISDEELAA RRAEMEARGS KAWKPENRDR YVSAALRAYG AMATSADKGA VRDVSQIER // ID IHFA_NEIG1 Reviewed; 100 AA. AC Q5F9T5; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=Integration host factor subunit alpha {ECO:0000255|HAMAP-Rule:MF_00380}; DE Short=IHF-alpha {ECO:0000255|HAMAP-Rule:MF_00380}; GN Name=ihfA {ECO:0000255|HAMAP-Rule:MF_00380}; GN Synonyms=himA {ECO:0000255|HAMAP-Rule:MF_00380}; GN OrderedLocusNames=NGO0305; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP-Rule:MF_00380}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC {ECO:0000255|HAMAP-Rule:MF_00380}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000255|HAMAP-Rule:MF_00380}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89052.1; -; Genomic_DNA. DR RefSeq; WP_003687686.1; NC_002946.2. DR RefSeq; YP_207464.1; NC_002946.2. DR ProteinModelPortal; Q5F9T5; -. DR SMR; Q5F9T5; 3-94. DR EnsemblBacteria; AAW89052; AAW89052; NGO_0305. DR GeneID; 3281528; -. DR KEGG; ngo:NGO0305; -. DR PATRIC; 20333591; VBINeiGon24812_0375. DR HOGENOM; HOG000043829; -. DR KO; K04764; -. DR OMA; FDLRDKK; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NGON242231:GI2G-285-MONOMER; -. DR Proteomes; UP000000535; 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_0000277747. SQ SEQUENCE 100 AA; 11392 MW; 4ADE1DDD5A1CF982 CRC64; MTLTKAELAD ILVDKVSNVT KNDAKEIVEL FFEEIRSTLA SGEEIKISGF GNFQLRDKPQ RPGRNPKTGE EVPITARRVV TFHASQKLKG MVEHYYDKQR // ID ISCS_NEIG1 Reviewed; 404 AA. AC Q5F8X4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO0636; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89363.1; -; Genomic_DNA. DR RefSeq; WP_003688882.1; NC_002946.2. DR RefSeq; YP_207775.1; NC_002946.2. DR ProteinModelPortal; Q5F8X4; -. DR SMR; Q5F8X4; 4-391. DR EnsemblBacteria; AAW89363; AAW89363; NGO_0636. DR GeneID; 3281390; -. DR KEGG; ngo:NGO0636; -. DR PATRIC; 20334356; VBINeiGon24812_0750. DR HOGENOM; HOG000017510; -. DR KO; K04487; -. DR OMA; EPIQSGG; -. DR OrthoDB; EOG62RSBK; -. DR BioCyc; NGON242231:GI2G-603-MONOMER; -. DR UniPathway; UPA00266; -. DR Proteomes; UP000000535; 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_1000019417. 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; 44578 MW; 88D9E6DDE319319E CRC64; MTVKTPVYLD YAATTPVDKR VAEKMIPYLT ETFGNPASNS HAFGWTAEEA VEKARADIAA LINADPKEIV FTSGATESDN LAIKGAANFY KTKGKHLITV KTEHKAVLDT MRELERQGFE VTYLGVQENG LIDLEELKAA IRDDTILISI MWVNNEIGVV QNIPAIGEIC RERKIAFHVD AAQACGKVPV DVEAAKIDLL SMSAHKVYGP KGIGALYVRR KPRVRLEAQM HGGGHERGFR SGTLPTHQIV GMGEAFRIAK EELAQDTAHY LKLRDIFLKG IEGIEEVYIN GDLEHRAPNN LNVSFNFVEG ESLIMAVKEL AVSSGSACTS ASLEPSYVLR ALGRNDELAH SSLRITFGRM TTEEEVQFAA ELIKSKIGKL RELSPLWEMF KDGIDLNSIE WAAH // ID ISPT_NEIG1 Reviewed; 248 AA. AC Q5F5X2; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1797; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90415.1; -; Genomic_DNA. DR RefSeq; WP_003690027.1; NC_002946.2. DR RefSeq; YP_208827.1; NC_002946.2. DR ProteinModelPortal; Q5F5X2; -. DR EnsemblBacteria; AAW90415; AAW90415; NGO_1797. DR GeneID; 3282548; -. DR KEGG; ngo:NGO1797; -. DR PATRIC; 20337244; VBINeiGon24812_2157. DR HOGENOM; HOG000006054; -. DR KO; K00806; -. DR OMA; WNRPKLE; -. DR OrthoDB; EOG68H89T; -. DR BioCyc; NGON242231:GI2G-1695-MONOMER; -. DR Proteomes; UP000000535; 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 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_0000123642. 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; 28345 MW; 3DA4CB80525DE717 CRC64; MKSSTQTILE HTAIPRHIAV IMDGNGRWAK KRFLPRIMGH KRGLDALENM VKHCAKLGVQ YLTVFAFSTE NWRRPEDEVS FLMGLFLQAL QKQVRRLHEN NMRLKILGSR ERFNRQILQG IEEAEALTAN NTGLTLSIAA DYGGRWDILQ AANKLIAEGV SEITEDTLAK HLMLGDAPEP DLFIRTGGET RISNFLLWQM AYAELYFTDI LWPDFDETAL DAAVASFQKR ERRFGRTSEQ LPIGQQRN // ID ISPG_NEIG1 Reviewed; 421 AA. AC Q5F913; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0594; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89324.1; -; Genomic_DNA. DR RefSeq; WP_003688953.1; NC_002946.2. DR RefSeq; YP_207736.1; NC_002946.2. DR ProteinModelPortal; Q5F913; -. DR EnsemblBacteria; AAW89324; AAW89324; NGO_0594. DR GeneID; 3281243; -. DR KEGG; ngo:NGO0594; -. DR PATRIC; 20334262; VBINeiGon24812_0703. DR HOGENOM; HOG000261017; -. DR KO; K03526; -. DR OMA; HNGMKIA; -. DR OrthoDB; EOG67Q96Z; -. DR BioCyc; NGON242231:GI2G-564-MONOMER; -. DR UniPathway; UPA00056; UER00096. DR Proteomes; UP000000535; 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_0000190603. 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; 45368 MW; 7480AAC5562C84B4 CRC64; MNTLQRRKTH QVLIDHITVG SEAPVVIQSM TNTDTADAKA TALQIKELSD AGSEMVRITV NSPEAASKVA EIRRRLDDMG YATPLIGDFH FNGERLLAEF PECGKALSKY RINPGNVGKG VKGDEKFAFM IRTAAENDKA VRIGVNWGSL DQSLAKRMMD ANLVSSAPKP PEEVMKEALI VSALESAEKA VLLGLPEDKI ILSCKVSAVH DLIQVYRELG SRCVYPLHLG LTEAGMGSKG IVASTAALSV LLQEGIGDTI RISLTPEPGS PRTQEVVVGQ EILQTMGLRS FTPMVTACPG CGRTTSTVFQ ELAQDVQNYL RQKMSIWRTL YPGVESLNVA VMGCVVNGPG ESKLADIGIS LPGTGETPVA PVYVDGERKV TLKGNNIASE FLAIVEEYVK TNYGKNSSKR NKGKVIPIQS L // ID ISPH_NEIG1 Reviewed; 322 AA. AC Q5FAF2; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. 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}; GN OrderedLocusNames=NGO0072; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88835.1; -; Genomic_DNA. DR RefSeq; WP_010356621.1; NC_002946.2. DR RefSeq; YP_207247.1; NC_002946.2. DR DNASU; 3282290; -. DR EnsemblBacteria; AAW88835; AAW88835; NGO_0072. DR GeneID; 3282290; -. DR KEGG; ngo:NGO0072; -. DR PATRIC; 20333018; VBINeiGon24812_0093. DR HOGENOM; HOG000220192; -. DR KO; K03527; -. DR OMA; DDLTFMT; -. DR OrthoDB; EOG6HF624; -. DR BioCyc; NGON242231:GI2G-64-MONOMER; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000535; 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_0000128843. 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; 35141 MW; 8C41368DF0033B13 CRC64; MNGKTIILAN PRGFCAGVDR AISIVERALE EFGAPVYVRH EVVHNKFVVD NLREKGAVFI EDLAEVPPGA TLVYSAHGVS KAVQQEAAER GFRVFDATCP LVTKVHKEVA RLDAQDCEII MIGHKGHAEV EGTMGQLAPG KMLLVETVGD VAKLEVRNPD KLAYVSQTTL SVDETKDIIA ALNARFPNIR NPHKEDICYA TTNRQTAVKE LAEQCDIVIV VGSPNSSNSN RLREVAASRG IDAYMVDNAS YLQRTWFEGK SKVGVTAGAS APEVLVREVL ATIRGWGHET VREGGGAEES IVFVLPKELR REGETKPDLC KR // ID ISPD_NEIG1 Reviewed; 229 AA. AC Q5F829; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO0972; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89658.1; -; Genomic_DNA. DR RefSeq; WP_003693342.1; NC_002946.2. DR RefSeq; YP_208070.1; NC_002946.2. DR PDB; 1VGW; X-ray; 2.35 A; A/B/C/D/E/F=2-229. DR PDB; 1VGZ; X-ray; 3.00 A; A/B=2-229. DR PDBsum; 1VGW; -. DR PDBsum; 1VGZ; -. DR ProteinModelPortal; Q5F829; -. DR SMR; Q5F829; 1-227. DR EnsemblBacteria; AAW89658; AAW89658; NGO_0972. DR GeneID; 3281402; -. DR KEGG; ngo:NGO0972; -. DR PATRIC; 20335138; VBINeiGon24812_1138. DR HOGENOM; HOG000218564; -. DR KO; K00991; -. DR OMA; QAYTPQM; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NGON242231:GI2G-900-MONOMER; -. DR UniPathway; UPA00056; UER00093. DR EvolutionaryTrace; Q5F829; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isoprene biosynthesis; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 229 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. FT /FTId=PRO_0000237799. 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}. FT STRAND 5 10 {ECO:0000244|PDB:1VGW}. FT HELIX 34 43 {ECO:0000244|PDB:1VGW}. FT STRAND 50 54 {ECO:0000244|PDB:1VGW}. FT HELIX 62 68 {ECO:0000244|PDB:1VGW}. FT STRAND 72 75 {ECO:0000244|PDB:1VGW}. FT HELIX 82 96 {ECO:0000244|PDB:1VGW}. FT STRAND 97 99 {ECO:0000244|PDB:1VGW}. FT STRAND 103 107 {ECO:0000244|PDB:1VGW}. FT HELIX 117 127 {ECO:0000244|PDB:1VGW}. FT STRAND 134 139 {ECO:0000244|PDB:1VGW}. FT STRAND 144 156 {ECO:0000244|PDB:1VGW}. FT STRAND 161 171 {ECO:0000244|PDB:1VGW}. FT HELIX 172 180 {ECO:0000244|PDB:1VGW}. FT HELIX 190 195 {ECO:0000244|PDB:1VGW}. FT TURN 196 198 {ECO:0000244|PDB:1VGW}. FT STRAND 202 205 {ECO:0000244|PDB:1VGW}. FT HELIX 216 225 {ECO:0000244|PDB:1VGW}. SQ SEQUENCE 229 AA; 24467 MW; 49E86A75051231A9 CRC64; MKRKNIALIP AAGIGVRFGA DKPKQYVEIG SKTVLEHVLG IFERHEAVDL TVVVVSPEDT FADKVQTAFP QVRVWKNGGQ TRAETVRNGV AKLLETGLAA ETDNILVHDA ARCCLPSEAL ARLIEQAGNA AEGGILAVPV ADTLKRAESG QISATVDRSG LWQAQTPQLF QAGLLHRALA AENLGGITDE ASAVEKLGVR PLLIQGDARN LKLTQPQDAY IVRLLLNAV // ID ISPE_NEIG1 Reviewed; 281 AA. AC Q5F9F6; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0440; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89181.1; -; Genomic_DNA. DR RefSeq; WP_010951042.1; NC_002946.2. DR RefSeq; YP_207593.1; NC_002946.2. DR ProteinModelPortal; Q5F9F6; -. DR EnsemblBacteria; AAW89181; AAW89181; NGO_0440. DR GeneID; 3282196; -. DR KEGG; ngo:NGO0440; -. DR PATRIC; 20333902; VBINeiGon24812_0527. DR HOGENOM; HOG000019601; -. DR KO; K00919; -. DR OMA; RWPSPAK; -. DR OrthoDB; EOG62VNQ2; -. DR BioCyc; NGON242231:GI2G-417-MONOMER; -. DR UniPathway; UPA00056; UER00094. DR Proteomes; UP000000535; 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_0000235105. 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; 30989 MW; 72AFC3A78B4922BB CRC64; MNIADGRQAF PAPAKLNLDL RITGRREDGY HNIESIFCLI DLQDTVYLKP RDDGKIILHN PVGGIPQEAD LSYRAASLLQ KYARNLAGVE IWLDKKIPTG AGLGGGSSDA ATVLLVLNRW WQCGLTQWQL IDLGAALGAD VPFFIFGKNA FASGIGKKLI GMDIPKQWYV IVKPPVHVST AKIFTYEGLT RDSASSIMPT FQNLQPFRND MQAVVFKEYP EVWKAYSELS KYGSAMMTGS GACIFAAFQA RNSAYNIYRQ VSGLYEAYLA EGLSKHPLLS V // ID KDSA_NEIG1 Reviewed; 280 AA. AC Q5F8Z0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. 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=NGO0619; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89347.1; -; Genomic_DNA. DR RefSeq; WP_003688911.1; NC_002946.2. DR RefSeq; YP_207759.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z0; -. DR SMR; Q5F8Z0; 1-277. DR EnsemblBacteria; AAW89347; AAW89347; NGO_0619. DR GeneID; 3282895; -. DR KEGG; ngo:NGO0619; -. DR PATRIC; 20334322; VBINeiGon24812_0733. DR HOGENOM; HOG000023021; -. DR KO; K01627; -. DR OMA; PIATDIH; -. DR OrthoDB; EOG680X4R; -. DR BioCyc; NGON242231:GI2G-587-MONOMER; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00357; UER00474. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipopolysaccharide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 280 2-dehydro-3-deoxyphosphooctonate FT aldolase. FT /FTId=PRO_0000304460. SQ SEQUENCE 280 AA; 30516 MW; 85F9A349A9B740BA CRC64; MDIKINDITL GNNSPFVLFG GINVLEDLDS TLQTCAHYVE VTRKLGIPYI FKASFDKANR SSIHSYRGVG LEEGLKIFEK VKAEFGIPVI TDVHEPHQCQ PVAEVCDVIQ LPAFLARQTD LVAAMAETGN VINIKKPQFL SPSQMKNIVE KFREAGNGKL ILCERGSSFG YDNLVVDMLG FGVMKQTCGN LPVIFDVTHS LQTRDAGSAA SGGRRAQALD LALAGMATRL AGLFLESHPD PKLAKCDGPS ALPLHLLENF LIRIKALDDL IKSQPILTIE // ID ISPF_NEIG1 Reviewed; 160 AA. AC Q5F830; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO0971; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89657.1; -; Genomic_DNA. DR RefSeq; WP_010951155.1; NC_002946.2. DR RefSeq; YP_208069.1; NC_002946.2. DR ProteinModelPortal; Q5F830; -. DR SMR; Q5F830; 3-159. DR EnsemblBacteria; AAW89657; AAW89657; NGO_0971. DR GeneID; 3281114; -. DR KEGG; ngo:NGO0971; -. DR PATRIC; 20335136; VBINeiGon24812_1137. DR HOGENOM; HOG000239175; -. DR KO; K01770; -. DR OMA; IRIGNGY; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NGON242231:GI2G-899-MONOMER; -. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000000535; 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_0000237734. 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; 17048 MW; 9C2224C1C4C6B02D CRC64; MTNIRIGQGY DVHQLTEGRK LILGGVEIPF EKGLLGHSDA DALLHAVTDA LLGAAGLGDI GSHFPDTAAE FKDADSRVLL RAAYQSVQAQ GWQVVNVDTT VIAQKPKLAP HIPQMRANIA ADLGIDISCV NIKGKTNEKL GYLGRMEGIE AQAAVLLVRI // ID KAD_NEIG1 Reviewed; 215 AA. AC Q5F9J3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0400; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89144.1; -; Genomic_DNA. DR RefSeq; WP_003687832.1; NC_002946.2. DR RefSeq; YP_207556.1; NC_002946.2. DR ProteinModelPortal; Q5F9J3; -. DR SMR; Q5F9J3; 1-214. DR EnsemblBacteria; AAW89144; AAW89144; NGO_0400. DR GeneID; 3283009; -. DR KEGG; ngo:NGO0400; -. DR PATRIC; 20333809; VBINeiGon24812_0482. DR HOGENOM; HOG000238772; -. DR KO; K00939; -. DR OMA; RTPEQVI; -. DR OrthoDB; EOG679TH4; -. DR BioCyc; NGON242231:GI2G-379-MONOMER; -. DR UniPathway; UPA00588; UER00649. DR Proteomes; UP000000535; 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_1000058862. 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; 23124 MW; 24629AA075539BED CRC64; MKALLLGAPG AGKGTQAQFI TAAFGIPQIS TGDMLRAAIK AGTPLGLEAK KIIDEGGLVR DDIIIGMVKE RIAQDDCKNG FLFDGFPRTL AQAEAMVEAG VGLDAVVEID VSDSVIVDRM SGRRVHLASG RTYHVTYNPP KTEGKDDVTG EDLIQRDDDK EETVKKRLAV YHEQTEVLVD FYSKLEGEHA PKYIKVDGTQ AVEAVKAEVL GALGK // ID KDSB_NEIG1 Reviewed; 253 AA. AC Q5F9Y9; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0245; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88998.1; -; Genomic_DNA. DR RefSeq; WP_003690726.1; NC_002946.2. DR RefSeq; YP_207410.1; NC_002946.2. DR ProteinModelPortal; Q5F9Y9; -. DR SMR; Q5F9Y9; 3-249. DR EnsemblBacteria; AAW88998; AAW88998; NGO_0245. DR GeneID; 3281505; -. DR KEGG; ngo:NGO0245; -. DR PATRIC; 20333441; VBINeiGon24812_0302. DR HOGENOM; HOG000007602; -. DR KO; K00979; -. DR OMA; NSGTERC; -. DR OrthoDB; EOG6KT2SK; -. DR BioCyc; NGON242231:GI2G-229-MONOMER; -. DR UniPathway; UPA00030; -. DR UniPathway; UPA00358; UER00476. DR Proteomes; UP000000535; 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_0000370101. SQ SEQUENCE 253 AA; 27723 MW; 4EAD5340D439BBD1 CRC64; MTEFVVLIPA RLDSSRLPGK ALADIHGKPM VVRVAEQAAK SKAARVVVAT DHPDIQTACQ AHGIEVVMTS NRHESGTTRL AEAAAALKLP PHLIVVNVQG DEPLIAPELI DRTAEVLVEN NVQMATAGHE LHDFDELMNP NAVKVVLDKN GNAIYFSRAP IPYPRDAMRA GKREMPSETA VLRHIGIYAY RVGFLQRYAE MSVSPLETIE SLEQLRVLWH GYPIAVETAK EAPAAGVDTQ EDLDRVRAVF QTV // ID KCY_NEIG1 Reviewed; 218 AA. AC Q5F904; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO0605; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89333.1; -; Genomic_DNA. DR RefSeq; WP_003688932.1; NC_002946.2. DR RefSeq; YP_207745.1; NC_002946.2. DR ProteinModelPortal; Q5F904; -. DR EnsemblBacteria; AAW89333; AAW89333; NGO_0605. DR GeneID; 3281500; -. DR KEGG; ngo:NGO0605; -. DR PATRIC; 20334288; VBINeiGon24812_0716. DR HOGENOM; HOG000242849; -. DR KO; K00945; -. DR OMA; LKIFMTA; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NGON242231:GI2G-573-MONOMER; -. DR Proteomes; UP000000535; 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_1000048240. FT NP_BIND 11 19 ATP. {ECO:0000255|HAMAP-Rule:MF_00238}. SQ SEQUENCE 218 AA; 24027 MW; F921E92A799AF0C0 CRC64; MNRQKVIAID GPGASGKGTV AARVAAALGY DYLDTGALYR LTALYAQKQG VEWHDEENVS ALAKKLPAVF SGNRILLDGE DVSDGIRTEA IGMGASAVAQ WPKVRAALLQ RQRDFLTEKG LVADGRDTGS VVFPQAELKI FLTAESKIRA ERRAKQIGIP CEGFTFERIL SDIETRDEAD RNRKVAPLKQ QPDALLLDTS RLTIEETVKK VLDWYRKV // ID KGUA_NEIG1 Reviewed; 205 AA. AC Q5F775; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=Guanylate kinase {ECO:0000255|HAMAP-Rule:MF_00328}; DE EC=2.7.4.8 {ECO:0000255|HAMAP-Rule:MF_00328}; DE AltName: Full=GMP kinase {ECO:0000255|HAMAP-Rule:MF_00328}; GN Name=gmk {ECO:0000255|HAMAP-Rule:MF_00328}; OrderedLocusNames=NGO1310; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential for recycling GMP and indirectly, cGMP. CC {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- CATALYTIC ACTIVITY: ATP + GMP = ADP + GDP. {ECO:0000255|HAMAP- CC Rule:MF_00328}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- SIMILARITY: Belongs to the guanylate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00328}. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC {ECO:0000255|HAMAP-Rule:MF_00328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89962.1; -; Genomic_DNA. DR RefSeq; WP_003691634.1; NC_002946.2. DR RefSeq; YP_208374.1; NC_002946.2. DR ProteinModelPortal; Q5F775; -. DR EnsemblBacteria; AAW89962; AAW89962; NGO_1310. DR GeneID; 3281823; -. DR KEGG; ngo:NGO1310; -. DR PATRIC; 20335981; VBINeiGon24812_1541. DR HOGENOM; HOG000037640; -. DR KO; K00942; -. DR OMA; MEGVKQI; -. DR OrthoDB; EOG6CP410; -. DR BioCyc; NGON242231:GI2G-1225-MONOMER; -. DR Proteomes; UP000000535; 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_0000266356. FT DOMAIN 7 185 Guanylate kinase-like. FT {ECO:0000255|HAMAP-Rule:MF_00328}. FT NP_BIND 14 21 ATP. {ECO:0000255|HAMAP-Rule:MF_00328}. SQ SEQUENCE 205 AA; 22488 MW; 1D10D9EDDD535795 CRC64; MSAYRKGNIF IISAASGTGK TTLVSRLLAN HNGLRVSVSH TTRPPREGEA NGVHYHFVSK EEFESLIAQE AFLEYADVFG NYYGTSTEGV NALAAAGYDV ILEIDVQGAA QVRNALPEAV GIFILPPSFD VLAARLKGRG TDSREVIQRR LSKARHEIEQ SVLFDFVVVN DDLEKAEGDL LHIVNACRLK RSRQLGFIAD LLENS // ID LEU3_NEIG1 Reviewed; 356 AA. AC Q5F8T6; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. 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=NGO0674; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89401.1; -; Genomic_DNA. DR RefSeq; WP_003697157.1; NC_002946.2. DR RefSeq; YP_207813.1; NC_002946.2. DR ProteinModelPortal; Q5F8T6; -. DR PRIDE; Q5F8T6; -. DR EnsemblBacteria; AAW89401; AAW89401; NGO_0674. DR GeneID; 3282023; -. DR KEGG; ngo:NGO0674; -. DR PATRIC; 20334446; VBINeiGon24812_0795. DR HOGENOM; HOG000021112; -. DR KO; K00052; -. DR OMA; HCGPEVV; -. DR OrthoDB; EOG65N1BN; -. DR BioCyc; NGON242231:GI2G-641-MONOMER; -. DR UniPathway; UPA00048; UER00072. DR Proteomes; UP000000535; 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_0000083709. 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; 39041 MW; 9EAD738A9F333C4B CRC64; MTKHIAILRG DGIGPEIVAE TVRVLDKFIA QGLDADYEYA PLGGEAYDEY GHPYPEFTQN LCRKADAVLL GAVGSPQYDN LDRPLRPERG LLAIRKDLNL FANLRPAVLY PELANASTLK PEIVAGLDIL IVRELTGDIY FGEPRGIRVL ENGEHEGYNT MKYSESEIRR IAHVAFQSAQ KRSKKVCSVG KANVLETTEL WREIFEEIGK QYPDVELSHM YVDNAAMQLV RAPKQFDVIA TGNIFGDILS DEASMLTGSI GMLPSASLDE NGKGLYEPSH GSAPDIAGQN KANPLATILS LAMLLRYSLN DEARAQQVEN SVQKVLQQGL RTGDIYEEGT KLVSCSEMGD AVLAAL // ID KTHY_NEIG1 Reviewed; 206 AA. AC Q5F9Z5; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165}; DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165}; DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165}; GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=NGO0239; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and CC salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP- CC Rule:MF_00165}. CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. {ECO:0000255|HAMAP- CC Rule:MF_00165}. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00165}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88992.1; -; Genomic_DNA. DR RefSeq; WP_003687582.1; NC_002946.2. DR RefSeq; YP_207404.1; NC_002946.2. DR ProteinModelPortal; Q5F9Z5; -. DR EnsemblBacteria; AAW88992; AAW88992; NGO_0239. DR GeneID; 3281463; -. DR KEGG; ngo:NGO0239; -. DR PATRIC; 20333429; VBINeiGon24812_0296. DR HOGENOM; HOG000229078; -. DR KO; K00943; -. DR OMA; GGIDIAE; -. DR OrthoDB; EOG64JFSH; -. DR BioCyc; NGON242231:GI2G-223-MONOMER; -. DR Proteomes; UP000000535; 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_0000155310. FT NP_BIND 10 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00165}. SQ SEQUENCE 206 AA; 22957 MW; 18728C9440DB9A41 CRC64; MKPQFITLDG IDGAGKSTNL AVIKAWFERR GLPVLFTREP GGTPVGEALR EILLNPETKA GLRAETLMMF AARMQHIEEV ILPALSDGIH VVSDRFTDAT FAYQGGGRGM PSEDIEILEH WVQGGLRPDL TLLLDVPLEV SMARIGQARE KDRFEQEQAD FFMRVRGVYL DRAAACPERY AVIDSNRSLD EVRNSIEKVL DGHFGC // ID LEPA_NEIG1 Reviewed; 597 AA. AC Q5F9P9; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO0344; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89088.1; -; Genomic_DNA. DR RefSeq; WP_003687751.1; NC_002946.2. DR RefSeq; YP_207500.1; NC_002946.2. DR ProteinModelPortal; Q5F9P9; -. DR SMR; Q5F9P9; 1-555. DR EnsemblBacteria; AAW89088; AAW89088; NGO_0344. DR GeneID; 3281791; -. DR KEGG; ngo:NGO0344; -. DR PATRIC; 20333685; VBINeiGon24812_0420. DR HOGENOM; HOG000020624; -. DR KO; K03596; -. DR OMA; KPMVFCG; -. DR OrthoDB; EOG6ZKXQ4; -. DR BioCyc; NGON242231:GI2G-323-MONOMER; -. DR Proteomes; UP000000535; 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_0000224777. 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; 66002 MW; 90B61147AFACE5B5 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 VYEVVLKSGE KIEVENPSKL PDIGSIETIL EPIITATILV PQEYVGNVMT LCNQKRGVQV NMQYMGRQVM LTYDLPMNEV VMDFFDKLKS TSRGYASLDY HFKEFQPSDL IKLDIMVNGE KVDALSLIVH RQSAVHKGRE LASKMRELIP RQMFDIAVQA AIGSRIIARE NVKALRKNVL AKCYGGDITR KKKLLEKQKA GKRRMKQVGN VEIPQSAFLA ILQVSDK // ID LIPB_NEIG1 Reviewed; 207 AA. AC Q5F8I1; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 16-MAR-2016, entry version 75. 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=NGO0792; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89506.1; 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; AE004969; AAW89506.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F8I1; -. DR EnsemblBacteria; AAW89506; AAW89506; NGO_0792. DR PATRIC; 20334732; VBINeiGon24812_0938. DR HOGENOM; HOG000194321; -. DR OrthoDB; EOG6XM7G6; -. DR BioCyc; NGON242231:GI2G-746-MONOMER; -. DR UniPathway; UPA00538; UER00592. DR Proteomes; UP000000535; 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_0000242734. 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; 22798 MW; FD5C877C8F819538 CRC64; MKIIHKGLVE YLPTFEAMKT FNAGRNADTE DELWVVEHPP VFTQGLAGKP EHLLIRDDIP VVQIDRGGQI TYHGPGQLVV YTMIDFKRRK TSVRNIVSAL ENSIIATLAE YGIEAAADPK RPGIYVGERK IASLGLRIKN GSVYHGLALN VNMDLSPFTQ INPCGYAGME MTQIADFVQP CPAPDEVASK LTAHLETQLT PKADNNE // ID LIPA_NEIG1 Reviewed; 327 AA. AC Q5F8I0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO0793; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89507.1; -; Genomic_DNA. DR RefSeq; WP_003688622.1; NC_002946.2. DR RefSeq; YP_207919.1; NC_002946.2. DR ProteinModelPortal; Q5F8I0; -. DR EnsemblBacteria; AAW89507; AAW89507; NGO_0793. DR GeneID; 3281929; -. DR KEGG; ngo:NGO0793; -. DR PATRIC; 20334734; VBINeiGon24812_0939. DR HOGENOM; HOG000235997; -. DR KO; K03644; -. DR OMA; NVCTRSC; -. DR OrthoDB; EOG6038ZS; -. DR BioCyc; NGON242231:GI2G-747-MONOMER; -. DR UniPathway; UPA00538; UER00593. DR Proteomes; UP000000535; 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_1000012241. 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; 37047 MW; 88EEE1076164C58D CRC64; MSEIKTDDPK RGIKLRGADK TARIPIKVVP LQEKLKKPEW IRAKLPSRKF FEIKDILREQ KMHTVCEEAS CPNIGECFSK GTATFMIMGD ICTRRCPFCD VGHGRPNMLD PDEPKNLAES VKAMNLRYVV ITSVDRDDLR DGGAQHFADC IKAIRETSPN TKIEILVPDF RGRLDIALKI LAETPPDVMN HNLETHPSLY RKARPGANYQ HSLDLLKRYK EMMPHIPTKS GIMVGLGETD EDVREIMRDM RAHNIEMITI GQYLQPSDGH LPVLRYVTPE QFKIFEKEAY ELGFTNAAIG AMVRSSYHAD EQAAEALRES HGGCGHH // ID LPXB_NEIG1 Reviewed; 390 AA. AC Q5F5Y6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392}; DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392}; GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392}; GN OrderedLocusNames=NGO1782; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP-Rule:MF_00392}. 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 {ECO:0000255|HAMAP-Rule:MF_00392}. 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. {ECO:0000255|HAMAP- CC Rule:MF_00392}. CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP- CC Rule:MF_00392}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90401.1; -; Genomic_DNA. DR RefSeq; WP_003689999.1; NC_002946.2. DR RefSeq; YP_208813.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y6; -. DR CAZy; GT19; Glycosyltransferase Family 19. DR EnsemblBacteria; AAW90401; AAW90401; NGO_1782. DR GeneID; 3282347; -. DR KEGG; ngo:NGO1782; -. DR PATRIC; 20337208; VBINeiGon24812_2140. DR HOGENOM; HOG000018003; -. DR KO; K00748; -. DR OMA; YIAPQEW; -. DR OrthoDB; EOG6FBWZR; -. DR BioCyc; NGON242231:GI2G-1680-MONOMER; -. DR UniPathway; UPA00359; UER00481. DR Proteomes; UP000000535; 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 1 390 Lipid-A-disaccharide synthase. FT /FTId=PRO_0000255200. SQ SEQUENCE 390 AA; 43064 MW; 8327E2A576E565BF CRC64; MWGQTNMVDK KSPLIAVSVG EASGDLLGAH LIRAIRKRCP QARLTGIGGE LMKAEGFESL YDQERLAVRG FVEVVRRLPE ILRIRRELVR DLLSLKPDVF VGIDAPDFNL GVAEKLKRAG IPTLHYVSPS VWAWRRERVG KIVHQVNRVL CLFPMEPQLY LDAGGRAEFV GHPMAQLMPL EDDRETARKT LGADVGIPVF ALLPGSRVSE IDYMAPVFFQ TALLLLERYP AARFLLPAAT EATKRRLAEV LQRPEFAGLA LTVTDRQSET VCRAADAVLV TSGTATLEVA LCKRPMVISY KISPLTYAYV KRKIKVPHVG LPNILLGKEA VPELLQSEAK PEKLAAALAD WYEHPDKVAA LQQDFGALHL LLKKDTADLA ARAVLEEAGC // ID LEU1_NEIG1 Reviewed; 517 AA. AC Q5F8D4; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO0848; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89553.1; -; Genomic_DNA. DR RefSeq; WP_003698389.1; NC_002946.2. DR RefSeq; YP_207965.1; NC_002946.2. DR ProteinModelPortal; Q5F8D4; -. DR EnsemblBacteria; AAW89553; AAW89553; NGO_0848. DR GeneID; 3282216; -. DR KEGG; ngo:NGO0848; -. DR PATRIC; 20334864; VBINeiGon24812_1002. DR HOGENOM; HOG000046859; -. DR KO; K01649; -. DR OMA; MAIKTRQ; -. DR OrthoDB; EOG6CGCF3; -. DR BioCyc; NGON242231:GI2G-795-MONOMER; -. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 517 2-isopropylmalate synthase. FT /FTId=PRO_1000149225. SQ SEQUENCE 517 AA; 55336 MW; 08BB5773D8CB7910 CRC64; MTQANRVIIF DTTLRDGEQS PGAAMTKEEK IRVARQLEKL GADIIEAGFA AASPGDFEAV NAIAKTITKS TVCSLSRAIE RDIRQAGKAV APAPKKRIHT FIATSPIHME YKLKMKPKQV IEAAVKAVKI AREYTDDVEF SCEDALRSQI DFLAEICGAV IEAGATTINI PDTVGYSIPY KTEEFFRELI AKTPNGGKVV WSAHCHNDLG LAVANSLAAL KGGARQVECT VNGLGERAGN ASVEEIVMAL KVRHDLFGLE TGIDTTQIVP SSKLVSTITG YPVQPNKAIV GANAFSHESG IHQDGVLKHR ETYEIMSAES VGWSANRLSL GKLSGRNAFK TKLADLGIEL ESEEALNAAF ARFKELADKK REIFDEDLHA LVSDEMGNMN AESYKFISQK ISTETGEEPR ADIVFGIKGE EKRASATGSG PVDAIFKAIE SVAQSGATLQ IYSVNAVTQG TESQGETSVR LARGNRVVNG QGADTDILAA TAKAYLSALS KLEFSAAKPK AQGSGTI // ID LEUC_NEIG1 Reviewed; 469 AA. AC Q5F8T1; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO0679; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89406.1; -; Genomic_DNA. DR RefSeq; WP_010951104.1; NC_002946.2. DR RefSeq; YP_207818.1; NC_002946.2. DR ProteinModelPortal; Q5F8T1; -. DR EnsemblBacteria; AAW89406; AAW89406; NGO_0679. DR GeneID; 3282485; -. DR KEGG; ngo:NGO0679; -. DR PATRIC; 20334456; VBINeiGon24812_0800. DR HOGENOM; HOG000226972; -. DR KO; K01703; -. DR OMA; CNMSIEM; -. DR OrthoDB; EOG600DP5; -. DR BioCyc; NGON242231:GI2G-646-MONOMER; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000535; 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; -; 2. 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_0000076767. 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; 50474 MW; 5EA993CA1537BBD2 CRC64; MTAQTLYDKL WNSHVVREEG DGTVLLYIDR HLVHEVTSPQ AFEGLKMAGR KLWRIDSVVS TADHNTPTGD WDKGIQDPIS KLQVDTLDQN IKEFGALAYF PFMDKGQGIV HVMGPEQGAT LPGMTVVCGD SHTSTHGAFG ALAHGIGTSE VEHTMATQCI TAKKSKSMLI AADGKLKAGV TAKDVALYII GQIGTAGGTG YAVEFGGEAI RSLSMEGRMT LCNMAIEAGA RSGMVAVDQT TIDYVKGKPF APEGEAWDKA VEYWRTLVSD EGAVFDKEYR FNAEDIEPQV TWGTSPEMVL NIGGKVPNPA EETDPVKRSG IERALEYMGL KAGTPLNEIP VDIVFIGSCT NSRIEDLREA AAIAKGHKKA GNVQRVLIVP GSGLVKEQAE KEGLDKIFIE AGFEWREPGC SMCLAMNADR LAPRQRCAST SNRNFEGRQG NGGRTHLVSP AMAAAAAVTG HFTDIRTMA // ID LEUD_NEIG1 Reviewed; 213 AA. AC Q5F8T3; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0677; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89404.1; -; Genomic_DNA. DR RefSeq; WP_010357988.1; NC_002946.2. DR RefSeq; YP_207816.1; NC_002946.2. DR ProteinModelPortal; Q5F8T3; -. DR PRIDE; Q5F8T3; -. DR EnsemblBacteria; AAW89404; AAW89404; NGO_0677. DR GeneID; 3282001; -. DR KEGG; ngo:NGO0677; -. DR PATRIC; 20334452; VBINeiGon24812_0798. DR HOGENOM; HOG000222939; -. DR KO; K01704; -. DR OMA; AFTTHTG; -. DR OrthoDB; EOG661HCP; -. DR BioCyc; NGON242231:GI2G-644-MONOMER; -. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000535; 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_0000141842. SQ SEQUENCE 213 AA; 24208 MW; 0835E832C3FE3C82 CRC64; MKAFTKITAI VAPLDRSNVD TDAIIPKQFL KSIKRSGFGP NAFDEWRYLD HGEPGMDNGK RPLNPDFSLN QPRYQGAQIL LTRKNFGCGS SREHAPWALD DYGFRAIIAP SFADIFFNNC YKNGLLPIVL TEEQVDRLFK EVEANEGYRL SIDLAEQTLT TPGGETFTFD ITEHRKHCLL NGLDEIGLTL QHADKIKAFE EKRRQSQPWL FNG // ID LFTR_NEIG1 Reviewed; 241 AA. AC Q5F5Z0; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1778; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90397.1; -; Genomic_DNA. DR RefSeq; WP_003689990.1; NC_002946.2. DR RefSeq; YP_208809.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z0; -. DR EnsemblBacteria; AAW90397; AAW90397; NGO_1778. DR GeneID; 3282505; -. DR KEGG; ngo:NGO1778; -. DR PATRIC; 20337198; VBINeiGon24812_2135. DR HOGENOM; HOG000102325; -. DR KO; K00684; -. DR OMA; YRQGIFP; -. DR OrthoDB; EOG6WX4R3; -. DR BioCyc; NGON242231:GI2G-1676-MONOMER; -. DR Proteomes; UP000000535; 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_0000258067. SQ SEQUENCE 241 AA; 26901 MW; CC5C7A13D54E7930 CRC64; MRIPLLAPDN YAFPDPAYAL ARCDGLVGVS RDLDAGRLLE AYRNGVFPWF SRDGWFFWYA VGPRAVIVPE RLHVPRSLAK TLRNGSYRVA VNGCFAEVVA HCAAAARPNQ DGTWIAPEFQ TAYLKLHEMG HAHSFECHYP DENGKTRLAG GFYGVQIGRV FYGESMFALQ PDASKIAFAC AVPFLADLGV ELIDCQQDTE HMRRFGSELL PFADFAERLR MLNAVPLKEE IGRREVACKG L // ID LPXC_NEIG1 Reviewed; 307 AA. AC Q5F569; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 66. 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=NGO2065; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90668.1; -; Genomic_DNA. DR RefSeq; WP_003687007.1; NC_002946.2. DR RefSeq; YP_209080.1; NC_002946.2. DR ProteinModelPortal; Q5F569; -. DR SMR; Q5F569; 1-295. DR EnsemblBacteria; AAW90668; AAW90668; NGO_2065. DR GeneID; 3282735; -. DR KEGG; ngo:NGO2065; -. DR PATRIC; 20337943; VBINeiGon24812_2494. DR HOGENOM; HOG000256663; -. DR KO; K02535; -. DR OMA; NSMLVKA; -. DR OrthoDB; EOG6PGK74; -. DR BioCyc; NGON242231:GI2G-1962-MONOMER; -. DR UniPathway; UPA00359; UER00478. DR Proteomes; UP000000535; 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_0000191939. 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; 33921 MW; 6DE8BDBD0F991784 CRC64; MLQRTLAKSI GVTGVGLHSG ERVALTLHPA PENSGISFRR TDLDGEMGEQ IKLNPYLIND TRLSSTIVTD KGLRVGTIEH IMSALSAYGI DNALIELNAP EIPIMDGSSL PFIYLLQDAG VVDQKAQKRF LKILKPVEIK EAGKWVRFTP YDGFKVTLTI EFDHPVFNRS PPTFEIDFAG KSYIGEIARA RTFGFMHEVE MMRAHNLGLG GNLNNAIVIG DTDVLNPEGL RYPDEFVRHK ILDAIGDLYI VGHPIVGAFE GYKSGHAVNN ALLRAVLADE TAYEWVEFAD SDDLPDAFHE LNIRNCG // ID LGT_NEIG1 Reviewed; 283 AA. AC Q5F8D6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO0846; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89551.1; -; Genomic_DNA. DR RefSeq; WP_003688557.1; NC_002946.2. DR RefSeq; YP_207963.1; NC_002946.2. DR EnsemblBacteria; AAW89551; AAW89551; NGO_0846. DR GeneID; 3282218; -. DR KEGG; ngo:NGO0846; -. DR PATRIC; 20334860; VBINeiGon24812_1000. DR HOGENOM; HOG000098666; -. DR KO; K13292; -. DR OMA; AHRTKRH; -. DR OrthoDB; EOG6MH5CQ; -. DR BioCyc; NGON242231:GI2G-793-MONOMER; -. DR UniPathway; UPA00664; -. DR Proteomes; UP000000535; 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_1000053457. FT TRANSMEM 17 37 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 56 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 194 214 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 222 242 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. FT TRANSMEM 255 275 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01147}. SQ SEQUENCE 283 AA; 31835 MW; 607D9CB00CB5D12D CRC64; MIIHHQFDPV LISIGPLAVR WYALSYILGF ILFTFLGRRR IAQGLSVFTK ESLDDFLTWG ILGVILGGRL GYVLFYKFSD YLAHPLDIFK VWEGGMSFHG GFLGVVIAIW LFSRKHGIGF LKLMDTVAPL VPLGLASGRI GNFINGELWG RITDINAFWA MGFPQAHYED AEAAAHNPLW AEWLQQYGML PRHPSQLYQF ALEGICLFAV VWLFSKKPRP TGQTAALFLG GYGVFRFIAE FARQPDDYLG LLTLGLSMGQ WLSVPMIVLG IVGFVRFGMK KQH // ID LPXH_NEIG1 Reviewed; 240 AA. AC Q5F6U7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1448; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90090.1; -; Genomic_DNA. DR RefSeq; WP_003689323.1; NC_002946.2. DR RefSeq; YP_208502.1; NC_002946.2. DR ProteinModelPortal; Q5F6U7; -. DR EnsemblBacteria; AAW90090; AAW90090; NGO_1448. DR GeneID; 3281706; -. DR KEGG; ngo:NGO1448; -. DR PATRIC; 20336313; VBINeiGon24812_1705. DR HOGENOM; HOG000261930; -. DR KO; K03269; -. DR OMA; FMHGNRD; -. DR OrthoDB; EOG6FNHR2; -. DR BioCyc; NGON242231:GI2G-1355-MONOMER; -. DR UniPathway; UPA00359; UER00480. DR Proteomes; UP000000535; 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_1000025063. SQ SEQUENCE 240 AA; 27652 MW; 781E31E9C53724B9 CRC64; MRPSYFISDL HLSEKHPELT ELLLRFLRSA AAGQARAVYI LGDLFDFWVG DDEVSELNTS VAREIRKLSD KGVAVFFVRG NRDFLIGRDF CRQAGMTLLP DYSVLDLFGS NTLICHGDTL CTDDKAYLRF RRIVHCRRLQ KLFLMLPLKW RTRLAAKIRR VSKMEKQVKP ADIMDVNAAF TARQVRAFNA ERLIHGHTHR EHIHHENGFT RIVLGDWHND YASILRVDGD GAVFVPPEEC // ID LOLA_NEIG1 Reviewed; 207 AA. AC Q5FA29; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=Outer-membrane lipoprotein carrier protein {ECO:0000255|HAMAP-Rule:MF_00240}; DE Flags: Precursor; GN Name=lolA {ECO:0000255|HAMAP-Rule:MF_00240}; GN OrderedLocusNames=NGO0205; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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). CC {ECO:0000255|HAMAP-Rule:MF_00240}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00240}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00240}. CC -!- SIMILARITY: Belongs to the LolA family. {ECO:0000255|HAMAP- CC Rule:MF_00240}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88958.1; -; Genomic_DNA. DR RefSeq; WP_003702312.1; NC_002946.2. DR RefSeq; YP_207370.1; NC_002946.2. DR ProteinModelPortal; Q5FA29; -. DR EnsemblBacteria; AAW88958; AAW88958; NGO_0205. DR GeneID; 3282546; -. DR KEGG; ngo:NGO0205; -. DR PATRIC; 20333345; VBINeiGon24812_0255. DR HOGENOM; HOG000257500; -. DR KO; K03634; -. DR OMA; YDADLNQ; -. DR OrthoDB; EOG6677VP; -. DR BioCyc; NGON242231:GI2G-188-MONOMER; -. DR Proteomes; UP000000535; 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|HAMAP-Rule:MF_00240}. FT CHAIN 24 207 Outer-membrane lipoprotein carrier FT protein. FT /FTId=PRO_1000005698. SQ SEQUENCE 207 AA; 22312 MW; 849EEFE3201AA5EA CRC64; MMKPHNLFQF LAVCSLTVAV ASAQAGAVDA LKQFNNDADG ISGSFTQTVQ SKKKTQTAHG TFKILRPGLF KWEYTLPYRQ TIVGDGQTVW LYDVDLAQVT KSSQDQAIGG SPAAILSNKT ALESSYTLKE DGSSNGIDYV RATPKRNNAG YQYIRIGFKG GNLAAMQLKD SFGNQTSISF GGLNTNPQLS RGAFKFTPPK GVDVLSN // ID LPXA_NEIG1 Reviewed; 258 AA. AC Q5F5W3; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO1806; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90424.1; -; Genomic_DNA. DR RefSeq; WP_003690038.1; NC_002946.2. DR RefSeq; YP_208836.1; NC_002946.2. DR ProteinModelPortal; Q5F5W3; -. DR EnsemblBacteria; AAW90424; AAW90424; NGO_1806. DR GeneID; 3282363; -. DR KEGG; ngo:NGO1806; -. DR PATRIC; 20337262; VBINeiGon24812_2166. DR HOGENOM; HOG000294326; -. DR KO; K00677; -. DR OMA; VQDRSET; -. DR OrthoDB; EOG6F81P1; -. DR BioCyc; NGON242231:GI2G-1704-MONOMER; -. DR UniPathway; UPA00359; UER00477. DR Proteomes; UP000000535; 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_0000302582. SQ SEQUENCE 258 AA; 28171 MW; B8B5D9D2EE8CCDD3 CRC64; MTLIHPTAVI DPKAELDSGV KVGAYTVIGP NVRIGANTEI GPHAVINGHT TIGENNRIFQ FASLGEIPQD KKYRDEPTKL IIGNGNTIRE FTTFNLGTVT GIGETRIGDD NWIMAYCHLA HDCVVGNHTI FANNASLAGH VTVGDYVVLG GYTLVFQFCR IGDYAMTAFA AGVHKDVPPY FMASGYRAEP AGLNSEGMRR NGFTAEQISA VKDVYKTLYH RGIPFEEAKA DILRRAETQA ELAVFQDFFA QSTRGIIR // ID LPXK_NEIG1 Reviewed; 343 AA. AC Q5F9Z2; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. 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=NGO0242; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88995.1; -; Genomic_DNA. DR RefSeq; WP_003687587.1; NC_002946.2. DR RefSeq; YP_207407.1; NC_002946.2. DR EnsemblBacteria; AAW88995; AAW88995; NGO_0242. DR GeneID; 3281520; -. DR KEGG; ngo:NGO0242; -. DR PATRIC; 20333435; VBINeiGon24812_0299. DR HOGENOM; HOG000004953; -. DR KO; K00912; -. DR OMA; PTVIYLI; -. DR OrthoDB; EOG60GRWT; -. DR BioCyc; NGON242231:GI2G-226-MONOMER; -. DR UniPathway; UPA00359; UER00482. DR Proteomes; UP000000535; 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; -; 1. 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 1 343 Tetraacyldisaccharide 4'-kinase. FT /FTId=PRO_0000229965. FT NP_BIND 65 72 ATP. {ECO:0000255|HAMAP-Rule:MF_00409}. SQ SEQUENCE 343 AA; 37021 MW; 6F1328427A58892D CRC64; MPNFFKFHTV IERHWQKPYP VLSFLLKPLS GLFAKIAAKW RADFLSGKRQ SEKLSVPVVV VGNIHAGGTG KTPIAAALVS GLQEKGVKVG IISRGYGRKS KAVYVLNAAS RAEDAGDEPL LLFRKTGAPT AVGSSRVEAG RALLAAHPEL ELIVADDGLQ HYALQRDVEI AVFPAADTGR TDLDLLPNGN LREPLSRLES VDAVVVGGRA ADGFMPSEHL FGSRIEAGAV YRLNRPSEKL DISTLSGKRV AAVAGIARPQ RFFDTLTHMG IRLDQTVALP DHADIFNRDL PPADVVLVTE KDAVKFSDGI CTDNVWVLPV CAIIEPDLAE FVLERLEGVP KAV // ID LSPA_NEIG1 Reviewed; 164 AA. AC Q5FAF3; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 71. 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}; GN OrderedLocusNames=NGO0071; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88834.1; -; Genomic_DNA. DR RefSeq; WP_003687321.1; NC_002946.2. DR RefSeq; YP_207246.1; NC_002946.2. DR MEROPS; A08.001; -. DR EnsemblBacteria; AAW88834; AAW88834; NGO_0071. DR GeneID; 3282278; -. DR KEGG; ngo:NGO0071; -. DR PATRIC; 20333016; VBINeiGon24812_0092. DR HOGENOM; HOG000096993; -. DR KO; K03101; -. DR OMA; DCAITVG; -. DR OrthoDB; EOG6PGKBM; -. DR BioCyc; NGON242231:GI2G-63-MONOMER; -. DR UniPathway; UPA00665; -. DR Proteomes; UP000000535; 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. 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 1 164 Lipoprotein signal peptidase. FT /FTId=PRO_0000289404. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 41 61 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 64 84 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00161}. FT TRANSMEM 132 152 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 164 AA; 18336 MW; CE4D906803289EC8 CRC64; MSSSVSSKTR YWVLALAAIV LDQWSKWAVL SSFQYRERVN VIPSFFDLTL VYNPGAAFSF LADQGGWQKY FFLVLAVAVS AYLVRAILRD EFAALGKIGA AMIIGGASGN VIDRLIHGHV VDFLLFYWQN WFYPAFNIAD SFICVGAVLA VLDNIVHRKD SKKT // ID LOLD_NEIG1 Reviewed; 231 AA. AC Q5F8K2; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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}; GN OrderedLocusNames=NGO0770; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89485.1; -; Genomic_DNA. DR RefSeq; WP_003688655.1; NC_002946.2. DR RefSeq; YP_207897.1; NC_002946.2. DR ProteinModelPortal; Q5F8K2; -. DR EnsemblBacteria; AAW89485; AAW89485; NGO_0770. DR GeneID; 3282041; -. DR KEGG; ngo:NGO0770; -. DR PATRIC; 20334688; VBINeiGon24812_0916. DR KO; K09810; -. DR OMA; DHTAGGV; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-725-MONOMER; -. DR Proteomes; UP000000535; 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_0000272109. 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; 25259 MW; 1CE7B3A5166BA48D CRC64; MSDLILKCEG VGKRYRDGGL DVPVLYGLDL EIRTGESTGI IGSSGSGKST LLHILGGLDM PSEGRVLLMG EDLRALNQRR LGDLRNRHLG FVYQFHHLLP EFSALENVMM PLLIGKKSRK EAVETAMAML DKVGLKHRST HRAGELSGGE RQRAAIARAL VTQPKCLLAD EPTGNLDRAN ARNVLDMMLE LKTELGTGLV VVTHDDELAG RFERVMVMKD GSLHPRQGAN A // ID LPTD_NEIG1 Reviewed; 801 AA. AC Q5F651; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO1715; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Belongs to the LptD family. {ECO:0000255|HAMAP- CC Rule:MF_01411}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90336.1; -; Genomic_DNA. DR RefSeq; WP_003698952.1; NC_002946.2. DR RefSeq; YP_208748.1; NC_002946.2. DR EnsemblBacteria; AAW90336; AAW90336; NGO_1715. DR GeneID; 3281158; -. DR KEGG; ngo:NGO1715; -. DR PATRIC; 20337022; VBINeiGon24812_2051. DR HOGENOM; HOG000220687; -. DR KO; K04744; -. DR OMA; DYSHLDW; -. DR OrthoDB; EOG6SZ1CP; -. DR BioCyc; NGON242231:GI2G-1611-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell outer membrane; Complete proteome; Membrane; Reference proteome; KW Signal. FT SIGNAL 1 23 {ECO:0000255|HAMAP-Rule:MF_01411}. FT CHAIN 24 801 LPS-assembly protein LptD. FT /FTId=PRO_0000281618. SQ SEQUENCE 801 AA; 87541 MW; F1B4179D5BF5E8DD CRC64; MARLFSLKPL VLALGFCFGT HCAADTVAAE EADGRVAEGG AQGASESAQA SDLTLGSTCL FCSNESGSPE RTEAAVQGSG EASVPEDYTR IVADRMEGQS KVKVRAEGSV IIERDGAVLN TDWADYDQSG DTVTVGDRFA LQQDGTLIRG ETLTYNLDQQ TGEAHNVRME TEQGGRRLQS VSRTAEMLGE GRYKLTETQF NTCSAGDAGW YVKAASVEAD RGKGIGVAKH AAFVFGGVPL FYTPWADFPL DGNRKSGLLV PSVSAGSDGV SLSVPYYFNL APNFDATFAP GIIGERGATF DGQIRYLRPD YSGQTDLTWL PHDKKSGRNN RYQAKWQHRH DISDTLQAGV DFNQVSDSGY YRDFYGGEEI AGNVNLNRRV WLDYGGRAAG GSLNAGLSVQ KYQTLANQSG YKDEPYAIMP RLSADWHKNA GRAQIGVSAQ FTRFSHDGRQ DGSRLVVYPG IKWDFSNSWG YVRPKLGLHA TYYSLDSFGG KASRSVGRVL PVVNIDGGTT FERNTRLFGG GVVQTIEPRL FYNYIPAKSQ NDLPNFDSSE SSFGYGQLFR ENLYYGNDRI NAANSLSTAV QSRILDGATG EERFRAGIGQ KFYFKDDAVM LDGSVGKNPR SRSDWVAFAS GGIGGRFTLD SSIHYNQNDK RAEHYAVGAG YRPAPGKVLN ARYKYGRNEK IYLQADGSYF YDKLSQLDLS AQWPLTRNLS AVVRYNYGFE AKKPIEMLAG AEYKSSCGCW GAGVYAQRYV TGENTYKNAV FFSLQLKDLS SVGRNPAGRM DVAVPGYIPA HSLSAGRNKR P // ID LUXS_NEIG1 Reviewed; 168 AA. AC Q5F534; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. 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=NGO2102; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90703.1; -; Genomic_DNA. DR RefSeq; WP_003687075.1; NC_002946.2. DR RefSeq; YP_209115.1; NC_002946.2. DR ProteinModelPortal; Q5F534; -. DR SMR; Q5F534; 3-162. DR EnsemblBacteria; AAW90703; AAW90703; NGO_2102. DR GeneID; 3282815; -. DR KEGG; ngo:NGO2102; -. DR PATRIC; 20338041; VBINeiGon24812_2543. DR HOGENOM; HOG000040371; -. DR KO; K07173; -. DR OMA; AGFMREH; -. DR OrthoDB; EOG68WRBM; -. DR BioCyc; NGON242231:GI2G-1997-MONOMER; -. DR Proteomes; UP000000535; 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_0000298015. 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; 18623 MW; 374BD83A58B92FBD CRC64; MPLLDSFKVD HTRMHAPAVR VAKTMTTPKG DTITVFDLRF CIPNKEILPE KGIHTLEHLF AGFMRDHLNG AGVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWLASMQD VLNVKDQSKI PELNEYQCGT YLMHSLAEAQ QIAQNVLARK VAVNRNGDLA LDESLLNA // ID MAFA1_NEIG1 Reviewed; 320 AA. AC Q5F5F6; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE RecName: Full=Adhesin MafA 1/4; DE Flags: Precursor; GN Name=mafA1; OrderedLocusNames=NGO1067; GN and GN Name=mafA4; OrderedLocusNames=NGO1972; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. 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; AE004969; AAW89737.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90581.1; -; Genomic_DNA. DR RefSeq; WP_010951170.1; NC_002946.2. DR RefSeq; YP_208149.1; NC_002946.2. DR RefSeq; YP_208993.1; NC_002946.2. DR EnsemblBacteria; AAW89737; AAW89737; NGO_1067. DR EnsemblBacteria; AAW90581; AAW90581; NGO_1972. DR GeneID; 3281190; -. DR GeneID; 3282651; -. DR KEGG; ngo:NGO1067; -. DR KEGG; ngo:NGO1972; -. DR PATRIC; 20335368; VBINeiGon24812_1250. DR HOGENOM; HOG000071263; -. DR OMA; ETDNSHE; -. DR OrthoDB; EOG6ZPSX7; -. DR BioCyc; NGON242231:GI2G-1871-MONOMER; -. DR BioCyc; NGON242231:GI2G-982-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell adhesion; Cell outer membrane; Complete proteome; Lipoprotein; KW Membrane; Palmitate; Reference proteome; Signal; Virulence. FT SIGNAL 1 18 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 19 320 Adhesin MafA 1/4. FT /FTId=PRO_0000344483. FT LIPID 19 19 N-palmitoyl cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. FT LIPID 19 19 S-diacylglycerol cysteine. FT {ECO:0000255|PROSITE-ProRule:PRU00303}. SQ SEQUENCE 320 AA; 34751 MW; 4137DEC55E2521CC CRC64; MRARLLIPIL FSVFILSACG TLTGIPSHGG GKRFAVEQEL VAASARAAVK DMDLQALHGR KVALYIATMG DQGSGSLTGG RYSIDALIRG EYINSPAVRT DYTYPRYETT AETTSGGLTG LTTSLSTLNA PALSRTQSDG SGSRSSLGLN IGGMGDYRNE TLTTNPRDTA FLSHLVQTVF FLRGIDVVSP ANADTDVFIN IDVFGTIRNR TEMHLYNAET LKAQTKLEYF AVDRTNKKLL IKPKTNAFEA AYKENYALWM GPYKVSKGIK PTEGLMVDFS DIQPYGNHTG NSAPSVEADN SHEGYGYSDE AVRQHRQGQP // ID LPXD_NEIG1 Reviewed; 347 AA. AC Q5F5W6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1803; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90421.1; -; Genomic_DNA. DR RefSeq; WP_003694315.1; NC_002946.2. DR RefSeq; YP_208833.1; NC_002946.2. DR ProteinModelPortal; Q5F5W6; -. DR EnsemblBacteria; AAW90421; AAW90421; NGO_1803. DR GeneID; 3282536; -. DR KEGG; ngo:NGO1803; -. DR PATRIC; 20337256; VBINeiGon24812_2163. DR HOGENOM; HOG000294339; -. DR KO; K02536; -. DR OMA; WANVTLY; -. DR OrthoDB; EOG6JB11D; -. DR BioCyc; NGON242231:GI2G-1701-MONOMER; -. DR UniPathway; UPA00973; -. DR Proteomes; UP000000535; 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 1 347 UDP-3-O-acylglucosamine N- FT acyltransferase. FT /FTId=PRO_0000264398. FT ACT_SITE 241 241 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00523}. SQ SEQUENCE 347 AA; 36269 MW; F9CD31A824E08AC0 CRC64; MIPATCTLSQ ITARLGGEWR GEDISVTAVR PLADAQAEHI SFLANPKYKA EVHDSSAGAI IVSAKAADGF EGRNLIVADD PYLYFAKVAR LFSPVVKARG GIHPTAVVEP GATVPASCEI GANAYIGANT VLGEGCRILA NAVVQHDCKL GDEVVLHPNA VVYYGCTLGR HVEIHSGAVI GADGFGLAFA GDSWFKIPQT GAVTLGDDVE IGSNTNIDRG AMSDTTVGNG TKIDNQVQIG HNCKIGSHTV IAAKTGISGS VTIGSYCIIG GGVGTVGHIE IADKTTIGGG TSVTHSITES GKHLAGIFPM SEHKEWARNA VYIHRLSEMN KRLKTLEQQL SDSKDTQ // ID MAFA2_NEIG1 Reviewed; 313 AA. AC Q5F6H4; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=Adhesin MafA 2/3; DE Flags: Precursor; GN Name=mafA2; OrderedLocusNames=NGO1393; GN and GN Name=mafA3; OrderedLocusNames=NGO1584; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid- CC anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. 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; AE004969; AAW90041.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90213.1; -; Genomic_DNA. DR RefSeq; WP_003691615.1; NC_002946.2. DR RefSeq; YP_208453.1; NC_002946.2. DR RefSeq; YP_208625.1; NC_002946.2. DR EnsemblBacteria; AAW90041; AAW90041; NGO_1393. DR EnsemblBacteria; AAW90213; AAW90213; NGO_1584. DR GeneID; 3281326; -. DR GeneID; 3281439; -. DR KEGG; ngo:NGO1393; -. DR KEGG; ngo:NGO1584; -. DR PATRIC; 20336177; VBINeiGon24812_1637. DR HOGENOM; HOG000071263; -. DR OMA; LTKNNGR; -. DR OrthoDB; EOG6VMTH8; -. DR BioCyc; NGON242231:GI2G-1306-MONOMER; -. DR BioCyc; NGON242231:GI2G-1481-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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 2/3. FT /FTId=PRO_0000344484. 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; 33926 MW; E94135BC6B476162 CRC64; MKTLLLLIPL VLTACGTLTG IPAHGGGKRF AVEQELVAAS SRAAVKEMDL SALKGRKAAL YVSVMGDQGS GNISGGRYSI DALIRGGYHN NPDSATRYSY PAYDTTATTK SDALSGVTTS TSLLNAPAAA LTKNNGRKGE RSAGLSVNGT GDYRNETLLA NPRDVSFLTN LIQTVFYLRG IEVVPPEYAD TDVFVTVDVF GTVRSRTELH LYNAETLKAQ TKLEYFAVDR DSRKLLIAPK TAAYESQYQE QYALWMGPYS VGKTVKASDR LMVDFSDITP YGDTTAQNRP DFKQNNGKNP DVGNEVIRRR KGG // ID MACB_NEIG1 Reviewed; 644 AA. AC Q5F6V6; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO1439; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90081.1; -; Genomic_DNA. DR RefSeq; WP_003697391.1; NC_002946.2. DR RefSeq; YP_208493.1; NC_002946.2. DR ProteinModelPortal; Q5F6V6; -. DR EnsemblBacteria; AAW90081; AAW90081; NGO_1439. DR GeneID; 3281707; -. DR KEGG; ngo:NGO1439; -. DR PATRIC; 20336297; VBINeiGon24812_1697. DR HOGENOM; HOG000208217; -. DR KO; K05685; -. DR OMA; LNTDDIR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1346-MONOMER; -. DR Proteomes; UP000000535; 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_0000269948. 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; 69355 MW; 04F8B662795298D5 CRC64; MSLIECKNIN RCFGSGENRV HILKDISLSI EKGDFVAIIG QSGSGKSTLM NILGCLDTAG SGSYRIDGIE TAKMQPDELA ALRRERFGFI FQRYNLLSSL TARDNVALPA VYMGMGGKER SARADKLLQD LGLASKEGNK PGELSGGQQQ RVSIARALMN GGEIIFADEP TGALDTASGK NVMEIIRRLH EAGHTVIMVT HDPGIAANAN RVIEIRDGEI ISDTSKNPEI PASNVGRIRE KASWSFYYDQ FVEAFRMSVQ AVLAHKMRSL LTMLGIIIGI ASVVSVVALG NGSQKKILED ISSMGTNTIS IFPGRGFGDR RSGKIKTLTI DDAKIIAKQS YVASATPMTS SGGTLTYRNT DLTASLYGVG EQYFDVRGLK LETGRLFDEN DVKEDAQVVV IDQNVKDKLF ADSDPLGKTI LFRKRPLTVI GVMKKDENAF GNSDVLMLWS PYTTVMHQIT GESHTNSITV KIKDNANTRV AEKGLAELLK ARHGTEDFFM NNSDSIRQMV ESTTGTMKLL ISSIALISLV VGGIGVMNIM LVSVTERTKE IGIRMAIGAR RGNILQQFLI EAVLICIIGG LVGVGLSAAV SLVFNHFVTD FPMDISAASV IGAVACSTGI GIAFGFMPAN KAAKLNPIDA LAQD // ID METK_NEIG1 Reviewed; 389 AA. AC Q5FAC0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 09-DEC-2015, entry version 85. 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=NGO0106; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW88867.1; 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; AE004969; AAW88867.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003704903.1; NC_002946.2. DR RefSeq; YP_207279.2; NC_002946.2. DR ProteinModelPortal; Q5FAC0; -. DR SMR; Q5FAC0; 2-389. DR EnsemblBacteria; AAW88867; AAW88867; NGO_0106. DR GeneID; 3282432; -. DR KEGG; ngo:NGO0106; -. DR PATRIC; 20333111; VBINeiGon24812_0139. DR HOGENOM; HOG000245710; -. DR KO; K00789; -. DR OrthoDB; EOG68WR6M; -. DR BioCyc; NGON242231:GI2G-96-MONOMER; -. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000535; 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_0000241008. 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; 41942 MW; 0FB0EEDF9A564C7E CRC64; MSEYLFTSES VSEGHPDKVA DQVSDAILDA ILAQDPKARV AAETLVNTGL CVLAGEITTT AQVDYIKVAR ETIKRIGYNS SELGFDANGC AVGVYYDQQS PDIAQGVNEG EGIDLNQGAG DQGLMFGYAC DETPTLMPFA IYYSHRLMQR QSELRKDGRL PWLRPDAKAQ LTVVYDSETG KVKRIDTVVL STQHDPAISQ EELSKAVIEQ IIKPVLPPEL LTDETKYLIN PTGRFVIGGP QGDCGLTGRK IIVDTYGGAA PHGGGAFSGK DPSKVDRSAA YACRYVAKNI VAAGLATQCQ IQVSYAIGVA EPTSISIDTF GTGKISEEKL IALVCEHFDL RPKGIVQMLD LLRPIYGKSA AYGHFGREEP EFTWERTDKA ASLKAAAGL // ID METE_NEIG1 Reviewed; 758 AA. AC Q5F863; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00172}; DE EC=2.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00172}; DE AltName: Full=Cobalamin-independent methionine synthase {ECO:0000255|HAMAP-Rule:MF_00172}; DE AltName: Full=Methionine synthase, vitamin-B12 independent isozyme {ECO:0000255|HAMAP-Rule:MF_00172}; GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00172}; GN OrderedLocusNames=NGO0928; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000255|HAMAP-Rule:MF_00172}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L- CC homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_00172}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00172}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00172}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-methionine from L-homocysteine (MetE route): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00172}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine CC synthase family. {ECO:0000255|HAMAP-Rule:MF_00172}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89624.1; -; Genomic_DNA. DR RefSeq; WP_003688382.1; NC_002946.2. DR RefSeq; YP_208036.1; NC_002946.2. DR ProteinModelPortal; Q5F863; -. DR PRIDE; Q5F863; -. DR EnsemblBacteria; AAW89624; AAW89624; NGO_0928. DR GeneID; 3282587; -. DR KEGG; ngo:NGO0928; -. DR PATRIC; 20335039; VBINeiGon24812_1089. DR HOGENOM; HOG000246221; -. DR KO; K00549; -. DR OMA; RFGWVQS; -. DR OrthoDB; EOG6FFS3G; -. DR BioCyc; NGON242231:GI2G-866-MONOMER; -. DR UniPathway; UPA00051; UER00082. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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_1000017257. FT METAL 643 643 Zinc. {ECO:0000255|HAMAP-Rule:MF_00172}. FT METAL 645 645 Zinc. {ECO:0000255|HAMAP-Rule:MF_00172}. FT METAL 728 728 Zinc. {ECO:0000255|HAMAP-Rule:MF_00172}. SQ SEQUENCE 758 AA; 85013 MW; 1EF1567F4AA09850 CRC64; MTTLHFSGFP RVGAFRELKF AQEKYWRKEI SEQELLDVAK DLREKNWKHQ AAANADYVAV GDFTFYDHIL DLQVATGAIP ARFGFDSQNL PLEQFFQLAR GNKDQFAIEM TKWFDTNYHY LVPEFHADTE FKANAKHYVQ QLQEAQTLGL KAKPTVVGPL TFLWVGKEKG SVEFDRLSLL PKLLPVYVEI LTALVEAGAE WIQIDEPALA VDLPKEWVEA YKDVYATLNK VSAKILLGTY FGSVAEHAAL LKSLPVDGLH IDLVRAPEQL DAFAGYDKVL SAGVIDGRNI WRANLNKVLE TVGPLQAKLG ERLWISSSCS LLHTPFDLSV EEKLKANKPD LYSWLAFTLQ KTQELRVLKA ALNEGRDSVA EELAASQAAA DSRANSSEIH RADVAKRLAD LPVNAGQRKS PFADRIKAQQ AWLNLPLLPT TNIGSFPQTT EIRQARAAFK KGELSASDYE AAMKKEIALV VEEQEKLDLD VLVHGEAERN DMVEYFGELL SGFAFTQYGW VQSYGSRCVK PPIIFGDVSR PEAMTVAWST YAQNLTKRPM KGMLTGPVTI LQWSFVRNDI PRATVCKQIA LALNDEVLDL EKAGIKVIQI DEPAIREGLP LKRADWDAYL NWAGESFRLS SAGCEDSTQI HTHMCYSEFN DILPAIAAMD ADVITIETSR SDMELLAAFG EFKYPNDIGP GVYDIHSPRV PTEAEVEHLL RKAIEVVPVE RLWVNPDCGL KTRGWKETLE QLQVMMNVTR KLRAELAK // ID MINE_NEIG1 Reviewed; 87 AA. AC Q5F5V5; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE RecName: Full=Cell division topological specificity factor {ECO:0000255|HAMAP-Rule:MF_00262}; GN Name=minE {ECO:0000255|HAMAP-Rule:MF_00262}; GN OrderedLocusNames=NGO1814; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP-Rule:MF_00262}. CC -!- SIMILARITY: Belongs to the MinE family. {ECO:0000255|HAMAP- CC Rule:MF_00262}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90432.1; -; Genomic_DNA. DR RefSeq; WP_003690052.1; NC_002946.2. DR RefSeq; YP_208844.1; NC_002946.2. DR ProteinModelPortal; Q5F5V5; -. DR EnsemblBacteria; AAW90432; AAW90432; NGO_1814. DR GeneID; 3282300; -. DR KEGG; ngo:NGO1814; -. DR PATRIC; 20337288; VBINeiGon24812_2179. DR HOGENOM; HOG000218362; -. DR KO; K03608; -. DR OMA; HERTGHS; -. DR OrthoDB; EOG6HMXJM; -. DR BioCyc; NGON242231:GI2G-1712-MONOMER; -. DR Proteomes; UP000000535; 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_0000298137. SQ SEQUENCE 87 AA; 10041 MW; AF5A261D415FE7C3 CRC64; MSLIELLFGR KQKTATVARD RLQIIIAQER AQEGQTPDYL PTLRKELMEV LSKYVNVSLD NIRISQEKQD GMDVLELNIT LPEQKKV // ID METX_NEIG1 Reviewed; 379 AA. AC Q5F858; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO0933; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89629.1; -; Genomic_DNA. DR RefSeq; WP_010951153.1; NC_002946.2. DR RefSeq; YP_208041.1; NC_002946.2. DR ProteinModelPortal; Q5F858; -. DR ESTHER; neima-metx; Homoserine_transacetylase. DR EnsemblBacteria; AAW89629; AAW89629; NGO_0933. DR GeneID; 3282566; -. DR KEGG; ngo:NGO0933; -. DR PATRIC; 20335049; VBINeiGon24812_1094. DR HOGENOM; HOG000246301; -. DR KO; K00641; -. DR OMA; GSVGGMN; -. DR OrthoDB; EOG67T5J4; -. DR BioCyc; NGON242231:GI2G-871-MONOMER; -. DR UniPathway; UPA00051; UER00074. DR Proteomes; UP000000535; 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_0000231874. 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; 42145 MW; E6D341BB93507CE8 CRC64; MSQNTSVGIV TPQKIPFEMP LVLENGKTLP RFDLMIETYG ELNAEKNNAV LICHALSGNH HVAGRHSAED KYTGWWDNMV GPGKPIDTER FFVVGLNNLG GCDGSSGPLS INPETGREYG ADFPMVTVKD WVKSQAALAD YLGIEQWAAV VGGSLGGMQA LQWAISYPER VRHALVIASA PKLSAQNIAF NDVARQAILT DPDFNEGHYR SHNTVPARGL RIARMMGHIT YLAEDGLGKK FGRDLRSNGY QYGYSVEFEV ESYLRYQGDK FVGRFDANTY LLMTKALDYF DPAADFGNSL TRAVQDVQAK FFVASFSTDW RFAPERSHEL VKALIAAQKS VQYIEVKSAH GHDAFLMEDE AYMRAVTAYM NNVDKDCRL // ID MIAA_NEIG1 Reviewed; 313 AA. AC Q5F852; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0940; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89635.1; -; Genomic_DNA. DR RefSeq; WP_003698342.1; NC_002946.2. DR RefSeq; YP_208047.1; NC_002946.2. DR ProteinModelPortal; Q5F852; -. DR EnsemblBacteria; AAW89635; AAW89635; NGO_0940. DR GeneID; 3281618; -. DR KEGG; ngo:NGO0940; -. DR PATRIC; 20335065; VBINeiGon24812_1102. DR HOGENOM; HOG000039996; -. DR KO; K00791; -. DR OMA; TWFRNQT; -. DR OrthoDB; EOG661HB3; -. DR BioCyc; NGON242231:GI2G-877-MONOMER; -. DR Proteomes; UP000000535; 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; 3. 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_1000020624. 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; 34855 MW; A27BEE85933889E0 CRC64; MPTPKAFTLL GPTACGKTAL ALKIAETLPV EIISLDSALL YTGMDIGTAK PSASERAFVP HHLIDIITPV QTYSAARFVE DCTRLTGEIT ARGKCPLIVG GTMMYFRALT QGLNDLPEAD ACLRADLDEQ KQMYGLDFLY RTLQKVDPET ACRLKPNDSQ RIGRALEVYY LTGRPMSAHL NGQPEHTLPF ELYTAALIPE DRARLHENIA LRFHLMLEQG FIGEVENLRR RYPGLTADSP AIRCVGYRQA WEHLDGATDR QTFIEKGIAA TRQLAKRQLT WLRKTPLDCV ADPFSDGTSG TRLIEAAKRF FGE // ID MINC_NEIG1 Reviewed; 237 AA. AC Q5F5V4; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Probable septum site-determining protein MinC; GN Name=minC; OrderedLocusNames=NGO1816; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11160816; RA Ramirez-Arcos S., Szeto J., Beveridge T., Victor C., Francis F., RA Dillon J.; RT "Deletion of the cell-division inhibitor MinC results in lysis of RT Neisseria gonorrhoeae."; RL Microbiology 147:225-237(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90433.1; -; Genomic_DNA. DR RefSeq; WP_003700581.1; NC_002946.2. DR RefSeq; YP_208845.1; NC_002946.2. DR ProteinModelPortal; Q5F5V4; -. DR EnsemblBacteria; AAW90433; AAW90433; NGO_1816. DR GeneID; 3282164; -. DR KEGG; ngo:NGO1816; -. DR PATRIC; 20337292; VBINeiGon24812_2181. DR HOGENOM; HOG000062060; -. DR KO; K03610; -. DR OMA; WAAVAMK; -. DR OrthoDB; EOG606588; -. DR BioCyc; NGON242231:GI2G-1713-MONOMER; -. DR Proteomes; UP000000535; 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_0000189043. SQ SEQUENCE 237 AA; 26268 MW; AEF6B9FF1A91684D CRC64; MMVYIMNAFD IKSTKMDVLS ISLHTSDLFD LEDVLVKLGK KFQESGVVPF VLDVQEFDYP ESLDLAALVS LFSRHGMQIL GLKHSNERWA AVAMKYHLLF CLSHSENVKE LGQVEVQKTE DGQKARKTVL ITSPVRTGQQ VYAEDGDLIV TGAVSQGAEL IADGNMHIYA PMRGRALAGA KGDTSARIFI HSMQAELVSV AGIYRNFEQD LPDHLHKQPV QILLQDNRLV ISAIGSE // ID MNTP_NEIG1 Reviewed; 188 AA. AC Q5F600; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO1768; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90387.1; -; Genomic_DNA. DR RefSeq; WP_003690352.1; NC_002946.2. DR RefSeq; YP_208799.1; NC_002946.2. DR EnsemblBacteria; AAW90387; AAW90387; NGO_1768. DR GeneID; 3281166; -. DR KEGG; ngo:NGO1768; -. DR PATRIC; 20337158; VBINeiGon24812_2119. DR HOGENOM; HOG000238852; -. DR OMA; FIGGKMI; -. DR OrthoDB; EOG676Z87; -. DR BioCyc; NGON242231:GI2G-1662-MONOMER; -. DR Proteomes; UP000000535; 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_0000155656. 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; 19778 MW; 0655523BC9981B7D CRC64; MSLYALLLVA LGMSMDAFAV ALAKGAAVRM PPRKIAATAL VFGTVEAFMP LAGWVGGFYA KPFISEWDHW VAFVLLGGLG LKMMREGLSG EAEDVRESKQ ESLWMTVLTA FGTSIDSMIV GVGLAFMEVN IAFAAAVIGM AATVMVTIGL TAGKAFGVLF GRRAEFAGGL VLIAIGTWTL LSHLGLIQ // ID MIAB_NEIG1 Reviewed; 442 AA. AC Q5FAI1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO0037; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88806.1; -; Genomic_DNA. DR RefSeq; WP_010950977.1; NC_002946.2. DR RefSeq; YP_207218.1; NC_002946.2. DR ProteinModelPortal; Q5FAI1; -. DR DNASU; 3282401; -. DR EnsemblBacteria; AAW88806; AAW88806; NGO_0037. DR GeneID; 3282401; -. DR KEGG; ngo:NGO0037; -. DR PATRIC; 20332906; VBINeiGon24812_0038. DR HOGENOM; HOG000224767; -. DR KO; K06168; -. DR OMA; IPMDLIL; -. DR OrthoDB; EOG6P5ZD8; -. DR BioCyc; NGON242231:GI2G-34-MONOMER; -. DR Proteomes; UP000000535; 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_0000374400. 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; 49652 MW; F48D269E78417ED1 CRC64; MKKVFIRTFG CQMNEYDSEK MLSVLAEEHG 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 IGTVQRCLVE GISKKDPDQL QARTVNNRVV NFTGTPDMIN QMIDLEITEA YTFSLRGKIV EA // ID MNME_NEIG1 Reviewed; 448 AA. AC Q5F529; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=trmE {ECO:0000255|HAMAP-Rule:MF_00379}; GN OrderedLocusNames=NGO2107; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90708.1; -; Genomic_DNA. DR RefSeq; WP_003687082.1; NC_002946.2. DR RefSeq; YP_209120.1; NC_002946.2. DR ProteinModelPortal; Q5F529; -. DR EnsemblBacteria; AAW90708; AAW90708; NGO_2107. DR GeneID; 3282810; -. DR KEGG; ngo:NGO2107; -. DR PATRIC; 20338053; VBINeiGon24812_2549. DR HOGENOM; HOG000200714; -. DR KO; K03650; -. DR OMA; FTPRYAY; -. DR OrthoDB; EOG6DC6K1; -. DR BioCyc; NGON242231:GI2G-2002-MONOMER; -. DR Proteomes; UP000000535; 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_0000345848. 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; 47440 MW; 54FED41EFB6A83D5 CRC64; MSDNVPTIAA VATAPGRGGV GVIRISGKNL LPMAQALCGK TPEPRVATYA DFTDADGQAI DSGLLLFFAA PASFTGEDVI ELQGHGGPVV MEMLLNRCLE LGARLAEPGE FTKRAFLNDK LDLAQAEGVA DLIDASGRSA ARLALRSLKG DFSRRIHGLV EGLITLRMLV EAALDFPEED IDFLEAADAR GKLDGLRRAV DDVLANAQQG AILREGLNVV LVGAPNVGKS SLLNALAGDE VAIVTDIAGT TRDAVRERIL IDGVPVHIVD TAGLRETDDV VERIGIERSR KAVSEADVAL VLVDPREGLN EKTRMILDTL PSDLKRIEIH SKSDLHAHAA GGFGTGAETV IALSAKTGDG LDALKRTLLC EAGWQGESEG LFLARTRHVN ALKAAQEELS LAALCGNHQI ELFAEHLRLA QVACGEITGE FTADDLLGVI FSRFCIGK // ID MNMG_NEIG1 Reviewed; 628 AA. AC Q5F5Y0; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 73. 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=NGO1788; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90407.1; -; Genomic_DNA. DR RefSeq; WP_010951347.1; NC_002946.2. DR RefSeq; YP_208819.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y0; -. DR SMR; Q5F5Y0; 1-554. DR EnsemblBacteria; AAW90407; AAW90407; NGO_1788. DR GeneID; 3282494; -. DR KEGG; ngo:NGO1788; -. DR PATRIC; 20337220; VBINeiGon24812_2146. DR HOGENOM; HOG000201059; -. DR KO; K03495; -. DR OMA; FRPGYAI; -. DR OrthoDB; EOG6W9X6J; -. DR BioCyc; NGON242231:GI2G-1686-MONOMER; -. DR Proteomes; UP000000535; 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_0000117139. 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; 69624 MW; 71AE232546B197F1 CRC64; MIYPKTYDVI VVGGGHAGTE AALAAARMGA QTLLLTHNIE TLGQMSCNPS IGGIGKGHLV RELDALGGAM ALATDKSGIQ FRRLNASKGA AVRATRAQAD RILYKASIRE MLENQENLDL FQQAVEDVTL EGERISGVIT AMGVEFKARA VVLTAGTFLS GKIHIGLENY EGGRAGDPAA KSLGGRLREL KLPQGRLKTG TPPRIDGRTI DFSQLTEQPG DTPVPVMSVR GNAEMHPRQV SCWITHTNTQ THDIIRSGFD RSPMFTGKIE GVGPRYCPSI EDKINRFADK DSHQIFLEPE GLTTHEYYPN GISTSLPFDI QIALVRSMKG LENAHILRPG YAIEYDYFDP RNLKASLETK TIEGLFFAGQ INGTTGYEEA AAQGLLAGAN AVQYVRGQDP LLLRREQAYL GVLVDDLITK GLNEPYRMFT SRAEYRLQLR EDNADMRLTE DGYKIGLVGE AQWRMFNEKR EAVEREIQRL KTTWYTPQKL AEDEQIRVFG QKLSREANLH DLLRRPNLDY AALMTLEGAM PSENLSAEVI EQVEIQVKYQ GYIDRQNEEI DSRRDIETLK LPDGIDYGRV KGLSAEVQQK LNQHKPETVG QASRISGVTP AAVALLMVHL KRGFKDAK // ID MNMA_NEIG1 Reviewed; 367 AA. AC Q5F7G4; DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 2. DT 16-MAR-2016, entry version 77. 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=NGO1214; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89873.1; 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; AE004969; AAW89873.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F7G4; -. DR SMR; Q5F7G4; 8-359. DR EnsemblBacteria; AAW89873; AAW89873; NGO_1214. DR PATRIC; 20335737; VBINeiGon24812_1427. DR HOGENOM; HOG000218046; -. DR OrthoDB; EOG6RZB5H; -. DR BioCyc; NGON242231:GI2G-1125-MONOMER; -. DR Proteomes; UP000000535; 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_0000121657. 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; 40866 MW; C1D3D5DFC0F8603A CRC64; MNTTSNTSNI IVGLSGGVDS SVTAALLKQQ GYQVRGVFMQ NWENDDNDEY CSIKQDSFDA IAVADIVGID IDIVNFAAQY KDKVFAYFLQ EYSAGRTPNP DVLCNAEIKF KCFLDYAVGQ GADTIATGHY ARKEARNGVH YLLKGLDRNK DQSYFLYRLK PFQLERAIFP LGGLEKPEVR RLAAEFNLPT AAKKDSTGIC FIGERPFREF LQKYLPTDNG KMVTPEGKTI GEHVGLMFYT LGQRKGLGIG GAGEPWFVAA KDLTKNELIV VQGHDHPLLY TRSLVMNDLS FTLPERPKAG RYTCKTRYRM ADAPCELCYL DDETAELVFD EPQWAVTPGQ SAVLYDVDIC LGGGIIQTTD KPVIITR // ID MSBA_NEIG1 Reviewed; 622 AA. AC Q5F4X8; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 82. 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=NGO2165; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90759.1; -; Genomic_DNA. DR RefSeq; WP_010359721.1; NC_002946.2. DR RefSeq; YP_209171.1; NC_002946.2. DR ProteinModelPortal; Q5F4X8; -. DR EnsemblBacteria; AAW90759; AAW90759; NGO_2165. DR GeneID; 3282759; -. DR KEGG; ngo:NGO2165; -. DR PATRIC; 20338186; VBINeiGon24812_2615. DR KO; K11085; -. DR OMA; AYAKEFV; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-2053-MONOMER; -. DR Proteomes; UP000000535; 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 1 622 Lipid A export ATP-binding/permease FT protein MsbA. FT /FTId=PRO_0000271634. 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 622 AA; 68803 MW; 97602CF557BFE3A5 CRC64; MIEKLTFGLF KKEDARSFMR LMAYVRPYKI RIVAALIAIF GVAATESYLA AFIAPLINHG FSAPAAPPDL SAAAGILSTL 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 AEVLSALQAA NLQSLIDASP LGLHQPIGSN GSNLSGGQRQ RVAIARAILK DAPILLLDEA TSALDNESER LVQQALERLM ENRTGIIVAH RLTTVESADR IIVMDGGKII EQGTHDQLMF QNGYYTMLRN ISGKDTAAVQ TA // ID MTGA_NEIG1 Reviewed; 233 AA. AC Q5F6F6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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}; GN OrderedLocusNames=NGO1603; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90231.1; -; Genomic_DNA. DR RefSeq; WP_003695505.1; NC_002946.2. DR RefSeq; YP_208643.1; NC_002946.2. DR ProteinModelPortal; Q5F6F6; -. DR CAZy; GT51; Glycosyltransferase Family 51. DR EnsemblBacteria; AAW90231; AAW90231; NGO_1603. DR GeneID; 3281606; -. DR KEGG; ngo:NGO1603; -. DR PATRIC; 20336742; VBINeiGon24812_1917. DR HOGENOM; HOG000288116; -. DR KO; K03814; -. DR OMA; KEETTFE; -. DR OrthoDB; EOG6HMXCD; -. DR BioCyc; NGON242231:GI2G-1499-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000257675. FT TRANSMEM 8 28 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00766}. SQ SEQUENCE 233 AA; 26643 MW; 95467FBE1195EDA9 CRC64; MFRIVKWLIA LPVGIFIFFN AYVYGNIITY RAVAPHRTAF MSMRMKQFEQ EGRDVALDYR WVPYNRISTN LKKALIASED VRFAGHGGFD WDGIQNAIRR NRNSGEVKAG GSTISQQLAK NLFLNESRNY LRKGEEAAIT AMMEAVTDKN RIFELYLNSI EWHYGVFGAE AASRYFYKKP AADLTKQQAA KLTALVPAPL YYADHPKSKR LRNKTNIVLR RMGSAELPES DTD // ID MQO_NEIG1 Reviewed; 488 AA. AC Q5F5E9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. 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=NGO1980; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90588.1; -; Genomic_DNA. DR RefSeq; WP_003686866.1; NC_002946.2. DR RefSeq; YP_209000.1; NC_002946.2. DR ProteinModelPortal; Q5F5E9; -. DR PRIDE; Q5F5E9; -. DR EnsemblBacteria; AAW90588; AAW90588; NGO_1980. DR GeneID; 3282644; -. DR KEGG; ngo:NGO1980; -. DR PATRIC; 20337725; VBINeiGon24812_2389. DR HOGENOM; HOG000109379; -. DR KO; K00116; -. DR OMA; EPIAATK; -. DR OrthoDB; EOG6X6R8Z; -. DR BioCyc; NGON242231:GI2G-1878-MONOMER; -. DR UniPathway; UPA00223; UER01008. DR Proteomes; UP000000535; 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; 2. 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_1000023810. SQ SEQUENCE 488 AA; 54158 MW; 72BE88D90334543A CRC64; MAEATDVVLV GGGIMSATLG VLLKELEPSW EITLIERLED VALESSNAWN NAGTGHSALC ELNYAPLGAD GVINPARALN IAEQFHVSRQ FWATLVAEGK LEDNSFINAV PHMSLVMNED HCRYLQKRYD VFKTQKLFEN MEFSTDRNKI SDWAPLIMRG RDENQPVAAN YSAEGTDVDF GRLTRQMVKY LQGKGVKTEF NRHVEDIKRE SDGAWVLKTA DTRNPDWQLT LRTRFLFLGA GGGALTLLQK SGIPEGKGYG GLPVSGLFFR NSNPETAEQH NAKVYGQASV GAPPMSVPHL DTRNVDGKRH LMFGPYAGFR SNFLKQGSFM DLPLSIHMDN LYPMLRAGWA NMPLTKYLLG ELRKTKEERF ASLLEYYPEA NPDDWELITA GQRVQIIKKD SEKGGVLQFG TEIVAHADGS LAALLGASPG ASTAVPLMIR LMHQCFPERA PSWEGRLKEL VPGYGIKLNE NPERADEIIA YTAKVLDI // ID MRAY_NEIG1 Reviewed; 360 AA. AC Q5F6L4; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1537; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90173.1; -; Genomic_DNA. DR RefSeq; WP_003689450.1; NC_002946.2. DR RefSeq; YP_208585.1; NC_002946.2. DR EnsemblBacteria; AAW90173; AAW90173; NGO_1537. DR GeneID; 3281456; -. DR KEGG; ngo:NGO1537; -. DR PATRIC; 20336570; VBINeiGon24812_1833. DR HOGENOM; HOG000275122; -. DR KO; K01000; -. DR OMA; HQNKKDT; -. DR OrthoDB; EOG69GZPZ; -. DR BioCyc; NGON242231:GI2G-1439-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000235458. 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 171 193 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; 39346 MW; 61AC03C9EDB08E67 CRC64; MFLWLAHFSN WLTGLNIFQY TTFRAVMAAL TALAFSLMFG PWTIRRLTAL KCGQAVRTDG PQTHLVKNGT PTMGGSLILT AITVSTLLWG NWANPYIWIL LGVLLATGAL GFYDDWRKVV YKDPNGVSAK FKMVWQSSVA VIAGLALFYL AANSANNILI VPFFKQIALP LGVVGFLVLS YLTIVGTSNA VNLTDGLDGL AAFPVVLVAA GLAIFAYVSG HYQFSQYLQL PYVAGANEVA IFCTAMCGAC LGFLWFNAYP AQVFMGDVGA LALGAALGTV AVIVRQEFVL VIMGGLFVVE AVSVMLQVGW YKKTKKRIFL MAPIHHHYEQ KGWKETQVVV RFWIITIVLV LIGLSTLKIR // ID MURB_NEIG1 Reviewed; 346 AA. AC Q5F9J9; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0394; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89138.1; -; Genomic_DNA. DR RefSeq; WP_003692788.1; NC_002946.2. DR RefSeq; YP_207550.1; NC_002946.2. DR ProteinModelPortal; Q5F9J9; -. DR EnsemblBacteria; AAW89138; AAW89138; NGO_0394. DR GeneID; 3283015; -. DR KEGG; ngo:NGO0394; -. DR PATRIC; 20333795; VBINeiGon24812_0475. DR HOGENOM; HOG000284356; -. DR KO; K00075; -. DR OMA; MQNIGAY; -. DR OrthoDB; EOG60CWQ3; -. DR BioCyc; NGON242231:GI2G-373-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000224696. 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; 38033 MW; 6E0DBA13F9442777 CRC64; MQPIRYRTDL TPYNTFGLHA QARAFIALKH ADELRDIVRL PEFDRDTVLW LGGGSNILLM QDYDGLVVHM ENKGIREIAR SDGMVLIEAQ AGEIWHDFVL HTVALGLSGL ENLSLIPGTV GASPVQNIGA YGVEAKDVIH SVRCFDLDTE TFVTLSNADC RFAYRESLFK QEGKGRYVIV SVVFALKTHF VPNLGYGDLA AKVAELSAGR EATAKDVSDA VSAIRNSKLP DPKVLGNVGS FFKNPVVSAE KAATLLQRHP DMPRYPQPDG SVKLAAGWLI DQCRLKGFQI GGAAVHDKQA LVLVNKNNAS ANDVRQLAQH IKFTVFARFQ VELHAEPNWL PTSFSL // ID MRAZ_NEIG1 Reviewed; 151 AA. AC Q5F6K6; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Transcriptional regulator MraZ; GN Name=mraZ {ECO:0000255|HAMAP-Rule:MF_01008}; GN OrderedLocusNames=NGO1545; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90181.1; -; Genomic_DNA. DR RefSeq; WP_003689463.1; NC_002946.2. DR RefSeq; YP_208593.1; NC_002946.2. DR ProteinModelPortal; Q5F6K6; -. DR EnsemblBacteria; AAW90181; AAW90181; NGO_1545. DR GeneID; 3281462; -. DR KEGG; ngo:NGO1545; -. DR PATRIC; 20336588; VBINeiGon24812_1842. DR HOGENOM; HOG000283907; -. DR KO; K03925; -. DR OMA; SNRVEIW; -. DR OrthoDB; EOG6G4W1C; -. DR BioCyc; NGON242231:GI2G-1447-MONOMER; -. DR Proteomes; UP000000535; 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_0000108512. 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; 17186 MW; 74B5F31CD6751E06 CRC64; MFGGAHELSI DSKGRLAVPA KFRDILSRLY TPAVVATLES KHKLLMYPVA EWEKVAAQLL NLKVADNPVL RRFQNLLLHN AEILEWDSAG RVLVPAGLRK RVDFDREVVL VGRANRLELW GREQWEAEMV QALDDDPDEL AFQLSQTDLQ L // ID MURA_NEIG1 Reviewed; 417 AA. AC Q5F5K6; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO1918; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90531.1; -; Genomic_DNA. DR RefSeq; WP_003688069.1; NC_002946.2. DR RefSeq; YP_208943.1; NC_002946.2. DR ProteinModelPortal; Q5F5K6; -. DR SMR; Q5F5K6; 1-417. DR EnsemblBacteria; AAW90531; AAW90531; NGO_1918. DR GeneID; 3282851; -. DR KEGG; ngo:NGO1918; -. DR PATRIC; 20337572; VBINeiGon24812_2313. DR HOGENOM; HOG000075602; -. DR KO; K00790; -. DR OMA; IRTAPHP; -. DR OrthoDB; EOG68M4GK; -. DR BioCyc; NGON242231:GI2G-1821-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000231225. 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; 43820 MW; 527F796F72000A67 CRC64; MDKLKISANG PLNGEITVSG AKNAALPLMC AGLLTSGTLR LKNVPMLADV ATTQKLLQGM GARVLTDNIS EFEINGGTVN NTCAPYELVR TMRASILVLG PTLARFGEAQ VSLPGGCAIG SRPVNQHLKG LEAMGAEIAI EHGYVKAKGK LKGARVAMDV VTVGGTENLL MAATLAEGTT VLENCAIEPE VVDLAECLVK MGAKISGIGT STMIVEGAGE LYGCEHSVVP DRIEAGTFLC AVAITGGRVV LRNAAPKTME VVLDKLVEAG AVIEAGDDWI AIDMRQRPKA VDIRTVVHPG FPTDMQAQFM ALNAVAEGSC RVVETIFENR FMHVPELNRM GANITTEGNT AFVQGVERLS GAVVKATDLR ASASLVIAGL AARGETVVER IYHLDRGYEN IEKKLGSVGA NIERVSG // ID MURG_NEIG1 Reviewed; 355 AA. AC Q5F6L8; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. 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=NGO1533; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90169.1; -; Genomic_DNA. DR RefSeq; WP_003689443.1; NC_002946.2. DR RefSeq; YP_208581.1; NC_002946.2. DR ProteinModelPortal; Q5F6L8; -. DR CAZy; GT28; Glycosyltransferase Family 28. DR EnsemblBacteria; AAW90169; AAW90169; NGO_1533. DR GeneID; 3281523; -. DR KEGG; ngo:NGO1533; -. DR PATRIC; 20336562; VBINeiGon24812_1829. DR HOGENOM; HOG000218321; -. DR KO; K02563; -. DR OMA; EQNALPG; -. DR OrthoDB; EOG61VZFD; -. DR BioCyc; NGON242231:GI2G-1435-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000225069. SQ SEQUENCE 355 AA; 38283 MW; B83843DF89739EE2 CRC64; MGGKTFMLMA GGTGGHIFPA LAVADSLRVR GHHVIWLGSK DSMEERIVPQ YGIRLETLAI KGIRGNGIKR KLMLPFTLYK TVREAQRIIR KHRVECVIGF GGFVTFPGGL AAKLLGVPIV IHEQNAVAGL SNRHLSRWAK RVLYAFPKAF SHEGGLVGNP VRADISNLPV PAERFQGREG RLKILVVGGS LGADVLNKTV PQALALLPEE VRPQMYHQSG RNKLGNLQAD YDALGVKAEC VEFITDMVSA YRDADLVICR AGALTIAELT AAGLGALLVP YPHAVDDHQT ANARFMVQAE AGLLLPQTQL TAEKLAEILG SLNREKCLKW AENARTLALP HSADDVAEAA IACAA // ID MURC_NEIG1 Reviewed; 468 AA. AC Q5F6L9; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 09-DEC-2015, entry version 83. 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=NGO1532; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW90168.1; 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; AE004969; AAW90168.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_010951291.1; NC_002946.2. DR RefSeq; YP_208580.3; NC_002946.2. DR ProteinModelPortal; Q5F6L9; -. DR SMR; Q5F6L9; 3-465. DR EnsemblBacteria; AAW90168; AAW90168; NGO_1532. DR GeneID; 3281507; -. DR KEGG; ngo:NGO1532; -. DR PATRIC; 20336560; VBINeiGon24812_1828. DR HOGENOM; HOG000256031; -. DR KO; K01924; -. DR OrthoDB; EOG64BQ73; -. DR BioCyc; NGON242231:GI2G-1434-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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 1 468 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_0000242566. FT NP_BIND 112 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00046}. SQ SEQUENCE 468 AA; 50194 MW; CB32AB59652B38B0 CRC64; MKNRVSNIHF VGIGGVGMSG IAEVLHNLGF KVSGSDQARN AATEHLSSLG IQVYPGHTAE HVNGADVVVA STAVKKENPE VVAALERQIP VIPRALMLAE LMRFRDGIAI AGTHGKTTTT SLTASILGAA GLDPTFVIGG KLNAAGTNAR LGKGEYIVAE ADESDASFLH LTPIMSVVTN IDEDHMDTYG HSVEKLHQAF IDFIHRMPFY GKAFLCVDSE HVRAILPKVS KPYATYGLDD TADIYATDIE NVGAQMKFTV HVQMKGHEQG SFEVVLNMPG RHNVLNALAA IGVALEVGAS VEAIQKGLLG FEGVGRRFQK YGDIKLPNGG TALLVDDYGH HPVEMAATLA AARGAYPEKR LVLAFQPHRY TRTRDLFEDF TKVLNTVDAL VLTEVYAAGE EPVAAADSRA LARAIRVLGK LEPIYCENVA DLPQMLMNVL QDGDVVLNMG AGSINRVPSA LLELSKQI // ID MURD_NEIG1 Reviewed; 445 AA. AC Q5F6L6; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 82. 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=NGO1535; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90171.1; -; Genomic_DNA. DR RefSeq; WP_003705695.1; NC_002946.2. DR RefSeq; YP_208583.1; NC_002946.2. DR ProteinModelPortal; Q5F6L6; -. DR DNASU; 3281493; -. DR EnsemblBacteria; AAW90171; AAW90171; NGO_1535. DR GeneID; 3281493; -. DR KEGG; ngo:NGO1535; -. DR PATRIC; 20336566; VBINeiGon24812_1831. DR HOGENOM; HOG000049427; -. DR KO; K01925; -. DR OMA; PGIPYTN; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NGON242231:GI2G-1437-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_0000109047. FT NP_BIND 117 123 ATP. {ECO:0000255|HAMAP-Rule:MF_00639}. SQ SEQUENCE 445 AA; 48035 MW; F82B484398EE15D3 CRC64; MTFQNKKILV AGLGGTGISM IAYLRKNGAE VAAYDAELKA ERVAQIGKMF DGLVFYTGRL KDALDNGFDI LALSPGISER QPDIEAFKQN GGRVLGDIEL LADIVNRRGD KVIAITGSNG KTTVTSLVGY LCIKCGLDTV IAGNIGTPVL EAELQREGKK ADVWVLELSS FQLENTESLR PTAATVMNIS EDHLDRYDDL LDYAHTKAEI FRGDGVQVLN ADDVFCRAMK RAGREVKRFS LEHEADFWLE RGTGCLKQGN EDLISTQDIP LQGLHNAANV MAAVALCEAV GLPREALLEH VKTFQGLPHR VEKIGEKNGV VFIDDSKGTN VGATAAAIAG LQNPLFVILG GMGKGQDFTP LRDALKDKAK GVFLIGVDAP QIRRDLDGCG LNLTDCVTLE EAVQTAYAQA EAGDIVLLSP ACASFDMFKG YAHRSEVFIE AFKAL // ID MURI_NEIG1 Reviewed; 270 AA. AC Q5F6P9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 72. 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}; GN OrderedLocusNames=NGO1500; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90138.1; -; Genomic_DNA. DR RefSeq; WP_003689383.1; NC_002946.2. DR RefSeq; YP_208550.1; NC_002946.2. DR ProteinModelPortal; Q5F6P9; -. DR EnsemblBacteria; AAW90138; AAW90138; NGO_1500. DR GeneID; 3281584; -. DR KEGG; ngo:NGO1500; -. DR PATRIC; 20336474; VBINeiGon24812_1785. DR HOGENOM; HOG000262396; -. DR KO; K01776; -. DR OMA; VYGCTHY; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NGON242231:GI2G-1404-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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_1000047589. 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; 29515 MW; 913E8ABBA2805564 CRC64; MENIGRQRPI GVFDSGIGGL TNVRALMERL PMENIIYFGD TARVPYGTKS KATIENFSMQ IVDFLLGHDV KAMVIACNTI AAVAGRKIRQ KTGNMPVLDV ISAGAKAALA TTRNNKIGII ATNTTVNSNA YARAIHRDNP DTLVRTQAAP LLVPLVEEGW LEHEVTRLTV CEYLKPLLAD GIDTLVLGCT HFPLLKPLIG REAHNVALVD SAITTAEETA RVLAQEGLLD TGNNNPDYRF YVSDIPLKFR TIGERFLGRT MEQIEMVSLG // ID NADD_NEIG1 Reviewed; 201 AA. AC Q5F556; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244}; DE EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244}; DE AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244}; DE AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244}; DE AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244}; DE Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244}; GN Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244}; GN OrderedLocusNames=NGO2080; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide CC (NaAD). {ECO:0000255|HAMAP-Rule:MF_00244}. CC -!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide = CC diphosphate + deamido-NAD(+). {ECO:0000255|HAMAP-Rule:MF_00244}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido- CC NAD(+) from nicotinate D-ribonucleotide: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00244}. CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP- CC Rule:MF_00244}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90681.1; -; Genomic_DNA. DR RefSeq; WP_003687035.1; NC_002946.2. DR RefSeq; YP_209093.1; NC_002946.2. DR ProteinModelPortal; Q5F556; -. DR EnsemblBacteria; AAW90681; AAW90681; NGO_2080. DR GeneID; 3282837; -. DR KEGG; ngo:NGO2080; -. DR PATRIC; 20337993; VBINeiGon24812_2519. DR HOGENOM; HOG000262781; -. DR KO; K00969; -. DR OMA; HLIMAQY; -. DR OrthoDB; EOG6F55KJ; -. DR BioCyc; NGON242231:GI2G-1975-MONOMER; -. DR UniPathway; UPA00253; UER00332. DR Proteomes; UP000000535; 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_0000181428. SQ SEQUENCE 201 AA; 22237 MW; 705154C1A1E8DAAE CRC64; MKKIGLFGGT FDPIHNGHFH IARAFADEIG LDAVVFLPAG GPYHKDAASA SAADRLAMVE LATAEDARFA VSDCDIVRES ATYTFDTVQI FRRQFPSAQL WWLMGSDSLL KLHTWKKWQL LVRETNIAVA MRQGDSLHQT PRELHAWLGN ALQDGSVRIL SAPMHNVSST EIRRNLSAAG VSDGIPPAAA RYIRKHGLYE K // ID MUTS_NEIG1 Reviewed; 864 AA. AC Q5F5J4; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO1930; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90543.1; -; Genomic_DNA. DR RefSeq; WP_003688085.1; NC_002946.2. DR RefSeq; YP_208955.1; NC_002946.2. DR ProteinModelPortal; Q5F5J4; -. DR EnsemblBacteria; AAW90543; AAW90543; NGO_1930. DR GeneID; 3282689; -. DR KEGG; ngo:NGO1930; -. DR PATRIC; 20337598; VBINeiGon24812_2326. DR HOGENOM; HOG000221407; -. DR KO; K03555; -. DR OMA; DSKEHAV; -. DR OrthoDB; EOG6Q5NPV; -. DR BioCyc; NGON242231:GI2G-1833-MONOMER; -. DR Proteomes; UP000000535; 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_0000224384. FT NP_BIND 607 614 ATP. {ECO:0000255|HAMAP-Rule:MF_00096}. SQ SEQUENCE 864 AA; 95149 MW; 612F7F3FDD52CD35 CRC64; MSKSAVSPMM QQYLGIKAQH TDKLVFYRMG DFYELFLDDA VEAAKLLDIT LTTRGQMDGV PIKMAGVPFH AAEQYLARLV KLGKSVAICE QVGEVGAGKG PVERKVVRIV TPGTLTDSAL LEDKETNRIV AVSPDKKYIG LAWASLQSGE FKTKLTTADK LNDELARLQA AEILLPDSKN APQLQTASGV TRLNAWQFAA DAGEKLLTEY FGCQDLRGFG LDSKEHAVSI GAAGALLNYI RLTQNLMPQH LDGLSLETDS QYIGMDAATR RNLEITQTLS GKKTPTLFSI LDGCATHMGS RLLALWLHHP LRNRAHIRAR QEAVTALESQ YEPLQCHLKS IADIERIAAR IAVGNARPRD LASLRDSLFE LAQIDLSATG SSLLETLKAV FPETLPVAET LKAAVMPEPS VWLKDGNVIN HGFHPELDEL RRIQNHGDEF LLDLEAKERE RTGLSTLKVE FNRVHGFYIE LSKTQAEQAP ADYQRRQTLK NAERFITPEL KAFEDKVLTA QDQALALEKQ LFDGVLKNLR TALPQLQKAA KAAAALDVLS TFSALAKERN FVRPEFADYP VVHIENGRHP VVEQQVRHFT ANHTDLDHKH RLMLLTGPNM GGKSTYMRQV ALIVLLAHTG CFVPADAATI GPVDQIFTRI GASDDLASNR STFMVEMSET AYILHHATEQ SIVLMDEVGR GTSTFDGLAL AHAIAEHLLQ KNKSFSLFAT HYFELTYLPE AHAAAVNMHL SALEQGRDIV FLHQIQPGPA GKSYGIAVAK LAGLPVRALK AAQKHLNGLE NQAAANRPQL DIFSTMPSEK GDEPNVDCFV DKAEEKHFEG ILAAALENLD PDSLTPREAL SELYRLKDLC KSVS // ID MUTL_NEIG1 Reviewed; 658 AA. AC Q5F8M6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. 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=NGO0744; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89461.1; -; Genomic_DNA. DR RefSeq; WP_003698476.1; NC_002946.2. DR RefSeq; YP_207873.1; NC_002946.2. DR PDB; 3NCV; X-ray; 2.40 A; A/B=460-658. DR PDBsum; 3NCV; -. DR ProteinModelPortal; Q5F8M6; -. DR EnsemblBacteria; AAW89461; AAW89461; NGO_0744. DR GeneID; 3282588; -. DR KEGG; ngo:NGO0744; -. DR PATRIC; 20334628; VBINeiGon24812_0886. DR HOGENOM; HOG000256550; -. DR KO; K03572; -. DR OMA; QFLFINN; -. DR OrthoDB; EOG6P8TMH; -. DR BioCyc; NGON242231:GI2G-701-MONOMER; -. DR EvolutionaryTrace; Q5F8M6; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; KW Reference proteome. FT CHAIN 1 658 DNA mismatch repair protein MutL. FT /FTId=PRO_1000010046. FT STRAND 469 474 {ECO:0000244|PDB:3NCV}. FT TURN 475 477 {ECO:0000244|PDB:3NCV}. FT STRAND 478 483 {ECO:0000244|PDB:3NCV}. FT STRAND 486 491 {ECO:0000244|PDB:3NCV}. FT HELIX 492 511 {ECO:0000244|PDB:3NCV}. FT STRAND 516 526 {ECO:0000244|PDB:3NCV}. FT HELIX 529 544 {ECO:0000244|PDB:3NCV}. FT STRAND 548 550 {ECO:0000244|PDB:3NCV}. FT STRAND 556 563 {ECO:0000244|PDB:3NCV}. FT HELIX 571 582 {ECO:0000244|PDB:3NCV}. FT HELIX 595 602 {ECO:0000244|PDB:3NCV}. FT STRAND 606 608 {ECO:0000244|PDB:3NCV}. FT HELIX 616 627 {ECO:0000244|PDB:3NCV}. FT TURN 630 633 {ECO:0000244|PDB:3NCV}. FT STRAND 640 646 {ECO:0000244|PDB:3NCV}. FT HELIX 647 652 {ECO:0000244|PDB:3NCV}. SQ SEQUENCE 658 AA; 71602 MW; 5B95436331D8C422 CRC64; MPRIAALPDH LVNQIAAGEV VERPANALKE IVENSIDAGA TAVDVELEGG GIRLIRVGDN GGGIHPDDIE LALHRHATSK IKTLNDLEHV ASMGFRGEGL ASIASVSRLT LTSRQEDSSH ATQVKAEDGK LSSPTAAAHP VGTTIEAAEL FFNTPARRKF LKSENTEYAH CATMLERLAL AHPHIAFSLK RDGKQVFKLP AQSLHERIAA IVGDDFQTAS LEIDSGNSAL RLYGAIAKPT FAKGKTDKQY CFVNHRFVRD KVMLHAVKQA YRDVLHNALT PAFVLFLELP PEAVDVNVHP TKTEIRFRDS RQVHQLVFHT LNKALADTRA NLTESVSNAG EVLHDITGVT PAPMPSENDG ENLFDSASNH PTGNKPDTRN AFGSSGKTAP MPYQAARAPQ QHSLSLRESR AAMDTYAELY KKTDDIDLEL SQFEQARFGN MPSETPAHKT DTPLSDGIPS QSELPPLGFA IAQLLGIYIL AQAEDSLLLI DMHAAAERVN YEKMKRQRQE NGNLQSQHLL IPVTFAASHE ECAALADHAE TLAGFGLELS DMGGNTLAVR AAPVMLGKSD VVSLARDVLG ELAQVGSSQT IASHENRILA TMSCHGSIRA GRRLTLPEMN ALLRDMENTP RSNQCNHGRP TWVKLTLKEL DTLFLRGQ // ID NADK_NEIG1 Reviewed; 296 AA. AC Q5F9K3; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0390; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89134.1; -; Genomic_DNA. DR RefSeq; WP_003687818.1; NC_002946.2. DR RefSeq; YP_207546.1; NC_002946.2. DR ProteinModelPortal; Q5F9K3; -. DR EnsemblBacteria; AAW89134; AAW89134; NGO_0390. DR GeneID; 3283019; -. DR KEGG; ngo:NGO0390; -. DR PATRIC; 20333787; VBINeiGon24812_0471. DR HOGENOM; HOG000227221; -. DR KO; K00858; -. DR OMA; APKSNVF; -. DR OrthoDB; EOG6PZXDR; -. DR BioCyc; NGON242231:GI2G-369-MONOMER; -. DR Proteomes; UP000000535; 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_0000229657. 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; 32876 MW; 60DCFC7C92489D7A CRC64; MNSPFHNIGI VTRPNTPDIQ DTAHTLITFL KQHGFTVYLD EVGVRECCIY TQDTDGCHIV NKTELGQYCD LVAVLGGDGT FLSAAREITP RAVPIIGINQ GHLGFLTQIP REYMTDKLLP VLEGKYLAEE RILIEAALIR EGKTAERALA LNDAVLSRGG AGQMIEFEVF VNQEFVYTQR SDGLIVSTPT GSTAYSLAAG GPIMQAGLHA FTLVPICPQS MTNRPIAIPD TSEIEILVTQ GGDARVHFDG QSFIDVQNLD RIIIRRYHNP LRILHPTDYQ YFKTLRQKLH WGEQLV // ID NAGZ_NEIG1 Reviewed; 361 AA. AC Q5FA94; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO0135; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88893.1; -; Genomic_DNA. DR RefSeq; WP_003704881.1; NC_002946.2. DR RefSeq; YP_207305.1; NC_002946.2. DR ProteinModelPortal; Q5FA94; -. DR CAZy; GH3; Glycoside Hydrolase Family 3. DR EnsemblBacteria; AAW88893; AAW88893; NGO_0135. DR GeneID; 3281288; -. DR KEGG; ngo:NGO0135; -. DR PATRIC; 20333181; VBINeiGon24812_0173. DR HOGENOM; HOG000248526; -. DR KO; K01207; -. DR OMA; DMVLICN; -. DR OrthoDB; EOG6BCT06; -. DR BioCyc; NGON242231:GI2G-123-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000535; 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_0000234917. 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; 39033 MW; AABBC553B4BEA82C CRC64; MTVPHIPRGP VMADIAAFRL TEEEKQRLLD PAIGGIILFR RNFQNIEQLK TLTAEIKALR TPELIIAVDH EGGRVQRFIE GFTRLPAMNV LGQIWDKDGA SAAETAAGQV GRVLATELSA CGIDLSFTPV LDLDWGNCAV IGNRSFHRNP EAVARLALAL QKGLAKGGMK SCGKHFPGHG FVEGDSHLVL PEDGRSLDEL EAADLAPFRI MSREGMAAVM PAHVVYPQVD TKPAGFSEIW LKQILRRDIG FKGVIFSDDL TMEGACGAGG IKERARISFE AGCDIVLVCN RPDLVDELRD GFTIPDNQDL AGRWQYMENS LGHEAVQAVM QTMGFQAAQA FVAGLASPQD TAGGVKVGEA F // ID NADA_NEIG1 Reviewed; 370 AA. AC Q5F6I7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO1567; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90200.1; -; Genomic_DNA. DR RefSeq; WP_003689487.1; NC_002946.2. DR RefSeq; YP_208612.1; NC_002946.2. DR ProteinModelPortal; Q5F6I7; -. DR EnsemblBacteria; AAW90200; AAW90200; NGO_1567. DR GeneID; 3281323; -. DR KEGG; ngo:NGO1567; -. DR PATRIC; 20336644; VBINeiGon24812_1868. DR HOGENOM; HOG000222769; -. DR KO; K03517; -. DR OMA; IAHPECE; -. DR OrthoDB; EOG6DJZ56; -. DR BioCyc; NGON242231:GI2G-1468-MONOMER; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000000535; 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_1000024958. 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; 40055 MW; 2EA16C1CF3017C9F CRC64; MQTAARRSFD YDMPLIQTPT SACQIRQAWA KVADTPDHET AGRLKDEIKV LLKRKNAVLV AHYYVDPLIQ DLALETGGCV GDSLEMARFG AEHEAGTLVV AGVRFMGESA KILCPEKTVL MPDLEAECSL DLGCPEEAFS AFCDQHPDRT VAVYANTSAA VKARADWVVT SSVALEIVSY LKSRGEKLIW GPDRHLGDYI RRETGADMLL WQGSCIVHNE FKGQELAALK AEHPDAVVLV HPESPQSVIE LGDVVGSTSK LLKAAVSRPE KKFIVATDLG ILHEMQKQAP DKEFIAAPTA GNGGSCKSCA FCPWMAMNSL GGIKHALTGG RNEILLDRKL GEAAKLPLQR MLDFAAGLKR GDVFNGMGPA // ID NNRD_NEIG1 Reviewed; 296 AA. AC Q5F8G9; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. 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=nnrD {ECO:0000255|HAMAP-Rule:MF_01965}; GN OrderedLocusNames=NGO0804; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89518.1; -; Genomic_DNA. DR RefSeq; WP_003688608.1; NC_002946.2. DR RefSeq; YP_207930.1; NC_002946.2. DR ProteinModelPortal; Q5F8G9; -. DR EnsemblBacteria; AAW89518; AAW89518; NGO_0804. DR GeneID; 3281980; -. DR KEGG; ngo:NGO0804; -. DR PATRIC; 20334762; VBINeiGon24812_0951. DR HOGENOM; HOG000024581; -. DR OMA; FTPHQME; -. DR OrthoDB; EOG6C018D; -. DR BioCyc; NGON242231:GI2G-760-MONOMER; -. DR Proteomes; UP000000535; 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_0000416146. 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; 30241 MW; 05E38075637EC2FB CRC64; MFPVFHLSGE SRRRMLQTAL RFPHVFKARA EDSHKGTFGT LAVVGGSAGM SGAPVLAASA AMYLGCGKVR AGFNQDTLPF AVIAGFPEIM LDTADGLTKR QGINAWTAGC GLGTDAAAVE TVAAVLARNR DEAVVLDADA LNILSTDAET RNLARGCKNL ILTPHPAEAA RLLGTTVAQV QADRTAAVRK IGAILGATVV LKGHKTLVAA SDTEIYVNES GNAGLATAGS GDVLGGIIGS LLAQGVPVFE AACAGAWLHG AAADVIKESA GIAAGLSAGE IAPAARWLRN WITESM // ID NQRA_NEIG1 Reviewed; 447 AA. AC Q5F6Y0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO1413; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90057.1; -; Genomic_DNA. DR RefSeq; WP_003689268.1; NC_002946.2. DR RefSeq; YP_208469.1; NC_002946.2. DR EnsemblBacteria; AAW90057; AAW90057; NGO_1413. DR GeneID; 3281162; -. DR KEGG; ngo:NGO1413; -. DR PATRIC; 20336233; VBINeiGon24812_1665. DR HOGENOM; HOG000273652; -. DR KO; K00346; -. DR OMA; DYHGMKP; -. DR OrthoDB; EOG6VMTG5; -. DR BioCyc; NGON242231:GI2G-1322-MONOMER; -. DR Proteomes; UP000000535; 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_1000060120. SQ SEQUENCE 447 AA; 48742 MW; 98CEC430E339A817 CRC64; MIKIKKGLNL PIAGRPEQVI YDGPAITEVA LLGEEYVGMR PSMKIKEGEA VKKGQVLFED KKNPGVVFTA PASGKIAAIH RGEKRVLQSV VIAVEGNDEI EFERYVPEAL AKLSSEKVRR NLIQSGLWTA LRTRPFSKIP AVDAEPFAIF VNAMDTNPLA ADPTVIIKEA AEDFKRGLLV LSRLTERKIH VCKAAGADVP SENAANIETH EFGGPHPAGL SGTHIHFIEP VGANKTVWTI NYQDVIAIGR LFVTGRLNTE RVVALGGLQV NKPRLLRTVL GAKVSQLTAG ELVDADNRVI SGSVLNGAIA QGAHDYLGRY HNQISVIEEG RSKELFGWVA PQPDKYSITR TTLGHFLKNK LFKFTTAVNG GDRAMVPIGT YERVMPLDIL PTLLLRDLIV GDTDSAQALG CLELDEEDLA LCSFVCPGKY EYGPLLRKVL ETIEKEG // ID NQRD_NEIG1 Reviewed; 208 AA. AC Q5F6X7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO1416; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90060.1; -; Genomic_DNA. DR RefSeq; WP_002214361.1; NC_002946.2. DR RefSeq; YP_208472.1; NC_002946.2. DR EnsemblBacteria; AAW90060; AAW90060; NGO_1416. DR GeneID; 3281797; -. DR KEGG; ngo:NGO1416; -. DR PATRIC; 20336239; VBINeiGon24812_1668. DR HOGENOM; HOG000279325; -. DR KO; K00349; -. DR OMA; PSKIRII; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; NGON242231:GI2G-1325-MONOMER; -. DR Proteomes; UP000000535; 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_1000060155. 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; 22700 MW; 009965AC96F6011C CRC64; MADMKRLKHL MFSPFIDNNP IALQVLGICS ALAVTTKLQT AIVMGISVAL VTGFSSFFIS LVRNYIPNSI RIIVQMAIIA SLVTLVDQLL QAFAYELSKQ LSVFVGLIIT NCIVMGRAEA FAMKEPPLES LIDGIGNGAG YGMMLLVVAT VRELIGSGKL LGYTVFQTVQ DGGWYQTNGL FLLAPSAFFI IGFLIWGLRT WKPEQAEE // ID NQRE_NEIG1 Reviewed; 197 AA. AC Q5F6X6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1417; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90061.1; -; Genomic_DNA. DR RefSeq; WP_003689273.1; NC_002946.2. DR RefSeq; YP_208473.1; NC_002946.2. DR EnsemblBacteria; AAW90061; AAW90061; NGO_1417. DR GeneID; 3281763; -. DR KEGG; ngo:NGO1417; -. DR PATRIC; 20336241; VBINeiGon24812_1669. DR HOGENOM; HOG000279324; -. DR KO; K00350; -. DR OMA; YFLGMCS; -. DR OrthoDB; EOG6GBMG7; -. DR BioCyc; NGON242231:GI2G-1326-MONOMER; -. DR Proteomes; UP000000535; 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_1000060201. 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; 21180 MW; 1A42024900546600 CRC64; MEHYLSLFIK SVFIENMALS FFLGMCTFLA VSKKVSTAFG LGVAVIFVLG LSVPANQLVY SLLKDGAIVE GVDLTFLKFI TFIGVIAALV QILEMFLDKF VPALYNALGI YLPLITVNCA IFGAVSFMAQ REYDFGESVV YGFGAGLGWM LAIVALAGIT EKMKYSDAPK GLKGLGITFI AAGLMAMAFM SFSGIQL // ID NQRF_NEIG1 Reviewed; 405 AA. AC Q5F6X5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 90. 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=NGO1418; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90062.1; -; Genomic_DNA. DR RefSeq; WP_010951261.1; NC_002946.2. DR RefSeq; YP_208474.1; NC_002946.2. DR ProteinModelPortal; Q5F6X5; -. DR SMR; Q5F6X5; 126-404. DR EnsemblBacteria; AAW90062; AAW90062; NGO_1418. DR GeneID; 3281779; -. DR KEGG; ngo:NGO1418; -. DR PATRIC; 20336243; VBINeiGon24812_1670. DR HOGENOM; HOG000263661; -. DR KO; K00351; -. DR OMA; EEHGIIM; -. DR OrthoDB; EOG6JHRM2; -. DR BioCyc; NGON242231:GI2G-1327-MONOMER; -. DR Proteomes; UP000000535; 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_1000080585. 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 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; 45173 MW; 4AF643459B338605 CRC64; MEIILGIVMF TVIVLALALM ILFAKSKLVS EGDITIKVND EKELTMPAGG KLLGALASQG IFVPSACGGG GSCGQCRVVV KSGGGDILPT ELSHISKREA REGCRLSCQV NVKTDMDIEV PEEVFGVKKW ECTVISNDNK ATFIKELKLA IPEGEEVPFR AGGYIQIEAP PHTVAYKDFD IPKEYHEDWD KYNLWQYVSK VNEPILRAYS MASYPEEKGI IMLNVRIATP PPRVPNAPPG QMSSYIWSLK PGDKVTISGP FGEFFAKDTD AEMVFIGGGA GMAPMRSHIF DQLKRLHSKR KITFWYGARS KREMFYVEDF DQLAAEFPNF TWHVALSDPL PEDNWDGYTG FIHNVVYENH LKNHEAPEDC EFYMCGPPIM NQSVIKMLKD LGVEDENILL DDFGG // ID NUON_NEIG1 Reviewed; 481 AA. AC Q5F629; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; DE EC=1.6.5.11 {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; DE AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445}; GN Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; GN OrderedLocusNames=NGO1737; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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_00445}. CC -!- CATALYTIC ACTIVITY: NADH + a quinone = NAD(+) + a quinol. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00445}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00445}. CC -!- SIMILARITY: Belongs to the complex I subunit 2 family. CC {ECO:0000255|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; AE004969; AAW90358.1; -; Genomic_DNA. DR RefSeq; WP_003694246.1; NC_002946.2. DR RefSeq; YP_208770.1; NC_002946.2. DR EnsemblBacteria; AAW90358; AAW90358; NGO_1737. DR GeneID; 3281148; -. DR KEGG; ngo:NGO1737; -. DR PATRIC; 20337072; VBINeiGon24812_2076. DR HOGENOM; HOG000100795; -. DR KO; K00343; -. DR OMA; MLAIAWK; -. DR OrthoDB; EOG64JFNZ; -. DR BioCyc; NGON242231:GI2G-1633-MONOMER; -. DR Proteomes; UP000000535; 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; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Reference proteome; Transmembrane; KW Transmembrane helix; Transport; Ubiquinone. FT CHAIN 1 481 NADH-quinone oxidoreductase subunit N. FT /FTId=PRO_0000391185. FT TRANSMEM 11 31 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 38 58 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 74 94 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 103 123 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 128 148 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 163 183 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 208 228 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 241 261 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 272 292 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 300 322 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 332 352 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 368 388 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 404 424 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. FT TRANSMEM 450 470 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00445}. SQ SEQUENCE 481 AA; 51833 MW; E82A5E649CBBF116 CRC64; MNWSDLNLMP ALPEVALLSL LVLLLPADLW ASDDKCRWTH YGALATVAVT AAVQLAVWEQ GSTSSFNGMY IADGMSRLAK MVLYALTFVL FVYAKPYNQV RGIFKGEFYT LSLFALLGMS VMVSAGHFLT AYIGLELLSL ALYALIALRR DSGFAAEAAL KYFVLGALAS GLLLYGISMV YGATGSLEFA GVLASSFNEE ANEWLLKLGL VFIVVAVAFK LGAVPFHMWM PDVYHGAPTS VTALVGTAPK IAAVVFAFRI LVTGLGTVHH DWSLMFALLA AASLLVGNLA AIMQTNIKRM LAYSTVSHMG FILLAFMAGA VGFAAGLYYA ITYALMAAAG FGVLMVLSDG DNECENISDL AGLNQHRVWL AFLMLLVMFS MAGIPPLMGF YAKFGVIMAL LKQGYVWLSV FAVVMSLVGA FYYLRVVKVM YFDESGRARP AAGGNNAAKS LLSVNALLLV LWGIMPQTVI DWCAKALENT L // ID NUOI_NEIG1 Reviewed; 159 AA. AC Q5F623; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. 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=NGO1743; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90364.1; -; Genomic_DNA. DR RefSeq; WP_002216341.1; NC_002946.2. DR RefSeq; YP_208776.1; NC_002946.2. DR ProteinModelPortal; Q5F623; -. DR EnsemblBacteria; AAW90364; AAW90364; NGO_1743. DR GeneID; 23783404; -. DR GeneID; 3281187; -. DR KEGG; ngo:NGO1743; -. DR PATRIC; 20337084; VBINeiGon24812_2082. DR HOGENOM; HOG000228289; -. DR KO; K00338; -. DR OMA; DLFKCIY; -. DR OrthoDB; EOG6XM7H5; -. DR BioCyc; NGON242231:GI2G-1639-MONOMER; -. DR Proteomes; UP000000535; 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_0000250915. 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 NUOD_NEIG1 Reviewed; 418 AA. AC Q5F618; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO1748; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90369.1; -; Genomic_DNA. DR RefSeq; WP_003689951.1; NC_002946.2. DR RefSeq; YP_208781.1; NC_002946.2. DR ProteinModelPortal; Q5F618; -. DR EnsemblBacteria; AAW90369; AAW90369; NGO_1748. DR GeneID; 3281201; -. DR KEGG; ngo:NGO1748; -. DR PATRIC; 20337098; VBINeiGon24812_2089. DR HOGENOM; HOG000228264; -. DR KO; K00333; -. DR OMA; IMGTSME; -. DR OrthoDB; EOG62G5MP; -. DR BioCyc; NGON242231:GI2G-1644-MONOMER; -. DR Proteomes; UP000000535; 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; -; 1. 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_0000357865. SQ SEQUENCE 418 AA; 47594 MW; 335F6FC85E5CF718 CRC64; MANKLRNYTI NFGPQHPAAH GVLRMILELD GEQIVRADPH IGLLHRGTEK LAETKTYLQA LPYMDRLDYV SMMVNEQAYC LAVEKLAGID VPIRAQYIRV MFAEVTRILN HLMGIGSHAF DIGAMTAILY AFRDREELMD LYEAVSGARM HAAYFRPGGV YRDLPGFMPK YESSKFRNAK VLKQLNESRE GTMLDFIDAF CERFPKNIDT LETLLTDNRI WKQRTVGIGV VSPERAMQKG FTGVMLRGSG VEWDVRKTQP YEVYDKMDFD IPVGVNGDCY DRYLCRMEEM RQSVRIIKQC ADWLRVNPGP VITANHKFAP PKRTEMKTGM EDLIHHFKLF TEGMHVPEGE TYTAVEHPKG EFGVYIISDG ANKPYRLKIR APGFAHLQGM DEMAKGHMLA DVVAIIGTQD IVFGEVDR // ID NUSB_NEIG1 Reviewed; 141 AA. AC Q5F9Y0; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO0256; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89007.1; -; Genomic_DNA. DR RefSeq; WP_002241285.1; NC_002946.2. DR RefSeq; YP_207419.1; NC_002946.2. DR ProteinModelPortal; Q5F9Y0; -. DR EnsemblBacteria; AAW89007; AAW89007; NGO_0256. DR GeneID; 3281560; -. DR KEGG; ngo:NGO0256; -. DR PATRIC; 20333469; VBINeiGon24812_0315. DR HOGENOM; HOG000281868; -. DR KO; K03625; -. DR OMA; WIGVYEF; -. DR OrthoDB; EOG6RJV9B; -. DR BioCyc; NGON242231:GI2G-239-MONOMER; -. DR Proteomes; UP000000535; 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_0000265549. SQ SEQUENCE 141 AA; 15997 MW; 274C8151B4A5BCFC CRC64; MKTARRRSRE LAVQAVYQSL INRTAAPEIA KNIREMSDFA KADEELFNKL FFGTQTNAAD YIQKIRPLLD RDEKDLNPIE RAVLLTACHE LSAMPETPYP VIINEAIEVT KTFGGTDGHK FVNGILDKLA AQIRPDEPKR R // ID NUOB_NEIG1 Reviewed; 160 AA. AC Q5F616; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1750; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90371.1; -; Genomic_DNA. DR RefSeq; WP_003703228.1; NC_002946.2. DR RefSeq; YP_208783.1; NC_002946.2. DR ProteinModelPortal; Q5F616; -. DR EnsemblBacteria; AAW90371; AAW90371; NGO_1750. DR GeneID; 3281198; -. DR KEGG; ngo:NGO1750; -. DR PATRIC; 20337102; VBINeiGon24812_2091. DR HOGENOM; HOG000228249; -. DR KO; K00331; -. DR OMA; PVMRRVY; -. DR OrthoDB; EOG62K20C; -. DR BioCyc; NGON242231:GI2G-1646-MONOMER; -. DR Proteomes; UP000000535; 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_0000358427. 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; 17603 MW; ED0D1D5ACDC299AF CRC64; MGIEGVLKKG FITTSADTVL NHMRTGSLWP VTFGLACCAV EMMHAGMARY DLDRFGIIFR PSPRQADLMI VAGTLTNKMA PALRRVYDQL AEPRWVLSMG SCANGGGYYH YSYSVVRGAD RVVPVDVYVP GCPPTAEALI YGLIQLQQKI KRTSTIARDE // ID NUOC_NEIG1 Reviewed; 197 AA. AC Q5F617; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO1749; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90370.1; -; Genomic_DNA. DR RefSeq; WP_003689952.1; NC_002946.2. DR RefSeq; YP_208782.1; NC_002946.2. DR ProteinModelPortal; Q5F617; -. DR EnsemblBacteria; AAW90370; AAW90370; NGO_1749. DR GeneID; 3281195; -. DR KEGG; ngo:NGO1749; -. DR PATRIC; 20337100; VBINeiGon24812_2090. DR HOGENOM; HOG000009799; -. DR KO; K00332; -. DR OMA; THNWRLR; -. DR OrthoDB; EOG60PHFK; -. DR BioCyc; NGON242231:GI2G-1645-MONOMER; -. DR Proteomes; UP000000535; 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_0000358144. SQ SEQUENCE 197 AA; 22841 MW; 4396866AD66989FF CRC64; MASIQNLYET VVGVLGDQAG KVISALGEIT VECLPEHYIS VMTALHDHED LHFELLVDLC GVDYSTYKNE AWQGKRFAVV SQLLSVKNNQ RIRVRVWVSD DDFPVVESVA DIYNSADWYE REAFDLYGIM FNNHPDLRRI LTDYGFVGHP FRKDFPISGY VEMRYDEEQK RVIYQPVTIE PREITPRIVR EENYGGQ // ID OBG_NEIG1 Reviewed; 384 AA. AC Q5F5D9; DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454}; DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:26122105}; DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454}; GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=NGO1990; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION RP PHENOTYPE, GTP-BINDING, AND MUTAGENESIS OF 192-THR-THR-193. RC STRAIN=ATCC 700825 / FA 1090; RX PubMed=26122105; DOI=10.1186/s12866-015-0453-1; RA Zielke R.A., Wierzbicki I.H., Baarda B.I., Sikora A.E.; RT "The Neisseria gonorrhoeae Obg protein is an essential ribosome- RT associated GTPase and a potential drug target."; RL BMC Microbiol. 15:129-129(2015). 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; the half-life of the CC GTP-bound state is about 50 minutes (PubMed:26122105). Plays a CC role in control of the cell cycle, stress response, ribosome CC biogenesis and in those bacteria that undergo differentiation, in CC morphogenesis control (By similarity). {ECO:0000255|HAMAP- CC Rule:MF_01454, ECO:0000269|PubMed:26122105}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454, CC ECO:0000269|PubMed:26122105}; CC Note=Optimal binding to GTP occurs between 5-10 mM Mg(2+), binding CC to GDP is inhibited at > 1 mM Mg(2+). CC {ECO:0000269|PubMed:26122105}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454, CC ECO:0000269|PubMed:26122105}. Note=Associates with 50S ribosomal CC subunits. A small amount may associate with the cell inner CC membrane. {ECO:0000269|PubMed:26122105}. CC -!- INDUCTION: Expressed constitutively, reaches maximum expression in CC early log phase and remains constant until stationary phase. CC Similar levels are seen when cells are grown under iron-limiting CC conditions, anoxically or in the presence of human serum, which CC mimic clinical infections (at protein level). CC {ECO:0000269|PubMed:26122105}. CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted. CC {ECO:0000269|PubMed:26122105}. 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; AE004969; AAW90598.1; -; Genomic_DNA. DR RefSeq; WP_003686881.1; NC_002946.2. DR RefSeq; YP_209010.1; NC_002946.2. DR ProteinModelPortal; Q5F5D9; -. DR EnsemblBacteria; AAW90598; AAW90598; NGO_1990. DR GeneID; 3282634; -. DR KEGG; ngo:NGO1990; -. DR PATRIC; 20337749; VBINeiGon24812_2401. DR HOGENOM; HOG000019084; -. DR KO; K03979; -. DR OMA; LVDFRYK; -. DR OrthoDB; EOG6H1Q1M; -. DR BioCyc; NGON242231:GI2G-1888-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. 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 1: Evidence at protein level; KW Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 384 GTPase Obg. FT /FTId=PRO_0000386081. 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}. FT MUTAGEN 192 193 TT->AA: Loss of GTP-binding, binds GDP FT normally. {ECO:0000269|PubMed:26122105}. SQ SEQUENCE 384 AA; 41998 MW; 2779AC222A662EEA CRC64; MKFIDEAKIE VAAGKGGNGA TSFRREKFVP RGGPDGGDGG KGGSVWAEAD ENTNTLVEYR FVKRYQAKNG EKGHGSDRYG AGADDIVLKM PVGTLIRDLD TDEIVADLTY HGQRVCLAKG GKGGLGNIHF KSSVNRAPKQ STPGEEGETR SLQLELKVLA DVGLLGMPNA GKSTLITAVS AARPKIANYP FTTLHPNLGV VRIDENHSFV MADIPGLIEG AAEGAGLGHR FLKHLSRTGL LLHVVDLAPF DETVNPAEEA LAIINELRKY DEELYGKPRW LVLNKLDMLD EEEARARTAA FLEAVGWDYP EPDDRFQFDM ETPRLFQISA LTHQGTQELV HQINQYLAEK KRIEAEKAEA EKAAANVEII EQQPKTDTGV FKPE // ID NUOH_NEIG1 Reviewed; 358 AA. AC Q5F622; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1744; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90365.1; -; Genomic_DNA. DR RefSeq; WP_003691926.1; NC_002946.2. DR RefSeq; YP_208777.1; NC_002946.2. DR EnsemblBacteria; AAW90365; AAW90365; NGO_1744. DR GeneID; 3281416; -. DR KEGG; ngo:NGO1744; -. DR PATRIC; 20337086; VBINeiGon24812_2083. DR HOGENOM; HOG000228276; -. DR KO; K00337; -. DR OMA; LDLGWKF; -. DR OrthoDB; EOG6B62B4; -. DR BioCyc; NGON242231:GI2G-1640-MONOMER; -. DR Proteomes; UP000000535; 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_0000240086. 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; 39835 MW; 2D777A59B1CF5F5E CRC64; MQEWFQNLFA ATLGLGDLGI TVGLVVSVIV KIVIILIPLI LTVAYLTYFE RKVIGFMQLR VGPNVTGPRG LIQPFADVFK LLFKEVTRPK LSNKALFYIG PIMSLAPSFA AWAVIPFNEE WVLTNINIGL LYILMITSLS VYGVIIAGWA SNSKYSFLGA MRASAQSISY EIAMSAALVC VVMVSGSMNF SDIVAAQAKG IAGGSVFSWN WLPLFPIFIV YLISAVAETN RAPFDVAEGE SEIVAGHHVE YSGFAFALFF LAEYIFMILI AALTSLMFLG GWLSPFPQSW GIVGTPSAFW MFVKMAAVLY WYLWIRATFP RYRYDQIMRL GWKVLIPIGF AYIVVLGVWM ISPLNLWK // ID NUOK_NEIG1 Reviewed; 101 AA. AC Q5F625; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. 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=NGO1741; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90362.1; -; Genomic_DNA. DR RefSeq; WP_002215628.1; NC_002946.2. DR RefSeq; YP_208774.1; NC_002946.2. DR EnsemblBacteria; AAW90362; AAW90362; NGO_1741. DR GeneID; 3281171; -. DR KEGG; ngo:NGO1741; -. DR PATRIC; 20337080; VBINeiGon24812_2080. DR HOGENOM; HOG000066429; -. DR KO; K00340; -. DR OMA; NFVAFSY; -. DR OrthoDB; EOG6MSS3R; -. DR BioCyc; NGON242231:GI2G-1637-MONOMER; -. DR Proteomes; UP000000535; 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_0000390139. 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 PANC_NEIG1 Reviewed; 278 AA. AC Q5F9F8; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO0437; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89179.1; -; Genomic_DNA. DR RefSeq; WP_003687896.1; NC_002946.2. DR RefSeq; YP_207591.1; NC_002946.2. DR ProteinModelPortal; Q5F9F8; -. DR SMR; Q5F9F8; 1-277. DR EnsemblBacteria; AAW89179; AAW89179; NGO_0437. DR GeneID; 3282128; -. DR KEGG; ngo:NGO0437; -. DR PATRIC; 20333893; VBINeiGon24812_0523. DR HOGENOM; HOG000175517; -. DR KO; K01918; -. DR OMA; QKDAQQF; -. DR OrthoDB; EOG6Z6FZ4; -. DR BioCyc; NGON242231:GI2G-415-MONOMER; -. DR UniPathway; UPA00028; UER00005. DR Proteomes; UP000000535; 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_0000128246. 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; 31000 MW; 991E4581702C699C CRC64; MQIIHTIREL RTWRENIGKV AFVPTMGNLH EGHLALVREA RKRADNVVVS IFVNRLQFGQ GEDFDKYPRT LQQDADKLAA EGVAVVFAPD EKELYPNVEQ RYNVEPPHLQ NELCGKFRPG HFRGVATVVS KLFNIVLPDV ACFGKKDYQQ LAVIKGLTED LNFDIEIVPV DTGRAADGLA LSSRNRYLSV GERAEAPRLY RELQAVAESL KQAGLDYAGL ERQAADHLTA AGWLVDYVEI RRADTLEMAR AGDKKLVVLA AARLGTTRLI DNVEVGLP // ID ORN_NEIG1 Reviewed; 187 AA. AC Q5FAH8; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO0042; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88809.1; -; Genomic_DNA. DR RefSeq; WP_003687260.1; NC_002946.2. DR RefSeq; YP_207221.1; NC_002946.2. DR ProteinModelPortal; Q5FAH8; -. DR SMR; Q5FAH8; 5-177. DR EnsemblBacteria; AAW88809; AAW88809; NGO_0042. DR GeneID; 3282379; -. DR KEGG; ngo:NGO0042; -. DR PATRIC; 20332922; VBINeiGon24812_0046. DR HOGENOM; HOG000246596; -. DR KO; K13288; -. DR OMA; AFFHYRN; -. DR OrthoDB; EOG6Z9B51; -. DR BioCyc; NGON242231:GI2G-37-MONOMER; -. DR Proteomes; UP000000535; 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_0000111052. 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; 21775 MW; 15E982D9971BF265 CRC64; MQDKNNLCWL DMEMTGLNPE TDRIIEVAMI ITDSDLNVLA QSEVYAIHQS DDLLDNMDEW NTATHGRTGL TQRVRESSHT EAEVEQKLLD FMSEWIPGRA TPMCGNSIHQ DRRFMVKYMP KLENYFHYRN LDVSTLKELA KRWNPPIAKS VVKRGSHKAL DDILESIEEM RHYREHFLIS APKAEAQ // ID OTC_NEIG1 Reviewed; 331 AA. AC Q5F7E6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109}; DE Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109}; DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109}; GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; GN OrderedLocusNames=NGO1232; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP-Rule:MF_01109}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 1/3. CC {ECO:0000255|HAMAP-Rule:MF_01109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. CC {ECO:0000255|HAMAP-Rule:MF_01109}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89891.1; -; Genomic_DNA. DR RefSeq; WP_003689682.1; NC_002946.2. DR RefSeq; YP_208303.1; NC_002946.2. DR ProteinModelPortal; Q5F7E6; -. DR SMR; Q5F7E6; 2-331. DR EnsemblBacteria; AAW89891; AAW89891; NGO_1232. DR GeneID; 3282465; -. DR KEGG; ngo:NGO1232; -. DR PATRIC; 20335781; VBINeiGon24812_1449. DR HOGENOM; HOG000022686; -. DR KO; K00611; -. DR OMA; DFRIFAP; -. DR OrthoDB; EOG690MGV; -. DR BioCyc; NGON242231:GI2G-1143-MONOMER; -. DR UniPathway; UPA00068; UER00112. DR Proteomes; UP000000535; 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_1000065106. FT REGION 55 59 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT REGION 133 136 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT REGION 234 235 Ornithine binding. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT REGION 271 274 Carbamoyl phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT BINDING 9 9 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 71 71 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 82 82 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 106 106 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 166 166 Ornithine. {ECO:0000250}. FT BINDING 230 230 Ornithine. {ECO:0000250}. FT BINDING 299 299 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT BINDING 317 317 Carbamoyl phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01109}. FT SITE 30 30 Important for structural integrity. FT {ECO:0000255|HAMAP-Rule:MF_01109}. FT SITE 146 146 Important for structural integrity. FT {ECO:0000255|HAMAP-Rule:MF_01109}. SQ SEQUENCE 331 AA; 36677 MW; 2E7C0EA0FD9DD962 CRC64; MNLKNRHFLK LLDFTPEEIT TYLDLAAELK DAKKAGREIQ RMKGKNIALI FEKTSTRTRC AFEVAARDQG ADATYLEPSA SQIGHKESIK DTARVLGRMY DAIEYRGFAQ ETVEELAKYA GVPVFNGLTN EFHPTQMLAD ALTMREHSGK PLNQTAFAYV GDARYNMGNS LLILGAKLGM DVRIGAPQSL WPSEGIIAAA HAAAKETGAK ITLTENAHEA VKGVGFIHTD VWVSMGEPKE VWQERIDLLK DYRVTPELMA ASGNPQVKFM HCLPAFHNRE TKVGEWIYET FGLNGVEVTE EVFESPAGIV FDQAENRMHT IKAVMVAALG D // ID PDXH_NEIG1 Reviewed; 210 AA. AC Q5F8V2; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 76. 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=NGO0658; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89385.1; -; Genomic_DNA. DR RefSeq; WP_003688841.1; NC_002946.2. DR RefSeq; YP_207797.1; NC_002946.2. DR ProteinModelPortal; Q5F8V2; -. DR EnsemblBacteria; AAW89385; AAW89385; NGO_0658. DR GeneID; 3282467; -. DR KEGG; ngo:NGO0658; -. DR PATRIC; 20334410; VBINeiGon24812_0777. DR HOGENOM; HOG000242755; -. DR KO; K00275; -. DR OMA; PEHWGGY; -. DR OrthoDB; EOG60KN2Z; -. DR BioCyc; NGON242231:GI2G-625-MONOMER; -. DR UniPathway; UPA01068; UER00304. DR UniPathway; UPA01068; UER00305. DR Proteomes; UP000000535; 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_0000167725. 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; 24177 MW; FF9C40DA2A1B5BB9 CRC64; MDLHNIREDY SKRELSEADC ADNPIEQFER WLDEAVRAEV NEPTAVNVAA VDGRGRPNSR MVLLKEVNSE GFVFFTNYHS RKGRSLELNP FAAMTFFWPE LERQVRVEGR VGRLAEKLSD EYFESRPYQS RLGAWASAQS EVIPNKAVLV AKAAAVGLKH PLHVPRPPHW GGYIVIPDLI EFWQGRPSRL HDRIQYRLLD GGWIRERLSP // ID PANB_NEIG1 Reviewed; 263 AA. AC Q5F9F9; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO0436; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_00156}. 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; AE004969; AAW89178.1; -; Genomic_DNA. DR RefSeq; WP_003687894.1; NC_002946.2. DR RefSeq; YP_207590.1; NC_002946.2. DR ProteinModelPortal; Q5F9F9; -. DR SMR; Q5F9F9; 1-261. DR EnsemblBacteria; AAW89178; AAW89178; NGO_0436. DR GeneID; 3282104; -. DR KEGG; ngo:NGO0436; -. DR PATRIC; 20333889; VBINeiGon24812_0521. DR HOGENOM; HOG000078427; -. DR KO; K00606; -. DR OMA; MAAGAQM; -. DR OrthoDB; EOG63C0WN; -. DR BioCyc; NGON242231:GI2G-414-MONOMER; -. DR UniPathway; UPA00028; UER00003. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW 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_0000297305. FT REGION 43 44 Alpha-ketoisovalerate binding. FT {ECO:0000255|HAMAP-Rule:MF_00156}. 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 {ECO:0000255|HAMAP-Rule:MF_00156}. FT BINDING 111 111 Alpha-ketoisovalerate. FT {ECO:0000255|HAMAP-Rule:MF_00156}. SQ SEQUENCE 263 AA; 27724 MW; C214D9634B416E0A CRC64; MITVNTLQKM KAAGEKIVML TAYESSFAAL MDDAGVDVLL VGDSLGMAVQ GRQSTLPVSL RDMCYHTECV ARGAKNAMIV SDLPFGAYQQ SKEQAFAAAA ELMAAGAHMV KLEGGVWMAE TTEFLQMRGI PVCAHIGLTP QSVFAFGGYK VQGRGGKAQA LLNDAKAHDE AGAAVVLMEC VPAELAKKVT ETVSCPTIGI GAGADCDGQV LVMHDMLGIF PGKTAKFVKN FMRGQSSIQA AVRAYVAEVK AKTFPAAEHI FAD // ID PAND_NEIG1 Reviewed; 127 AA. AC Q5F8Y9; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO0620; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89348.1; -; Genomic_DNA. DR RefSeq; WP_003688909.1; NC_002946.2. DR RefSeq; YP_207760.1; NC_002946.2. DR ProteinModelPortal; Q5F8Y9; -. DR SMR; Q5F8Y9; 26-117. DR EnsemblBacteria; AAW89348; AAW89348; NGO_0620. DR GeneID; 3282899; -. DR KEGG; ngo:NGO0620; -. DR PATRIC; 20334324; VBINeiGon24812_0734. DR HOGENOM; HOG000221007; -. DR KO; K01579; -. DR OMA; LYSKIHR; -. DR OrthoDB; EOG6P5ZMC; -. DR BioCyc; NGON242231:GI2G-588-MONOMER; -. DR UniPathway; UPA00028; UER00002. DR Proteomes; UP000000535; 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_0000023123. FT CHAIN 25 127 Aspartate 1-decarboxylase alpha chain. FT {ECO:0000255|HAMAP-Rule:MF_00446}. FT /FTId=PRO_0000023124. 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; 13745 MW; E4445E525854AAE3 CRC64; MFRTILGGKI HRATVTEADL NYVGSITVDQ DLLDAAGICP NEKVAIVNNN NGERFETYTI AGKRGSGVIC LNGAAARLVQ KGDIVIIMSY IQLSEPEIAA HEPKVVLVDG NNKIRDIISY EPPHTVL // ID PBPA_NEIG1 Reviewed; 798 AA. AC Q5FAC7; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 82. 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; OrderedLocusNames=NGO0099; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9098083; RA Ropp P.A., Nicholas R.A.; RT "Cloning and characterization of the ponA gene encoding penicillin- RT binding protein 1 from Neisseria gonorrhoeae and Neisseria RT meningitidis."; RL J. Bacteriol. 179:2783-2787(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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). Essential for cell wall synthesis. CC {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; AE004969; AAW88860.1; -; Genomic_DNA. DR RefSeq; WP_003687357.1; NC_002946.2. DR RefSeq; YP_207272.1; NC_002946.2. DR ProteinModelPortal; Q5FAC7; -. DR SMR; Q5FAC7; 63-248. DR EnsemblBacteria; AAW88860; AAW88860; NGO_0099. DR GeneID; 3282452; -. DR KEGG; ngo:NGO0099; -. DR PATRIC; 20333095; VBINeiGon24812_0131. DR HOGENOM; HOG000041138; -. DR KO; K05366; -. DR OMA; ANSGVYI; -. DR OrthoDB; EOG6HMXCD; -. DR BioCyc; NGON242231:GI2G-89-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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 INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 798 Penicillin-binding protein 1A. FT /FTId=PRO_0000083168. FT TOPO_DOM 2 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; 88495 MW; FBA4BA9D5CB0995A CRC64; MIKKILTTCF GLFFGFCVFG 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 RRELYEKYGE DAYTQGFKVY TTVRTDHQKA ATEALRKALR NFDRGSSYRG AENYIDLSKS EDVEETVSQY LSGLYTVDKM VPAVVLDVTK KKNVVIQLPG GRRVALDRRA LGFAARAVDN EKMGEDRIRR GAVIRVKNNG GRWAVVQEPL LQGALVSLDA KTGAVRALVG GYDFHSKTFN RAVQAMRQPG STFKPFVYSA ALSKGMTAST VVNDAPISLP GKGPNGSVWT PKNSDGRYSG YITLRQALTA SKNMVSIRIL MSIGVGYAQQ YIRRFGFRPS ELPASLSMAL GTGETTPLKV AEAYSVFANG GYRVSSHVID KIYDRDGRLR AQMQPLVAGQ NAPQAIDPRN AYIMYKIMQD VVRVGTARGA AALGRTDIAG KTGTTNDNKD AWFVGFNPDV VTAVYIGFDK PKSMGRAGYG GTIAVPVWVD YMRFALKGKQ GKGMKMPEGV VSSNGEYYMK ERMVTDPGLM LDNSGIAPQP SRRAKEDDEA AVENEQQGRS DETRQDVQET PVLPSNTDSK QQQLDSLF // ID PGK_NEIG1 Reviewed; 397 AA. AC Q5F5K5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145}; DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145}; GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=NGO1919; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. {ECO:0000255|HAMAP-Rule:MF_00145}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_00145}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00145}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90532.1; -; Genomic_DNA. DR RefSeq; WP_003699253.1; NC_002946.2. DR RefSeq; YP_208944.1; NC_002946.2. DR ProteinModelPortal; Q5F5K5; -. DR SMR; Q5F5K5; 3-391. DR EnsemblBacteria; AAW90532; AAW90532; NGO_1919. DR GeneID; 3282854; -. DR KEGG; ngo:NGO1919; -. DR PATRIC; 20337574; VBINeiGon24812_2314. DR HOGENOM; HOG000227107; -. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR OrthoDB; EOG64N9Z0; -. DR BioCyc; NGON242231:GI2G-1822-MONOMER; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000535; 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 1 397 Phosphoglycerate kinase. FT /FTId=PRO_1000058018. FT NP_BIND 346 349 ATP. {ECO:0000255|HAMAP-Rule:MF_00145}. FT REGION 21 23 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00145}. FT REGION 59 62 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00145}. FT BINDING 36 36 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00145}. FT BINDING 114 114 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00145}. FT BINDING 147 147 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00145}. FT BINDING 198 198 ATP. {ECO:0000255|HAMAP-Rule:MF_00145}. FT BINDING 320 320 ATP. {ECO:0000255|HAMAP-Rule:MF_00145}. SQ SEQUENCE 397 AA; 41182 MW; E52F667D13EBD38A CRC64; MAFLKLTEQN VRGKTVLIRA DMNVPFKGGK ISDDTRIRAS LASVKYCLDN GASVIVMTHL GRPTEGEFHP EDDVAPVAAH LGGLLGKDVK VLNDWRENKP ALNAGDVVML QNVRINKGEK KNDLELGKAY AALCDVFVND AFGTAHRAQA STEAVAQAAP VACAGVLMAG ELDALGKALK QPARPMVAIV AGSKVSTKLT ILESLADKVD QLIVGGGIAN TFLLAEGKAI GKSLAEHDLV EESKKIMAKM AAKGGSVPLP TDVVVAKAFA ADAEAVVKDI ADVAEDEMIL DIGPKSAAAL ADLLKAAGTV VWNGPVGVFE FDQFAGGTKA LAEAIAQSKA FSIAGGGDTL AAIAKFGVTE QIGYISTGGG AFLEFLEGKE LPAVAALEKT RRVNGLI // ID PDXJ_NEIG1 Reviewed; 242 AA. AC Q5F6P1; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1508; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90146.1; -; Genomic_DNA. DR RefSeq; WP_003695556.1; NC_002946.2. DR RefSeq; YP_208558.1; NC_002946.2. DR ProteinModelPortal; Q5F6P1; -. DR SMR; Q5F6P1; 1-239. DR EnsemblBacteria; AAW90146; AAW90146; NGO_1508. DR GeneID; 3281573; -. DR KEGG; ngo:NGO1508; -. DR PATRIC; 20336490; VBINeiGon24812_1793. DR HOGENOM; HOG000258094; -. DR KO; K03474; -. DR OMA; ERHIRYQ; -. DR OrthoDB; EOG6M9F0H; -. DR BioCyc; NGON242231:GI2G-1412-MONOMER; -. DR UniPathway; UPA00244; UER00313. DR Proteomes; UP000000535; 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_0000231818. 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; C4A33C3C07A16B6C CRC64; MLLGVNIDHI ATVRNARGTT YPSPVEAALV AETHGADLIT MHLREDRRHI KDADVFAVKN AIRTRLNLEM ALTEEMLENA LKVMPEDVCI VPEKRQEITT EGGLDVLAQQ EKIAEFAKIL TDAGIRVSLF IDADDRQIQA ARDVGAPVVE LHTGAYADAQ SHAEQIRQFE RIQNGAHFAG DLGLVVNAGH GLTIHNVTPV AQILAIRELN IGHSLIAQAL FLGLPEAVRQ MKEAMFRARL LP // ID PILQ_NEIG1 Reviewed; 723 AA. AC Q5FAD2; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Type IV pilus biogenesis and competence protein PilQ; DE AltName: Full=Outer membrane protein Omc; DE Flags: Precursor; GN Name=pilQ; Synonyms=omc; OrderedLocusNames=NGO0094; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=14729699; DOI=10.1128/JB.186.3.730-739.2004; RA Chen C.-J., Tobiason D.M., Thomas C.E., Shafer W.M., Seifert H.S., RA Sparling P.F.; RT "A mutant form of the Neisseria gonorrhoeae pilus secretin protein RT PilQ allows increased entry of heme and antimicrobial compounds."; RL J. Bacteriol. 186:730-739(2004). 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. {ECO:0000269|PubMed:14729699}. CC -!- SUBUNIT: Homododecamer. Tetramer of trimer (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane. Note=Associated to the CC membrane through its C-terminus. CC -!- DISRUPTION PHENOTYPE: Cells show decreased piliation and CC transformation efficiency. It uses hemoglobin as a heme and iron CC source in the absence of a hemoglobin receptor and it has elevated CC sensitivities to various antimicrobial compounds. CC {ECO:0000269|PubMed:14729699}. 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; AE004969; AAW88855.1; -; Genomic_DNA. DR RefSeq; WP_003698035.1; NC_002946.2. DR RefSeq; YP_207267.1; NC_002946.2. DR EnsemblBacteria; AAW88855; AAW88855; NGO_0094. DR GeneID; 3282403; -. DR KEGG; ngo:NGO0094; -. DR PATRIC; 20333085; VBINeiGon24812_0126. DR HOGENOM; HOG000255072; -. DR KO; K02666; -. DR OMA; FAINTKH; -. DR OrthoDB; EOG6423BN; -. DR BioCyc; NGON242231:GI2G-84-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell outer membrane; Competence; Complete proteome; Membrane; KW Protein transport; Reference proteome; Signal; Transport. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 723 Type IV pilus biogenesis and competence FT protein PilQ. FT /FTId=PRO_0000013114. SQ SEQUENCE 723 AA; 77951 MW; EDE9A3D62101EBBE CRC64; MNTKLTKIIS GLFVATAAFQ TASAGNITDI KVSSLPNKQK IVKVSFDKEI VNPTGFVTSS PARIALDFEQ TGISMDQQVL EYADPLLSKI SAAQNSSRAR LVLNLNKPGQ YNTEVRGNKV WIFINESDDT VSAPARPAVK AAPAAPAKQQ AAAPFTESVV SVSAPFSPAK QQAAASAKQT NIDFRKDGKN AGIIELAALG FAGQPDISQQ HDHIIVTLKN HTLPTALQRS LDVADFKTPV QKVTLKRLNN DTQLIITTTG NWELVNKSAA PGYFTFQVLP KKQNLESGGV NNAPKTFTGR KISLDFQDVE IRTILQILAK ESGMNIVASD SVSGKMTLSL KDVPWDQALD LVMQARNLDM RQQGNIVNIA PRDELLAKDK AFLQAEKDIA DLGALYSQNF QLKYKNVEEF RSILRLDNAD TTGNRNTLVS GRGSVLIDPA TNTLIVTDTR SVIEKFRKLI DELDVPAQQV MIEARIVEAA DGFSRDLGVK FGATGRKKLK NETSAFGWGV NSGFGGGDKW EAQTKINLPV AAAANSISLV RAISSGALNL ELSASESLSK TKTLANPRVL TQNRKEAKIE SGYEIPFTVT TASGGGNSTN TELKKAVLGL TVTPNITPDG QIIMTVKINK DSPAQCASGN NTILCISTKS LNTQAMVENG GTLIVGGIYE ENNGNTLTKV PLLGDIPVIG NLFKTRGKKT DRRELLIFIT PRIIDTAGNS LRY // ID PHEA_NEIG1 Reviewed; 362 AA. AC Q9ZHY3; Q5F6N9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 16-MAR-2016, entry version 109. DE RecName: Full=P-protein; DE Includes: DE RecName: Full=Chorismate mutase; DE Short=CM; DE EC=5.4.99.5; DE Includes: DE RecName: Full=Prephenate dehydratase; DE Short=PDT; DE EC=4.2.1.51; GN Name=pheA; OrderedLocusNames=NGO1510; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10094619; DOI=10.1046/j.1365-2958.1998.01089.x; RA Mehr I.J., Seifert H.S.; RT "Differential roles of homologous recombination pathways in Neisseria RT gonorrhoeae pilin antigenic variation, DNA transformation and DNA RT repair."; RL Mol. Microbiol. 30:697-710(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Chorismate = prephenate. CC -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2). CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; CC phenylpyruvate from prephenate: step 1/1. CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate CC biosynthesis; prephenate from chorismate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC -!- SIMILARITY: Contains 1 chorismate mutase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00515}. CC -!- SIMILARITY: Contains 1 prephenate dehydratase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00517}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD05425.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAW90148.1; 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; AF047375; AAD05425.1; ALT_INIT; Genomic_DNA. DR EMBL; AE004969; AAW90148.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003689394.1; NC_002946.2. DR ProteinModelPortal; Q9ZHY3; -. DR PRIDE; Q9ZHY3; -. DR EnsemblBacteria; AAW90148; AAW90148; NGO_1510. DR PATRIC; 20336494; VBINeiGon24812_1795. DR HOGENOM; HOG000018971; -. DR OrthoDB; EOG6WHNT1; -. DR BioCyc; NGON242231:GI2G-1414-MONOMER; -. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:UniProtKB-EC. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. 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 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Isomerase; Lyase; KW Multifunctional enzyme; Phenylalanine biosynthesis; KW Reference proteome. FT CHAIN 1 362 P-protein. FT /FTId=PRO_0000119189. FT DOMAIN 3 91 Chorismate mutase. {ECO:0000255|PROSITE- FT ProRule:PRU00515}. FT DOMAIN 92 269 Prephenate dehydratase. FT {ECO:0000255|PROSITE-ProRule:PRU00517}. FT DOMAIN 281 356 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT REGION 270 362 Regulatory (Phe-binding). FT SITE 262 262 Essential for prephenate dehydratase FT activity. {ECO:0000255}. SQ SEQUENCE 362 AA; 39354 MW; BEC6582338E84DE2 CRC64; MSQTIDELLI PHRNAIDTID AEILRLLNER AQHAHAIGEL KGTGAVYRPE REVAVLRRIQ DLNKGPLPDE SVARLFREVM SECLAVERPL TIAYLGPQGT FTQQAAIKHF GHAAHTMACP TIDDCFKQVE TRQADYLVAP VENSTEGSVG RTLDLLAVTA LQACGEVVLR IHHNLLRKNN GSTEGIAKVF SHAQALAQCN DWLGRRLPNA ERIAVSSNAE AARLVAESDD GTVAAIAGRT AAEIYGLDMV AECIEDEPNN TTRFLVMGHH ETGASGSDKT SLAVSAPNRA GAVASLLQPL TESGISMTKF ESRPSKSVLW EYLFFIDIEG HRRDAQIQTA LERLGERASF VKAIGSYPTA VL // ID PLSY_NEIG1 Reviewed; 200 AA. AC Q5F8C7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. 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=NGO0858; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89560.1; -; Genomic_DNA. DR RefSeq; WP_003691121.1; NC_002946.2. DR RefSeq; YP_207972.1; NC_002946.2. DR EnsemblBacteria; AAW89560; AAW89560; NGO_0858. DR GeneID; 3282318; -. DR KEGG; ngo:NGO0858; -. DR PATRIC; 20334884; VBINeiGon24812_1012. DR HOGENOM; HOG000283806; -. DR KO; K08591; -. DR OMA; HIWPVWL; -. DR OrthoDB; EOG6M6JSX; -. DR BioCyc; NGON242231:GI2G-802-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000535; 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_0000188409. 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 158 178 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01043}. SQ SEQUENCE 200 AA; 20752 MW; 4615D9FE92D1E426 CRC64; MFNIPAVAVS YLIGSLSFAV IVSKYYGMDD PRTYGSGNPG ATNVLRSGKK KAAALTLLGD AAKGLVAVLL ARVLQEPLGL SDSAIAAVAL AALVGHMWPV FFGFKGGKGV ATALGVLLAL SPATALVCAL IWLVMAFGFK VSSLAALVAT TAAPLAALFF MPHTSWIFAT LAIAILVLLR HKSNILNLIK GKESKIGEKR // ID PNP_NEIG1 Reviewed; 707 AA. AC Q5F9Q7; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO0335; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW89080.1; -; Genomic_DNA. DR RefSeq; WP_003690787.1; NC_002946.2. DR RefSeq; YP_207492.1; NC_002946.2. DR ProteinModelPortal; Q5F9Q7; -. DR SMR; Q5F9Q7; 618-693. DR EnsemblBacteria; AAW89080; AAW89080; NGO_0335. DR GeneID; 3283038; -. DR KEGG; ngo:NGO0335; -. DR PATRIC; 20333661; VBINeiGon24812_0408. DR HOGENOM; HOG000218327; -. DR KO; K00962; -. DR OMA; RFMFHYN; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NGON242231:GI2G-315-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transferase. FT CHAIN 1 707 Polyribonucleotide FT nucleotidyltransferase. FT /FTId=PRO_0000329729. 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; 76455 MW; F85D2089CEBE9E3D CRC64; MMFNKYVKTF QYGNQTVTLE TGEIARQAAA AVKVSMGDTV VFVAVTTNKE VKEGQDFFPL AVDYLERTYA AGKIPGGFFK REGKQSEKEI LTSRLIDRPI RPLFPEGFYH DIQIVAMVVS VDPEIDSDIP AMLGASAALV LSGVPFAGPI GAARVGYING VYVLNPTKAE LAKSQLDLVV AGTSKAVLMV ESEAKILPED VMLGAVVYGH DQMQVAINAI NEFADEVNPE VWDWKAPETN EELVAKVRGI AGETIKEAFK IRQKQARSAK LDEAWNAVKE ALITEETDTL AANEIKGIFK RLEADVVRSQ ILDGQPRIDG RDTRTVRPLN IQTGVLPRTH GSALFTRGET QALAVATLGT SRDEQIIDAL SGEYTDRFML HYNFPPYSTG EVGRMGAPKR REIGHGRLAK RALLAVLPKP EDFSYTMRVV SEITESNGSS SMASVCGGCL SLLSAGVPLK AHVAGIAMGL ILEGNKFAVL TDILGDEDHL GDMDFKVAGT TEGVTALQMD IKIQGITKEI MQIALAQAKE ARLHILDQMK AAVAGPQELS AHAPRLFTMK ISQDKIRDVI GKGGETIRSI TAETGTEINI AEDGTITIAA TTQEAGDAAK KRIEEITAEV EVGKVYEGTV VKILDNNVGA IVSVMPGKDG LVHISQIAHE RVRNVGDYLQ VGQVVNVKAL EVDDRGRVRL SIKALLDAPV REENAAE // ID PLSX_NEIG1 Reviewed; 348 AA. AC Q5F4X3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO2171; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90764.1; -; Genomic_DNA. DR RefSeq; WP_010951419.1; NC_002946.2. DR RefSeq; YP_209176.1; NC_002946.2. DR ProteinModelPortal; Q5F4X3; -. DR EnsemblBacteria; AAW90764; AAW90764; NGO_2171. DR GeneID; 3282754; -. DR KEGG; ngo:NGO2171; -. DR PATRIC; 20338204; VBINeiGon24812_2624. DR HOGENOM; HOG000154730; -. DR KO; K03621; -. DR OMA; KFCLRTM; -. DR OrthoDB; EOG68H88P; -. DR BioCyc; NGON242231:GI2G-2058-MONOMER; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000000535; 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 1 348 Phosphate acyltransferase. FT /FTId=PRO_1000001790. SQ SEQUENCE 348 AA; 36797 MW; 79B4E07B2112212B CRC64; MITLAVESMG GDQGLAVTVP GATAFLQAHP DVRLIMTGDE TQLRQALNAA GAPMERIDIC HTTQVVGMDE SPQSALKNKK YSSMRVAINQ VKEGKAQAAV SAGNTGALMA TARFVLKTIP GIERPAIAKF LPSDTDHVTL ALDLGANVDC TPEQLAQFAV IGSELVHALH PQKGQPRVGL VNVGTEDIKG TDTVKQTYKL LQNSKLNFIG NIESNGILYG EADVVVADGF VGNVMLKTIE GAVKFMSGAI RREFQSNLFN KLAAVAALPA LKGLKNKLDP RKFNGAILLG LRGIVIKSHG GTDKTGFRYA LEEAYHEAKS AGLSKIEQGV AEQLAALEAA QNETAASL // ID PRMB_NEIG1 Reviewed; 303 AA. AC Q5F783; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1300; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89954.1; -; Genomic_DNA. DR RefSeq; WP_003691605.1; NC_002946.2. DR RefSeq; YP_208366.1; NC_002946.2. DR ProteinModelPortal; Q5F783; -. DR EnsemblBacteria; AAW89954; AAW89954; NGO_1300. DR GeneID; 3281814; -. DR KEGG; ngo:NGO1300; -. DR PATRIC; 20335947; VBINeiGon24812_1528. DR HOGENOM; HOG000076275; -. DR KO; K07320; -. DR OMA; VLVCEVG; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; NGON242231:GI2G-1212-MONOMER; -. DR Proteomes; UP000000535; 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_0000414180. SQ SEQUENCE 303 AA; 33827 MW; FB141734F9C03F17 CRC64; MVHIMFNQAA QELTTIRDVL RFAVSRFNEA GLFFGHGTDN AHDEAVYLIL HTLNLPLDML APYLDAKLLE AEKEEVLAVI ERRAVEHIPA AYLTHQAWQG EFDFYVDERV IVPRSFIYEL LGDGLRPWIE YDELVHNALD LCTGSGCLAI QMAHHYPDAQ IDAVDVSLDA LEVAGINIED YGLEERIQLI HTDLFEGLEG TYDLIVSNPP YVDAESVGAL PEEYLHEPEL ALGSGADGLD ATRQILLNAA KFLNPKGVLL VEIGHNRDVL EAAYPELPFT WLETSGGDGF VFLLTREQLL GEE // ID PRMC_NEIG1 Reviewed; 285 AA. AC Q5F5B4; DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000255|HAMAP-Rule:MF_02126}; DE Short=RF MTase {ECO:0000255|HAMAP-Rule:MF_02126}; DE EC=2.1.1.297 {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000255|HAMAP-Rule:MF_02126}; GN Name=prmC {ECO:0000255|HAMAP-Rule:MF_02126}; GN OrderedLocusNames=NGO2015; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000255|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:0000255|HAMAP-Rule:MF_02126}. CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase CC family. PrmC subfamily. {ECO:0000255|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; AE004969; AAW90623.1; -; Genomic_DNA. DR RefSeq; WP_010951382.1; NC_002946.2. DR RefSeq; YP_209035.1; NC_002946.2. DR ProteinModelPortal; Q5F5B4; -. DR EnsemblBacteria; AAW90623; AAW90623; NGO_2015. DR GeneID; 3282697; -. DR KEGG; ngo:NGO2015; -. DR PATRIC; 20337813; VBINeiGon24812_2430. DR HOGENOM; HOG000076274; -. DR KO; K02493; -. DR OMA; HGWTQGE; -. DR OrthoDB; EOG68Q0SZ; -. DR BioCyc; NGON242231:GI2G-1916-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 285 Release factor glutamine FT methyltransferase. FT /FTId=PRO_0000414534. FT REGION 121 125 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT REGION 188 191 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_02126}. FT BINDING 144 144 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT BINDING 171 171 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. FT BINDING 188 188 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_02126}. SQ SEQUENCE 285 AA; 31835 MW; 27C7BE43C13EAEEA CRC64; MFKPHRRQTG RKMTFDEWLG LSKLPKIEAR MLLQYVSEYT RVQLLTRGGE EMPDEIRQRA DRLAQRRLNG EPVAYILGVR EFYGRRFTVN PNVLIPRPET EHLVEAVLAR LPENGRVWDL GTGSGAVAVT VALERPDAFV RASDISTPAL ETARKNAADL GARVEFAHGS WFDTDMPSER QWDIIVSNPP YIENGDKHLS QGDLRFEPQI ALTDFSDGLS CIRTLAQGAP DRLAEGGFLL LEHGFDQGAA VRGVLAENGF SGVEILPDLA GLDRVTLGKY MKHLK // ID PNCB_NEIG1 Reviewed; 402 AA. AC Q5F836; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 16-MAR-2016, entry version 81. 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=NGO0962; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89651.1; 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; AE004969; AAW89651.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F836; -. DR EnsemblBacteria; AAW89651; AAW89651; NGO_0962. DR PATRIC; 20335114; VBINeiGon24812_1126. DR HOGENOM; HOG000284928; -. DR OrthoDB; EOG6X10XB; -. DR BioCyc; NGON242231:GI2G-893-MONOMER; -. DR UniPathway; UPA00253; UER00457. DR Proteomes; UP000000535; 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_0000205832. SQ SEQUENCE 402 AA; 46265 MW; 87785B369B2D9AA0 CRC64; MTGIIHSLLD TDLYKFTMLQ VVLHQFPQTH SLYEFRCRNV STVYPLADIR EDLEAELDAL CRLRFTHDEL GYLRSLRFIK SDFVDYLELF QLQRRFVEVG TDDKGRLNIR IEGPMIQAMF FEIFILAIVN ELYFRRLETP AVIEEGERRL QAKAARLKEI AAAQNPDEPP FLISDFGTRR RYKLAWQEHV IRTLLEAAPS IVRGTSNVYL AKKLGITPIG TMAHEFLQAF QALDVRLRNF QKAALESWVH EYRGDLGVAL TDVVGMDAFL RDFDLYFAKL FDGLRHDSGD PYVWGDKAYA HYQKLKIDSR TKMLTFSDGL DIERSWALHQ YFKGRFKTGF GIGTNLTNDM GHTPLNIVLK LVECNGQSVA KLSDSPGKTM TNNSTFLAYL RQVFGIPEPR TP // ID PRMA_NEIG1 Reviewed; 295 AA. AC Q5FAH7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO0043; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88810.1; -; Genomic_DNA. DR RefSeq; WP_010950979.1; NC_002946.2. DR RefSeq; YP_207222.1; NC_002946.2. DR ProteinModelPortal; Q5FAH7; -. DR EnsemblBacteria; AAW88810; AAW88810; NGO_0043. DR GeneID; 3282387; -. DR KEGG; ngo:NGO0043; -. DR PATRIC; 20332924; VBINeiGon24812_0047. DR HOGENOM; HOG000007390; -. DR KO; K02687; -. DR OMA; FVHKIEQ; -. DR OrthoDB; EOG6N684G; -. DR BioCyc; NGON242231:GI2G-38-MONOMER; -. DR Proteomes; UP000000535; 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_1000046049. SQ SEQUENCE 295 AA; 31879 MW; 20CFE580BB0128C6 CRC64; MPYQQITVNV NDAVAERLAD ALMEHGALSA AIEDACAGTQ NEQAIFGEPG MPTEQIWQQS KVIALFGEHD EAAAVIDAAA QECGLKDLAY TGETIENQDW VRLTQSQFDP IRISDRLWIT PSWHEAPEGC AVNLRLDPGL AFGTGSHPTT RLCLKWLDTQ LKNGESVLDY GCGSGILTIA ALKLGAGSAV GVDIDEQAVR SGRDNAEQNN VDAQFFLPDS LPQGQFDVVV ANILANPLRM LGEMLAARTK QGGRIVLSGL LDEQAEELGG IYSQWFDLDP AETDEGWARL SGVKR // ID PROA_NEIG1 Reviewed; 420 AA. AC Q5F8D3; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO0850; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89554.1; -; Genomic_DNA. DR RefSeq; WP_003693256.1; NC_002946.2. DR RefSeq; YP_207966.1; NC_002946.2. DR ProteinModelPortal; Q5F8D3; -. DR EnsemblBacteria; AAW89554; AAW89554; NGO_0850. DR GeneID; 3282227; -. DR KEGG; ngo:NGO0850; -. DR PATRIC; 20334870; VBINeiGon24812_1005. DR HOGENOM; HOG000246356; -. DR KO; K00147; -. DR OMA; CNAIETL; -. DR OrthoDB; EOG6FFSCX; -. DR BioCyc; NGON242231:GI2G-796-MONOMER; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000000535; 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_0000189754. SQ SEQUENCE 420 AA; 44919 MW; 014DD6F8B31E7961 CRC64; MSNTQKQLAL AKAAKKSVNT ADAEEKNRAL LAMADSLEAA AEDILAANRL DLKAAAGKIP DSMTDRLLLD GKRICAMADG IRAVAALPDP VGEILETSTL PNGLEIVKKR VAMGVIGIIY ESRPNVTSDA AALALKSGSA VVLRSGKDAF QSARAIVAAL KTGLAQTRID PEAVQLIEDT GREGSYEMMR AKDYLDLLIP RGGAGLIRAV VENAVVPVIE TGTGIVHIYI DKDADWDKAL RIVYNAKTGR PSVCNSMEVL LVHEGIAADF LPKLERLLVR GRIEAGLPPV RFRLDPQAAR YIGGEAAGAD DFDTEFLDYI LAVKTVASVE EAVGHIEARG THHSDGIVTE NRHAADYFTT HIDSAAVYIN ASTRFTDGGE FGLGCEMGIS TQKLHARGPM GLKELTSYKY IVQGTGQVRE // ID PPK_NEIG1 Reviewed; 685 AA. AC Q5FAJ0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0003; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate of ATP to form a long-chain polyphosphate (polyP). CC {ECO:0000255|HAMAP-Rule:MF_00347}. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88776.1; -; Genomic_DNA. DR RefSeq; WP_010950968.1; NC_002946.2. DR RefSeq; YP_207188.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ0; -. DR EnsemblBacteria; AAW88776; AAW88776; NGO_0003. DR GeneID; 3283051; -. DR KEGG; ngo:NGO0003; -. DR PATRIC; 20332834; VBINeiGon24812_0003. DR HOGENOM; HOG000248948; -. DR KO; K00937; -. DR OMA; VRLMQVP; -. DR OrthoDB; EOG65TRRG; -. DR BioCyc; NGON242231:GI2G-3-MONOMER; -. DR Proteomes; UP000000535; 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_1000079369. 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}. SQ SEQUENCE 685 AA; 77258 MW; 78173C96D4554246 CRC64; MTEQNRILCR ELSLLAFNRR VLAQAEDKNV PLLERLRFLC IVSSNLDEFF EVRMAWLKRE NKLHPRRRPD NGKMPSETIA DVTEAARSLI RHQYDLFNNV LQPELARESI HFYRRRNWTG TQKKWIEDYF DRELLPILTP IGLDPSHPFP RPLNKSLNFA VELDGTDAFG RPSGMAIVQA PRILPRVVPL PSELCGGGHG FVFLSSILHA HVGKLFPGMN VKGCHQFRLT RDSDLTVDEE DVQNLRAAIQ NELHDREYGD GVRLEVADTC PAYIRDFLLA QFRLTDAELY QVKGPVNLVR LNAVPDLVNR PDLKFPPHTP GRLKALGKNS PIFDLVRQSP ILLHHPYQSF DPVVDMIREA AADPAVLAVK MTIYRTGTRS ELVPALMKAA LADKQVTVVV ELMARFDEAN NVNWAKQLEE AGAHVVYGVF GYKVHAKMAL VIRREDGVLK RYAHLGTGNY HQGTSRIYTD FGLITADEQI TADVNTLFME ITGLGKPGRL NKLYQSPFTL HKMVIGRIAR ETEHAKAGKP ARITAKMNSL IEPTVIEALY RASAAGVQID LIVRGMCTLR PGVKGLSENI RVRSIVGRQL EHARVYCFHN NGADDTFISS ADWMGRNFFR RIETATPITA PELKKRVIRE GLEMALADNT HAWLMQPDGG YIRAAPAEGE SEADLQNDLW DLLRG // ID PSD_NEIG1 Reviewed; 259 AA. AC Q5F7H2; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 67. 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=NGO1206; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89865.1; -; Genomic_DNA. DR RefSeq; WP_003689647.1; NC_002946.2. DR RefSeq; YP_208277.1; NC_002946.2. DR EnsemblBacteria; AAW89865; AAW89865; NGO_1206. DR GeneID; 3281969; -. DR KEGG; ngo:NGO1206; -. DR PATRIC; 20335713; VBINeiGon24812_1415. DR HOGENOM; HOG000229359; -. DR KO; K01613; -. DR OMA; FNVHSNR; -. DR OrthoDB; EOG6KT2P7; -. DR BioCyc; NGON242231:GI2G-1117-MONOMER; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000000535; 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_0000042279. FT CHAIN 183 259 Phosphatidylserine decarboxylase alpha FT chain. {ECO:0000255|HAMAP-Rule:MF_00664}. FT /FTId=PRO_0000042280. 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 259 AA; 28294 MW; A4D013CF6066A7BE CRC64; MNRLYPHPII AREGWPIIGG GLALSLLVSM CCGWWSLPFW VFTVFALQFF RDPAREIPQN PEAVLSPVDG RIVVVERARD PYRDVDALKI SIFMNVFNVH SQKSPADCTV TKVVYNKGKF VNADLDKAST ENERNAVLAT TASGREITFV QVAGLVARRI LCYTQAGAKL SRGERYGFIR FGSRVDMYLP VDAQAQVAIG DKVTGVKTVL ARLPLTDSQA DPVSQAASVE TAANPSAEQQ QIEAAAAKIQ AAVQDVLKD // ID PSRP_NEIG1 Reviewed; 273 AA. AC Q5FA32; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO0202; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88955.1; -; Genomic_DNA. DR RefSeq; WP_003687512.1; NC_002946.2. DR RefSeq; YP_207367.1; NC_002946.2. DR EnsemblBacteria; AAW88955; AAW88955; NGO_0202. DR GeneID; 3281768; -. DR KEGG; ngo:NGO0202; -. DR PATRIC; 20333337; VBINeiGon24812_0251. DR HOGENOM; HOG000218053; -. DR KO; K09773; -. DR OMA; YAQCEFE; -. DR OrthoDB; EOG6KHG2N; -. DR BioCyc; NGON242231:GI2G-185-MONOMER; -. DR Proteomes; UP000000535; 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_0000196677. FT NP_BIND 154 161 ADP. {ECO:0000255|HAMAP-Rule:MF_01062}. SQ SEQUENCE 273 AA; 30883 MW; DC749B728FE81080 CRC64; MSSPRQVFYI SDRTGLTAEN IGEALLNQFG NLSFKRHTHP FVDTPEKARA VVEKVNRSRQ ENGQRPIAFV SVVDDEIRRI IKGADAFQIN FFETFLGLLE KELNTEATVS GQGHHSIGNT KRYDARMEAV NFSLNHDDGV SDKNLQEADV ILMGVSRSGK TPTCLYLALQ YGIRAANYPL IPDDLESADL PRMVKPYKDK LFGLTIQPER LQAIRQERRP NSAYARIDTC RSEVADAQSM FRRHGIPFAN TTDKSVEELA VHILQACKLK RRF // ID PTH_NEIG1 Reviewed; 192 AA. AC Q5F9L4; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0379; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89123.1; -; Genomic_DNA. DR RefSeq; WP_003687802.1; NC_002946.2. DR RefSeq; YP_207535.1; NC_002946.2. DR ProteinModelPortal; Q5F9L4; -. DR SMR; Q5F9L4; 4-191. DR EnsemblBacteria; AAW89123; AAW89123; NGO_0379. DR GeneID; 3282007; -. DR KEGG; ngo:NGO0379; -. DR PATRIC; 20333763; VBINeiGon24812_0459. DR HOGENOM; HOG000004796; -. DR KO; K01056; -. DR OMA; FMNRSGL; -. DR OrthoDB; EOG6C5RTR; -. DR BioCyc; NGON242231:GI2G-358-MONOMER; -. DR Proteomes; UP000000535; 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_0000187781. SQ SEQUENCE 192 AA; 21446 MW; 11ED35EFF04152F6 CRC64; MSNTIKMVVG LGNPGKEYEQ TRHNAGFWFL DELAWKWKAS FKEEKKFFGE VARAALPDGD VWLLKPATFM NRSGQAVAAL AQFYKIKPEE ILVVHDELDI PCGRIKFKLG GGNGGHNGLK DIQAKLGTAD YYRLRLGIGH PGDRNLVVGY VLNKPSAEHR RQIDDAVAKS LQAVPDIISG KWEEATRFLH SK // ID PUR4_NEIG1 Reviewed; 1314 AA. AC Q5F7J4; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 09-DEC-2015, entry version 78. 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=NGO1183; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89843.1; 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; AE004969; AAW89843.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_208255.1; NC_002946.2. DR ProteinModelPortal; Q5F7J4; -. DR MEROPS; C56.972; -. DR EnsemblBacteria; AAW89843; AAW89843; NGO_1183. DR GeneID; 3281977; -. DR KEGG; ngo:NGO1183; -. DR PATRIC; 20335663; VBINeiGon24812_1390. DR HOGENOM; HOG000261359; -. DR KO; K01952; -. DR OrthoDB; EOG6FNHHR; -. DR BioCyc; NGON242231:GI2G-1095-MONOMER; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000535; 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; 2. 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 1314 Phosphoribosylformylglycinamidine FT synthase. FT /FTId=PRO_0000264582. FT DOMAIN 1063 1314 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00419}. FT NP_BIND 307 318 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1156 1156 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT ACT_SITE 1279 1279 {ECO:0000255|HAMAP-Rule:MF_00419}. FT ACT_SITE 1281 1281 {ECO:0000255|HAMAP-Rule:MF_00419}. FT METAL 675 675 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 714 714 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 718 718 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT METAL 880 880 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00419}. FT BINDING 674 674 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00419}. FT BINDING 882 882 ATP. {ECO:0000255|HAMAP-Rule:MF_00419}. SQ SEQUENCE 1314 AA; 142972 MW; B9DD36708873144D CRC64; MPLRGVTALS DFRVEKLLQK AAALGLPEVK LSSEFWYFAG SEKALDAATV EKLQALLAAQ SVEQTPEARE GLHLFLVTPR LGTISPWASK ATNIAENCGL AGIERIERGM AVWLEGALTD EQKQQWAALL HDRMTESVLP DFQTASKLFH HLKSETFSTV DVLGGGKEAL VKANTETGLA LSADEIDYLV ENYQALQRNP SDVELMMFAQ ANSEHCRHKI FNADFILNGE KQPKSLFGMI RDTHNAHPEG TVVAYKDNSS VIKGAKIERF YPNAAENQGY RFHEEDTHII MKVETHNHPT AIAPFAGAAT GAGGEIRDEG ATGKGSRPKA GLTGFTVSNL NIPDLKQPWE QDYGKPEHIS SPLDIMIEGP IGGAAFNNEF GRPNLLGYFR TFEEKFDGQV RGYHKPIMIA GGLGSIQAQQ THKDEIPEGA LLIQLGGPGM LIGLGGGAAS SMDTGTNDAS LDFNSVQRGN PEIERRAQEV IDRCWQLGDQ NPIISIHDVG AGGLSNAFPE LVNDAGRGAV FELREVPLEE HGLTPLQIWC NESQERYVLS ILEKDLDTFR AICERERCPF AVVGTATDDG HLKVRDDLFS NNPVDLPLNV LLGKPPKTTR TDKTVTPSKK PFHAGDIDIT EAAYRVLRLP AVAAKNFLIT IGDRSVGGMT HRDQMVGKYQ TPVADCAVTM MGFNTYRGEA MSMGEKPAVA LFDAPASGRM CVGEAITNIA AVNIGDIGNI KLSANWMAAC GNEGEDEKLY RTVEAVSKAC QALDLSIPVG KDSLSMKTVW QDGEEKKSVV SPLSLIISAF APVKDVRKTV TPELKNVEGS VLLFIDLGFG KARMGGSAFG QVYNNMSGDA PDLDDAGRLK AFYSVIQQLV AEDKLLAYHD RSDGGLFATL AEMAFAARCG ISADIDCLMD KFLPIHLPDF QGDPAEDLSD ELYNHAAIKI LFNEELGAVI QIRQKDRDYV DAAFETAGLT DAVSRIGSPD FDNEFISFFG YGYFLEQNRA DLQRAWQETS HAIQRLRDNP ACADSEFALI GDNERSALFA DVKFDVNEDI AAPFINSGAK PKIAILREQG VNGQIEMAAA FTRAGFDAYD VHMSDLMAGR FRLADFKMLA ACGGFSYGDV LGAGEGWAKS ILFHPALRDQ FAAFFADPNT LTLGVCNGCQ MVSNLAEIIP GAETWPKFKR NLSEQFEARL NMVHVPKSAS LILNEMQDSS LPVVVSHGEG RADFALHGGN ISADLGIALQ YVDGQNQVTQ TYPLNPNGSP QGIAGITNAD GRVTIMMPHP ERVYRAAQMS RKPEGWTELS GWYRLFAGAR KALG // ID PYRB_NEIG1 Reviewed; 306 AA. AC Q5F5P0; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1877; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90497.1; -; Genomic_DNA. DR RefSeq; WP_003705350.1; NC_002946.2. DR RefSeq; YP_208909.1; NC_002946.2. DR ProteinModelPortal; Q5F5P0; -. DR SMR; Q5F5P0; 3-306. DR EnsemblBacteria; AAW90497; AAW90497; NGO_1877. DR GeneID; 3282349; -. DR KEGG; ngo:NGO1877; -. DR PATRIC; 20337450; VBINeiGon24812_2256. DR HOGENOM; HOG000022685; -. DR KO; K00609; -. DR OMA; KQSFYGV; -. DR OrthoDB; EOG61KBJZ; -. DR BioCyc; NGON242231:GI2G-1781-MONOMER; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000000535; 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_0000301596. SQ SEQUENCE 306 AA; 34196 MW; BEC45F8497711EDD CRC64; MPNPLYRQHI ISISDLSREQ LEYLLQTALK LKAHPRGDLL EGKLIGSCFF EPSTRTRLSF ETAVQRLGGK VIGFSDGANT SAKKGETLAD TARIISGYTD AIVQRHPKDG AARVAAEFSR VPVINAGDGT NQHPSQTLLD LVTIYETQGR LDKLKIAMAG DLKYGRTVHS LCQALKRWGC EFAFVSPPSL AMPDYITEEL EEADCRYRAL GSLEEAAEWA DILYMTRVQR ERFDEQEFAK IQGKFNLEAS MLARAKPNLR VLHPLPRTDE IHPDVDAAPH AYYFEQATNG VYARMAILSL VLNEEV // ID PYRC_NEIG1 Reviewed; 344 AA. AC Q5F9Y1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0255; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89006.1; -; Genomic_DNA. DR RefSeq; WP_003706656.1; NC_002946.2. DR RefSeq; YP_207418.1; NC_002946.2. DR ProteinModelPortal; Q5F9Y1; -. DR SMR; Q5F9Y1; 2-343. DR EnsemblBacteria; AAW89006; AAW89006; NGO_0255. DR GeneID; 3281552; -. DR KEGG; ngo:NGO0255; -. DR PATRIC; 20333467; VBINeiGon24812_0314. DR HOGENOM; HOG000256259; -. DR KO; K01465; -. DR OMA; YAEAFEQ; -. DR OrthoDB; EOG6TFCMH; -. DR BioCyc; NGON242231:GI2G-238-MONOMER; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000535; 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_1000024023. 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; 37068 MW; 9FBF97FD9D68F06E CRC64; MQTLTIIRPD DMHLHLRDGD ALKAVAPYTA RQMGRAVIMP NLKPPVVSVA DALAYKARIM AALPEGSAFE PLMTLYLTDQ ATPELVREAK AAGIVAFKLY PAGATTNSDS GVTDLFKLIP VLEEMAKQGI LFLVHGEVTD PEIDIFDREA AFIGRVMKPV LAQVPNLKVV FEHITTAEAA RLVLEAGDNV AATVTPQHLL LNRNDLLVGG VRPHHFCLPV LKRETHRQAL VAAVTGEKAH KFFLGTDSAP HAKSAKENAC GCAGMFSAMT AIELYAEVFE KAGALDKLEA FASKNGARFY GIPENADTIT LVKQSQTVPA SVPYGDGELV PMRAGGEIGW TVQY // ID PYRG_NEIG1 Reviewed; 544 AA. AC Q5F7G6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1212; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89871.1; -; Genomic_DNA. DR RefSeq; WP_003689652.1; NC_002946.2. DR RefSeq; YP_208283.1; NC_002946.2. DR ProteinModelPortal; Q5F7G6; -. DR SMR; Q5F7G6; 2-543. DR EnsemblBacteria; AAW89871; AAW89871; NGO_1212. DR GeneID; 3281956; -. DR KEGG; ngo:NGO1212; -. DR PATRIC; 20335731; VBINeiGon24812_1424. DR HOGENOM; HOG000077515; -. DR KO; K01937; -. DR OMA; MRLGEYE; -. DR OrthoDB; EOG6RC3NR; -. DR BioCyc; NGON242231:GI2G-1123-MONOMER; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000000535; 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_0000266160. 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; 59841 MW; 1533C588C8A1304B CRC64; MTKFIFVTGG VVSSLGKGIA AASIAAILES RGLNVTMLKL DPYINVDPGT MSPFQHGEVF VTDDGAETDL DLGHYERFID STMTRRNSFS TGQVYENVIA KERRGDYLGG TVQVIPHITD EIKRRIHEGA AGYDVAIVEI GGTVGDIESL PFLEAIRQMR SQLGRNNTLF AHLSYVPYIA AAGEIKTKPT QHTVKEMLSI GLQPDILICR MDRKMPADER RKIALFCNVE ERAIVGSYDV DSIYECPEML HDQGIDNIIT EQLQLNVQQA DLTAWKKIVH AVKNPKHTVK IAMVGKYVDL TESYKSLIEA LKHAGIHTET DVQITFVDSE SIEKNKGDVS VLKDMDAILV PGGFGSRGVE GKIAAVRYAR ENNVPYLGIC LGMQIALIEY ARDVAGLKGA NSTEFDLKCA APVVALIDEW QTADGSVETR DESADLGGTM RLGAQEVELK AGSLAVKIYG SGHIRERHRH RYEVNNNYVS ALEQAGLVIG GVSAGRERLV ETIELPNHPW FFACQFHPEF TSNPRKGHPL FTAFVKAALN NKKA // ID PUR9_NEIG1 Reviewed; 526 AA. AC Q5F6T1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1466; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90106.1; -; Genomic_DNA. DR RefSeq; WP_010358883.1; NC_002946.2. DR RefSeq; YP_208518.1; NC_002946.2. DR ProteinModelPortal; Q5F6T1; -. DR EnsemblBacteria; AAW90106; AAW90106; NGO_1466. DR GeneID; 3281673; -. DR KEGG; ngo:NGO1466; -. DR PATRIC; 20336365; VBINeiGon24812_1731. DR HOGENOM; HOG000230372; -. DR KO; K00602; -. DR OMA; PCGVAEG; -. DR OrthoDB; EOG6QCDFF; -. DR BioCyc; NGON242231:GI2G-1371-MONOMER; -. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000535; 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_1000018917. SQ SEQUENCE 526 AA; 56688 MW; 81B4D1A62A843711 CRC64; MSVIKRALIS LSDKAGAVEF AQNLHKLGVE ILSTGGTAKL LAGAGVPVIE VADYTGFPEM LDGRVKTLHP KIHGGILGRR DLDEHVAKME EHGIGNIDLV CVNLYPFAAT IAKPGCTLED AIENIDIGGP TMVRSAAKNW KHVAIVTDTA DFPAIAAELE ANNGALSDKT RFNLSRKAFS HTAQYDGMIS NYLTSLSDGV LSGEPEIGEF PSRFNQSWIK VQDMRYGENP HQRAAFYRDI DPAAGSLSAY NQLQGKELSY NNIADADAAW EAVKSFDAPA CVIVKHANPC GVAVAADTLT AYKLAYATDT TSAFGGIIAF NREVDGETVK QITDNQFMEV LMAPKFTAEA LEIAAAKKNV RVLEVPLKAG ANRFELKRVG GGLLVQTPDI NRINRADLKV VSKRQPTEQE WNDLLFVWNV AKYVKSNAIV FGKGGQTYGI GAGQMSRVDS TRIAARKAQD AGLDLNGACA ASDAFFPFRD GVDVIAEQGI KAIIHPAGSM RDQEVFDAAD EHGIAMAVTG IRHFRH // ID PYRF_NEIG1 Reviewed; 246 AA. AC Q5F9J2; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO0401; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89145.1; -; Genomic_DNA. DR RefSeq; WP_003687835.1; NC_002946.2. DR RefSeq; YP_207557.1; NC_002946.2. DR ProteinModelPortal; Q5F9J2; -. DR PRIDE; Q5F9J2; -. DR EnsemblBacteria; AAW89145; AAW89145; NGO_0401. DR GeneID; 3283006; -. DR KEGG; ngo:NGO0401; -. DR PATRIC; 20333811; VBINeiGon24812_0483. DR HOGENOM; HOG000226071; -. DR KO; K01591; -. DR OMA; NFKIFLD; -. DR OrthoDB; EOG6N6815; -. DR BioCyc; NGON242231:GI2G-380-MONOMER; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000535; 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_0000241878. 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; 26506 MW; B02D9E41AFB1EECA CRC64; MNPLITDFQT PQQRTPVIVA LDFANEKDTL GFVRNLDPAL CQIKIGKELF TATGRSLAES LIHQGFKLFL DLKYHDIPHT VAQACKVAAD MGVWMVDMHA SGGRRMMEAA AEAVAGYGTK PLLIGVTVLT SMEQSDLAEI GLNTAPEEQV IRLAKLAQSS GLDGVVCSAQ EAAPLRRELG RDFVLVTPGI RLDVAGNNDD QRRIMTPAEA LAAGSTYLVM GRPVTRAADP VAVLREVNRV ANLEAN // ID PURA_NEIG1 Reviewed; 434 AA. AC Q5F9J5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 79. 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=NGO0398; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89142.1; -; Genomic_DNA. DR RefSeq; WP_003690856.1; NC_002946.2. DR RefSeq; YP_207554.1; NC_002946.2. DR ProteinModelPortal; Q5F9J5; -. DR SMR; Q5F9J5; 4-434. DR EnsemblBacteria; AAW89142; AAW89142; NGO_0398. DR GeneID; 3283011; -. DR KEGG; ngo:NGO0398; -. DR PATRIC; 20333803; VBINeiGon24812_0479. DR HOGENOM; HOG000260959; -. DR KO; K01939; -. DR OMA; FHHAKPI; -. DR OrthoDB; EOG68Q0QG; -. DR BioCyc; NGON242231:GI2G-377-MONOMER; -. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000000535; 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 1 434 Adenylosuccinate synthetase. FT /FTId=PRO_0000224296. FT NP_BIND 15 21 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 43 45 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 335 337 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 418 420 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT REGION 16 19 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 41 44 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 303 309 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 16 16 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 44 44 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 16 16 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 43 43 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 133 133 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 147 147 IMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 228 228 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 243 243 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 307 307 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 309 309 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. SQ SEQUENCE 434 AA; 45982 MW; 9E02DE741966037B CRC64; MAMAKNVVVI GAQWGDEGKG KIVDWLAEEA GGVVRFQGGH NAGHTLVVGG KKTILRLIPS GILHEGLDCF IGSGVVVSPE ALLGEIDELN AAGVKNVEGR LKIAPTCPLI LPYHIALDQA REASRGKGKI GTTGRGIGPA YEDKVARRAI RAADLLHPEK LREKLDAVLA YYNVQLQYLH NAGPVKAEDV MAVIEKVAPR IAPMIADVSR VLNEKNKNGE KLLFEGAQGA LLDIDYGTYP FVTSSNCLAG AASAGAGVGP QMLDYVLGIV KAYTTRVGSG PFPTELFDEV GAGLAERGHE FGSVTGRARR CGWFDAAALK RSIQINGISG MCITKLDVMD GVETINICVG YELPGGGKTD ILPCGSDAVE TCKPIYETMP GWRESTVGVK SYDALPANAK AYLKRIEEVC GAPVAIVSTG PDREETIVLH HPFA // ID PUR5_NEIG1 Reviewed; 344 AA. AC Q5F973; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0526; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89264.1; -; Genomic_DNA. DR RefSeq; WP_003691398.1; NC_002946.2. DR RefSeq; YP_207676.1; NC_002946.2. DR ProteinModelPortal; Q5F973; -. DR SMR; Q5F973; 3-337. DR EnsemblBacteria; AAW89264; AAW89264; NGO_0526. DR GeneID; 3282922; -. DR KEGG; ngo:NGO0526; -. DR PATRIC; 20334098; VBINeiGon24812_0621. DR HOGENOM; HOG000229090; -. DR KO; K01933; -. DR OMA; NHCVNDI; -. DR OrthoDB; EOG61CM1V; -. DR BioCyc; NGON242231:GI2G-504-MONOMER; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000535; 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_0000258373. SQ SEQUENCE 344 AA; 36898 MW; 2B0C48782E32F485 CRC64; MSTSLSYRDA GVGIDAGDQL VEKIKPFAKR TMRPEVLGDL GGFGALVEIG KKYQNPVLVS GTDGVGTKLK LAFDWDKHDT VGIDLVAMSV NDILVQGAEP LFFLDYFACG KLDVPRATDV IKGIAQGCEE SGCALIGGET AEMPGMYPVG EYDLAGFAVG VVEKENVITG LSIGAGDVVL GLASNGAHSN GYSLIRKIIE RDNPDLDAEF DNGKTLREAV IAPTRLYVKP ILAALEKFTI KGMAHITGGG ITENVPRVLP KNTVAQIDAE SWELPKLFQW LQKAGNVETQ EMYRTFNCGI GMVVIVAAED ADAVRSFLSG QGETVYRLGC IRERQGNEHQ TQVA // ID QUEC_NEIG1 Reviewed; 224 AA. AC Q5FA99; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0129; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88888.1; -; Genomic_DNA. DR RefSeq; WP_010950996.1; NC_002946.2. DR RefSeq; YP_207300.1; NC_002946.2. DR ProteinModelPortal; Q5FA99; -. DR EnsemblBacteria; AAW88888; AAW88888; NGO_0129. DR GeneID; 3282488; -. DR KEGG; ngo:NGO0129; -. DR PATRIC; 20333165; VBINeiGon24812_0166. DR HOGENOM; HOG000110563; -. DR KO; K06920; -. DR OMA; AYGYGCD; -. DR OrthoDB; EOG6091HB; -. DR BioCyc; NGON242231:GI2G-117-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000535; 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 1 224 7-cyano-7-deazaguanine synthase. FT /FTId=PRO_0000246863. FT NP_BIND 10 20 ATP. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 193 193 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 201 201 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 204 204 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 207 207 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. SQ SEQUENCE 224 AA; 24798 MW; 6EE981FC8A4C6F2C CRC64; MSNQKALVIF SGGQDSTTCL IQAIQTYGRE NVQAITFRYG QRHAVELERA EWIAQDLGVS QTVLDLSLMR QITHNALMDE TAAIETAAIE TADNGVPNTF VDGRNALFLL YAAIFAKGQG IRHIIAGVCE TDFSGYPDCR GVFVKSMNVT LNLAMDYDFQ IHTPLMYLTK AQTWALADEM GVLDYIREQT HTCYKGIVGG CRECPSCILR ERGLAECLES KKAV // ID PYRE_NEIG1 Reviewed; 213 AA. AC Q5FAK5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO0029; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88798.1; -; Genomic_DNA. DR RefSeq; WP_003690501.1; NC_002946.2. DR RefSeq; YP_207210.1; NC_002946.2. DR ProteinModelPortal; Q5FAK5; -. DR SMR; Q5FAK5; 1-212. DR EnsemblBacteria; AAW88798; AAW88798; NGO_0029. DR GeneID; 3282518; -. DR KEGG; ngo:NGO0029; -. DR PATRIC; 20332888; VBINeiGon24812_0029. DR HOGENOM; HOG000037974; -. DR KO; K00762; -. DR OMA; MKAYQRQ; -. DR OrthoDB; EOG6091H8; -. DR BioCyc; NGON242231:GI2G-26-MONOMER; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000535; 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_1000066259. 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 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; 23268 MW; 8AC4ABB32FB6A7DD CRC64; MTDFRQDFLK FSLAQNVLKF GEFTTKAGRR SPYFFNAGLF NDGASTLQLA KFYAQSIIES GIRFDMLFGP AYKGIILAAA TAMMLAEKGV NVPFAYNRKE AKDRGEGGVL VGAPLKGRVL IIDDVISAGT SVRESIKLIE AEGATPAGVA IALDRMEKGT GKLSAVQEVE KQYGLPVAPI ASLNDLFILL QNNPEFGQFL EPVRTYRRQY GVE // ID PYRI_NEIG1 Reviewed; 152 AA. AC Q5F5P1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002}; GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; GN OrderedLocusNames=NGO1876; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90496.1; -; Genomic_DNA. DR RefSeq; WP_003690135.1; NC_002946.2. DR RefSeq; YP_208908.1; NC_002946.2. DR ProteinModelPortal; Q5F5P1; -. DR SMR; Q5F5P1; 13-151. DR EnsemblBacteria; AAW90496; AAW90496; NGO_1876. DR GeneID; 3282329; -. DR KEGG; ngo:NGO1876; -. DR PATRIC; 20337448; VBINeiGon24812_2255. DR HOGENOM; HOG000113530; -. DR KO; K00610; -. DR OMA; MNVPSDR; -. DR OrthoDB; EOG6JX7QS; -. DR BioCyc; NGON242231:GI2G-1780-MONOMER; -. DR Proteomes; UP000000535; 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_1000000043. 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; 16916 MW; 0DC3D378EB02970B CRC64; MEAQKLSVEA IEKGTVIDHI PAGRGLTILR QFKLLHYGNA VTVGFNLPSK TQGSKDIIKI KGVCLDDKAA DRLALFAPEA VVNTIDNFKV VQKRHLTLPD EIAEVFRCPN PNCAGHGEPV KSRFYVKKHN GQTRLKCHYC EKTYNRDSVA EA // ID QUEA_NEIG1 Reviewed; 346 AA. AC Q5FAH3; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO0047; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88814.1; -; Genomic_DNA. DR RefSeq; WP_010950980.1; NC_002946.2. DR RefSeq; YP_207226.1; NC_002946.2. DR ProteinModelPortal; Q5FAH3; -. DR EnsemblBacteria; AAW88814; AAW88814; NGO_0047. DR GeneID; 3282377; -. DR KEGG; ngo:NGO0047; -. DR PATRIC; 20332934; VBINeiGon24812_0052. DR HOGENOM; HOG000004401; -. DR KO; K07568; -. DR OMA; YGDAMFL; -. DR OrthoDB; EOG6X6RBB; -. DR BioCyc; NGON242231:GI2G-42-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000535; 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_0000231350. SQ SEQUENCE 346 AA; 38151 MW; 3179645DF091AFAC CRC64; MDISDFDFTL PEHLIAQHPP EVRGSSRLLV ALSDMPLQDR VFGDLPDYVE AGDVLVFNNT KVMKARLFGQ KDSGGRIEAL IERVLDNHTA LAHIRSSKSP KPGMGLVFEG GIRAVMVGRE GELFCLRFEG GQTVYELLEQ NGHLPLPPYI ERAADADDDS RYQTVYAKYQ GAVAAPTAGL HFTEELLRRL KDKGAVTAEV TLHVGAGTFQ PVRVDKIEEH KMHSEWFEVP SETVAAVEAA KARGNKAWAV GTTSMRALES AARATGYLKD GQGDTDIFIT PGYRFNVVDR LVTNFHLPKS TLLMLVGAFS GMGHIRAVYR HAIEREYRFF SYGDAMVLGR NEGGGL // ID QUEF_NEIG1 Reviewed; 157 AA. AC Q5F678; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO1684; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90309.1; -; Genomic_DNA. DR RefSeq; WP_003689837.1; NC_002946.2. DR RefSeq; YP_208721.1; NC_002946.2. DR ProteinModelPortal; Q5F678; -. DR EnsemblBacteria; AAW90309; AAW90309; NGO_1684. DR GeneID; 3281260; -. DR KEGG; ngo:NGO1684; -. DR PATRIC; 20336926; VBINeiGon24812_2007. DR HOGENOM; HOG000009528; -. DR KO; K09457; -. DR OMA; LITLECK; -. DR OrthoDB; EOG6D5G0M; -. DR BioCyc; NGON242231:GI2G-1579-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000535; 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_0000162980. 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; 17999 MW; E36CADA89FC71A42 CRC64; MSRNNEELQG ISLLGNQKTQ YPTGYAPEIL EAFDNKHPDN DYFVKFVCPE FTSLCPMTGQ PDFATIVIRY IPHIKMVESK SLKLYLFSFR NHGDFHEDCV NIIMKDLIAL MDPKYIEVFG EFTPRGGIAV HPFANYGKAG TEFEALARKR LFEHDAQ // ID PYRD_NEIG1 Reviewed; 335 AA. AC Q5F605; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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=NGO1761; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90382.1; -; Genomic_DNA. DR RefSeq; WP_003689966.1; NC_002946.2. DR RefSeq; YP_208794.1; NC_002946.2. DR ProteinModelPortal; Q5F605; -. DR SMR; Q5F605; 2-333. DR EnsemblBacteria; AAW90382; AAW90382; NGO_1761. DR GeneID; 3281087; -. DR KEGG; ngo:NGO1761; -. DR PATRIC; 20337136; VBINeiGon24812_2108. DR HOGENOM; HOG000225103; -. DR KO; K00254; -. DR OMA; TLVRHKM; -. DR OrthoDB; EOG65BDN8; -. DR BioCyc; NGON242231:GI2G-1657-MONOMER; -. DR UniPathway; UPA00070; UER00946. DR Proteomes; UP000000535; 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_0000148458. 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; 35821 MW; E30F203F14C40560 CRC64; MYPLARRILF ALDAEKAHHF TLDALNTVYK LGLIPVTDNR TKPIKLMGMD LPNPVGLAAG LDKNGEYIDA LGALGFGFLE IGTVTRNPQP GNPQPRLFRV PEHQGIINRM GFNNHGIDAM IRNIEKSKYQ GVLGINIGKN AVTPIQNAAD DYLICLEKAY AHASYITVNI SSPNTKNLRA LQGGGELGAL LEALKNKQAQ LAAAHGKYIP LAVKIAPDLD EAQIEDIARV VKSVEMDGII ATNTTIDKSS LGSHPLAGEQ GGLSGFPVRE KSNRVLKKLA EHIDGALPII GVGGIMEGGD AAEKIRLGTT AVQVYSGLIY KGPALVKECL KALAR // ID RDGC_NEIG1 Reviewed; 299 AA. AC O87408; Q5F9H1; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Recombination-associated protein RdgC; GN Name=rdgC; OrderedLocusNames=NGO0423; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RX PubMed=10655208; RA Mehr I.J., Long C.D., Serkin C.D., Seifert H.S.; RT "A homologue of the recombination-dependent growth gene, rdgC, is RT involved in gonococcal pilin antigenic variation."; RL Genetics 154:523-532(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be involved in recombination. CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mutations affect pilin antigenic variation; CC some mutations create growth defects. CC {ECO:0000269|PubMed:10655208}. CC -!- SIMILARITY: Belongs to the RdgC 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; AF058711; AAC63509.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89166.1; -; Genomic_DNA. DR RefSeq; WP_003687870.1; NC_002946.2. DR RefSeq; YP_207578.1; NC_002946.2. DR ProteinModelPortal; O87408; -. DR EnsemblBacteria; AAW89166; AAW89166; NGO_0423. DR GeneID; 3282581; -. DR KEGG; ngo:NGO0423; -. DR PATRIC; 20333859; VBINeiGon24812_0507. DR HOGENOM; HOG000117544; -. DR KO; K03554; -. DR OMA; PCSSQDI; -. DR OrthoDB; EOG6WX4MD; -. DR BioCyc; NGON242231:GI2G-401-MONOMER; -. DR Proteomes; UP000000535; 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_0000211741. SQ SEQUENCE 299 AA; 33292 MW; 5D3A12F4274717C8 CRC64; MWFKQISFYP LNKEKLPEAD VLADKLAEAE FTHCQGLDWF SEGFTAPVSF SPELVFPADF TLRVALKKEE KVLPAGVIRD ILEEKVAEIQ NNEARNVGRK EKQELKEQIT DDLLPRAFTR SSRTEAVFNT RHGYLLVNNA ASAKAENILT KLREALGGLE ASLPNTKQSP SSLMTGWLLQ GHCEGGFELD SDCELKGTGD IVPVVKVSKQ DLTADEVVQH VKNGKTVTRL GLVWREQIAF ILTQDFTLKR IQYLDVLQEE AESNGDDAAG LAFASQILMA ESVSTMLEEL VSYLGGWQD // ID PYRH_NEIG1 Reviewed; 239 AA. AC Q5F5F5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. DE RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UK {ECO:0000255|HAMAP-Rule:MF_01220}; DE EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220}; DE AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220}; GN Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220}; GN OrderedLocusNames=NGO1973; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- ENZYME REGULATION: Inhibited by UTP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90582.1; -; Genomic_DNA. DR RefSeq; WP_003686859.1; NC_002946.2. DR RefSeq; YP_208994.1; NC_002946.2. DR ProteinModelPortal; Q5F5F5; -. DR SMR; Q5F5F5; 4-239. DR EnsemblBacteria; AAW90582; AAW90582; NGO_1973. DR GeneID; 3282650; -. DR KEGG; ngo:NGO1973; -. DR PATRIC; 20337711; VBINeiGon24812_2382. DR HOGENOM; HOG000047187; -. DR KO; K09903; -. DR OMA; RSRADYM; -. DR OrthoDB; EOG6M0T8S; -. DR BioCyc; NGON242231:GI2G-1872-MONOMER; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000000535; 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 Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02075; pyrH_bact; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 239 Uridylate kinase. FT /FTId=PRO_1000053965. FT NP_BIND 13 16 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 136 143 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 55 55 UMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 56 56 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 60 60 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 75 75 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 163 163 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 164 164 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 169 169 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 172 172 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 239 AA; 25714 MW; 1F0C3837C252E466 CRC64; MTQQIKYKRV LLKLSGESLM GSDPFGINHD TIVQTVGEIA EIVKMGVQVG IVVGGGNIFR GVSAQAGSMD RATADYMGMM ATVMNALALK DAFETLGIKA RVQSALSMQQ IAETYARPKA IQYLEEGKVV IFAAGTGNPF FTTDTAAALR GAEMNCDVML KATNVDGVYT ADPKKDPSAT RYETITFDEA LNKNLKVMDA TAFALCRERK LNIVVFGIAK QGSLKRVITG EDEGTLVHC // ID RF3_NEIG1 Reviewed; 531 AA. AC Q5FA25; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO0209; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88962.1; -; Genomic_DNA. DR RefSeq; WP_003704835.1; NC_002946.2. DR RefSeq; YP_207374.1; NC_002946.2. DR ProteinModelPortal; Q5FA25; -. DR SMR; Q5FA25; 1-527. DR EnsemblBacteria; AAW88962; AAW88962; NGO_0209. DR GeneID; 3281358; -. DR KEGG; ngo:NGO0209; -. DR PATRIC; 20333355; VBINeiGon24812_0260. DR HOGENOM; HOG000236725; -. DR KO; K02837; -. DR OMA; DFAEDTY; -. DR OrthoDB; EOG6677Q1; -. DR BioCyc; NGON242231:GI2G-192-MONOMER; -. DR Proteomes; UP000000535; 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_0000242192. 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; 59506 MW; 8B8EEB7F7F4F490C CRC64; MSQEILDQVR RRRTFAIISH PDAGKTTLTE KLLLFSGAIQ SAGTVKGKKT GKFATSDWMD IEKQRGISVA SSVMQFDYKD HTVNLLDTPG HQDFSEDTYR VLTAVDSALM VIDAAKGVEA QTIKLLNVCR LRDTPIVTFM NKYDREVRDS LELLDEVEDI LQIRCAPVTW PIGMGKNFKG VYHILNDEIY LFEAGGERLP HEFDIIKGIN NPELEQRFPL EIQQLRDEIE LVQAASNEFN LDEFLAGELT PVFFGSAINN FGIQEILNSL IDWAPAPKPR DATMRMVGPD EPKFSGFIFK IQANMDPKHR DRIAFLRVCS GKFERGMKMK HLRINREIAA SSVVTFMSHD RELAEEAYAG DIIGIPNHGN IQIGDSFSEG EQLAFTGIPF FAPELFRSVR IKNPLKIKQL QKGLQQLGEE GAVQVFKPMS GADLILGAVG VLQFEVVTSR LANEYGVEAV FDSASIWSAR WVSCDDKKKL AEFEKANAGN LAIDAGGNLA YLAPNRVNLG LTQERWPDIV FHETREHSVK L // ID RECX_NEIG1 Reviewed; 153 AA. AC Q5F7W3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=Regulatory protein RecX {ECO:0000255|HAMAP-Rule:MF_01114}; GN Name=recX {ECO:0000255|HAMAP-Rule:MF_01114}; GN OrderedLocusNames=NGO1053; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Modulates RecA activity. {ECO:0000255|HAMAP- CC Rule:MF_01114}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01114}. CC -!- SIMILARITY: Belongs to the RecX family. {ECO:0000255|HAMAP- CC Rule:MF_01114}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89724.1; -; Genomic_DNA. DR RefSeq; WP_003688187.1; NC_002946.2. DR RefSeq; YP_208136.1; NC_002946.2. DR ProteinModelPortal; Q5F7W3; -. DR EnsemblBacteria; AAW89724; AAW89724; NGO_1053. DR GeneID; 3281800; -. DR KEGG; ngo:NGO1053; -. DR PATRIC; 20335338; VBINeiGon24812_1235. DR HOGENOM; HOG000242561; -. DR KO; K03565; -. DR OMA; IESAMHF; -. DR OrthoDB; EOG693GQ0; -. DR BioCyc; NGON242231:GI2G-969-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032780; P:negative regulation of ATPase activity; IDA:CACAO. 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_1000065191. SQ SEQUENCE 153 AA; 17745 MW; 0F0D5833D4FCBD29 CRC64; MKPQKSLRAR AMDILSRQEV SRIGLKRKLA PHAESEEELE NVLNEFAERN WQSDLRYAEA YIRSKSRKHG SLRLKQALAQ QGIDEKTSRN LLPDRSSEKQ AAIAVLRKKF KHPAANLKEK QKQARFLAYR GFDADTVQTA LKHAWDENWE DSC // ID RBFA_NEIG1 Reviewed; 123 AA. AC Q5F8W6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Ribosome-binding factor A {ECO:0000255|HAMAP-Rule:MF_00003}; GN Name=rbfA {ECO:0000255|HAMAP-Rule:MF_00003}; GN OrderedLocusNames=NGO0644; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89371.1; -; Genomic_DNA. DR RefSeq; WP_010951100.1; NC_002946.2. DR RefSeq; YP_207783.1; NC_002946.2. DR ProteinModelPortal; Q5F8W6; -. DR EnsemblBacteria; AAW89371; AAW89371; NGO_0644. DR GeneID; 3281282; -. DR KEGG; ngo:NGO0644; -. DR PATRIC; 20334372; VBINeiGon24812_0758. DR HOGENOM; HOG000218325; -. DR KO; K02834; -. DR OMA; RGMNLSA; -. DR OrthoDB; EOG6XQ3TJ; -. DR BioCyc; NGON242231:GI2G-611-MONOMER; -. DR Proteomes; UP000000535; 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_1000000151. SQ SEQUENCE 123 AA; 14369 MW; F2607DCEF7B39DE3 CRC64; MKKPQRGYAR QDRVKEQIMR ELAELVRTGL KDPRAGFITI NEVEITRDYS HATVFYTVLN QDTREITEEV LEHARGHLRS ELSKRIKLFK IPELHFKYDE SLERGMSLSA LIDQVAAEKP VED // ID RECO_NEIG1 Reviewed; 247 AA. AC Q9ZHY2; Q5F6P0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=DNA repair protein RecO; DE AltName: Full=Recombination protein O; GN Name=recO; OrderedLocusNames=NGO1509; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10094619; DOI=10.1046/j.1365-2958.1998.01089.x; RA Mehr I.J., Seifert H.S.; RT "Differential roles of homologous recombination pathways in Neisseria RT gonorrhoeae pilin antigenic variation, DNA transformation and DNA RT repair."; RL Mol. Microbiol. 30:697-710(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in DNA repair and RecF pathway recombination. CC Involved in pilin antigenic variation. 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; AF047375; AAD05426.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90147.1; -; Genomic_DNA. DR RefSeq; WP_003695555.1; NC_002946.2. DR RefSeq; YP_208559.1; NC_002946.2. DR ProteinModelPortal; Q9ZHY2; -. DR EnsemblBacteria; AAW90147; AAW90147; NGO_1509. DR GeneID; 3281563; -. DR KEGG; ngo:NGO1509; -. DR PATRIC; 20336492; VBINeiGon24812_1794. DR HOGENOM; HOG000245560; -. DR KO; K03584; -. DR OMA; YVLHSRA; -. DR OrthoDB; EOG6X10W9; -. DR BioCyc; NGON242231:GI2G-1413-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. 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 1 247 DNA repair protein RecO. FT /FTId=PRO_0000204973. SQ SEQUENCE 247 AA; 27820 MW; 4CC46EA13457EC91 CRC64; MSEYRVNHEP VFMLASSPWR ESSLRVEAFS RRYGRVALLA RSARKRQSEL RGVLVPFVPA SVSWYGSQEL KTLHRAEWMG GWRQPQGRAL FSGLYVNELV LKLTAREDPM SELYDALAKV MEAVCREANH IADLRRFEWK LLNALGVAPD LHADGTGGDI LADKTYRLMP EEAVMPVCRD TGALSHEAGA IVEGQSLIDL REGSFRTAES LQQALKITRL LIGTLLPEGL KSRQVLEQIR QFDRNTA // ID RF1_NEIG1 Reviewed; 358 AA. AC Q5F750; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1337; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89987.1; -; Genomic_DNA. DR RefSeq; WP_003698734.1; NC_002946.2. DR RefSeq; YP_208399.1; NC_002946.2. DR ProteinModelPortal; Q5F750; -. DR SMR; Q5F750; 8-354. DR EnsemblBacteria; AAW89987; AAW89987; NGO_1337. DR GeneID; 3282034; -. DR KEGG; ngo:NGO1337; -. DR PATRIC; 20336043; VBINeiGon24812_1571. DR HOGENOM; HOG000074815; -. DR KO; K02835; -. DR OMA; NRLSEHR; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; NGON242231:GI2G-1251-MONOMER; -. DR Proteomes; UP000000535; 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_0000263303. FT MOD_RES 235 235 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_00093}. SQ SEQUENCE 358 AA; 39780 MW; 89748F0F3B843156 CRC64; MKPSILEKLQ QLGDRLEEVT HLLGQPEATS DMDNYRKLTR EHAELTPVVE VFQNYRLAQS DLADAEEMLS DPEMKDFAAE EIEAAKAKID ELDTELQKLL LPKDADDDKN IFIEIRAGTG GDEAALFAGD LLRMYSRYAE RNRWQVEIVS ANESELGGYK EVIARIVGLG AYSRLKFESG GHRVQRVPAT ESQGRIHTSA CTVAVMPEAD ELEDIELNPA DLRTDTFRAS GAGGQHINKT DSAVRITHLP TGMVVECQDG RSQHANKAQA MKVLAARLND AQKREVQAKE AAERKSLIGS GDRSERIRTY NYPQGRVTDH RINLTLHKLD FVMDGDLAEI TDALIAEHQA ELLAAMGD // ID RECA_NEIG1 Reviewed; 348 AA. AC Q5F8M9; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO0741; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89458.1; -; Genomic_DNA. DR RefSeq; WP_003688695.1; NC_002946.2. DR RefSeq; YP_207870.1; NC_002946.2. DR ProteinModelPortal; Q5F8M9; -. DR SMR; Q5F8M9; 1-326. DR EnsemblBacteria; AAW89458; AAW89458; NGO_0741. DR GeneID; 3281893; -. DR KEGG; ngo:NGO0741; -. DR PATRIC; 20334620; VBINeiGon24812_0882. DR HOGENOM; HOG000264120; -. DR KO; K03553; -. DR OMA; IRQNAGL; -. DR OrthoDB; EOG6ZKXNZ; -. DR BioCyc; NGON242231:GI2G-698-MONOMER; -. DR Proteomes; UP000000535; 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_0000122775. FT NP_BIND 66 73 ATP. {ECO:0000255|HAMAP-Rule:MF_00268}. SQ SEQUENCE 348 AA; 37643 MW; 514DBE0F745D7BAF 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 ENPEISDEID AKIRALNGVE MHITEGTQDE TDGERPEE // ID RECR_NEIG1 Reviewed; 205 AA. AC Q5F8K5; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017}; GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; GN OrderedLocusNames=NGO0767; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89482.1; -; Genomic_DNA. DR RefSeq; WP_003706246.1; NC_002946.2. DR RefSeq; YP_207894.1; NC_002946.2. DR ProteinModelPortal; Q5F8K5; -. DR EnsemblBacteria; AAW89482; AAW89482; NGO_0767. DR GeneID; 3282500; -. DR KEGG; ngo:NGO0767; -. DR PATRIC; 20334684; VBINeiGon24812_0914. DR HOGENOM; HOG000103272; -. DR KO; K06187; -. DR OMA; DVMAIEN; -. DR OrthoDB; EOG62NX85; -. DR BioCyc; NGON242231:GI2G-722-MONOMER; -. DR Proteomes; UP000000535; 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 1 205 Recombination protein RecR. FT /FTId=PRO_0000190353. FT DOMAIN 82 177 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00017}. FT ZN_FING 59 74 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00017}. SQ SEQUENCE 205 AA; 22434 MW; D891A3D7473570CF CRC64; MNSKKQDAFQ RLIGALKVLP NVGPKSAQRM AYHLLQQKRK EAEELVDALQ TALRQVCHCA RCNTFCEGGL CDICADETRD GRRLMVVHMP ADVSNIEAAN CHDGLYFVLM GQINTALGMD VSAIALDRLA QRLDGGEIEE IIIATAFTAE GNATAYVLSE FFKNLPYKVS RLSQGIPLGG ELEYVDAGTL AQAVYERRLI KEGGA // ID RIMM_NEIG1 Reviewed; 169 AA. AC Q5FA58; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=Ribosome maturation factor RimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN Name=rimM {ECO:0000255|HAMAP-Rule:MF_00014}; GN OrderedLocusNames=NGO0173; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88929.1; -; Genomic_DNA. DR RefSeq; WP_003690619.1; NC_002946.2. DR RefSeq; YP_207341.1; NC_002946.2. DR ProteinModelPortal; Q5FA58; -. DR EnsemblBacteria; AAW88929; AAW88929; NGO_0173. DR GeneID; 3281175; -. DR KEGG; ngo:NGO0173; -. DR PATRIC; 20333269; VBINeiGon24812_0217. DR HOGENOM; HOG000220989; -. DR KO; K02860; -. DR OMA; QPWFIQR; -. DR OrthoDB; EOG6SBT2K; -. DR BioCyc; NGON242231:GI2G-159-MONOMER; -. DR Proteomes; UP000000535; 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_0000163321. FT DOMAIN 97 169 PRC barrel. {ECO:0000255|HAMAP- FT Rule:MF_00014}. SQ SEQUENCE 169 AA; 18756 MW; 9CE0658F2A7338E4 CRC64; MTDTQNRVAM GYIKGVFGIK GWLKIAANTE YSDSLLDYPE WHLAKDGKTV SVTLEAGKVV NGELQVKFEG IDDRDSAFSL RGYTIEIPRE AFAPTEEDEY YWADLVGMTV VNKDDTVLGK VSNLMETGAN DVLMIDGEHG QILIPFVSQY IETVDTGSKT ITADWGLDY // ID RIMP_NEIG1 Reviewed; 149 AA. AC Q5F799; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=Ribosome maturation factor RimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN Name=rimP {ECO:0000255|HAMAP-Rule:MF_01077}; GN OrderedLocusNames=NGO1284; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89938.1; -; Genomic_DNA. DR RefSeq; WP_003689194.1; NC_002946.2. DR RefSeq; YP_208350.1; NC_002946.2. DR ProteinModelPortal; Q5F799; -. DR EnsemblBacteria; AAW89938; AAW89938; NGO_1284. DR GeneID; 3282099; -. DR KEGG; ngo:NGO1284; -. DR PATRIC; 20335911; VBINeiGon24812_1510. DR HOGENOM; HOG000242360; -. DR KO; K09748; -. DR OMA; GLKEFEG; -. DR OrthoDB; EOG6NSGP3; -. DR BioCyc; NGON242231:GI2G-1196-MONOMER; -. DR Proteomes; UP000000535; 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_0000229254. SQ SEQUENCE 149 AA; 16460 MW; C72D16E03775E2F4 CRC64; MYIGSSMDIQ TILEKTLPGL GYELVDFELA AQGTLRVFID KEGGITVEDC ATVSNHLSRV FMVEDIGYKN LEISSPGLDR PLKKAADFVR FAGQNAKIKT RLPIGGQKNF IGKIEGCEND TVTVSFDGKT VQIELGNIDK ARLRPEFKF // ID RIBA_NEIG1 Reviewed; 197 AA. AC Q5F7N6; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 70. 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=NGO1134; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89801.1; -; Genomic_DNA. DR RefSeq; WP_003689161.1; NC_002946.2. DR RefSeq; YP_208213.1; NC_002946.2. DR ProteinModelPortal; Q5F7N6; -. DR SMR; Q5F7N6; 5-174. DR EnsemblBacteria; AAW89801; AAW89801; NGO_1134. DR GeneID; 3282140; -. DR KEGG; ngo:NGO1134; -. DR PATRIC; 20335528; VBINeiGon24812_1329. DR HOGENOM; HOG000115442; -. DR KO; K01497; -. DR OMA; PTPFGVF; -. DR OrthoDB; EOG679TK8; -. DR BioCyc; NGON242231:GI2G-1047-MONOMER; -. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000000535; 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_0000151763. 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; 21854 MW; AB10C6483D750B9A CRC64; MSELLDHVAS CRLPTEWGVF TMHGFEEANG QEHVALTVGN CSDGNPVLTR IHSECLTGDA LFSRKCDCGP QLEAAMRAVQ AEGRGIIVYL RQEGRGIGLI NKIRAYHLQE QGMDTVEANL ALGLPVDARD FRLAQSIYEY LGIRSVKLLT NNPEKIQTLK DAGINVVERI PLHVGENLEN ERYLQTKADK LGHLMSE // ID RF2_NEIG1 Reviewed; 367 AA. AC Q5F5H5; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1951; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90562.1; -; Genomic_DNA. DR RefSeq; WP_003688127.1; NC_002946.2. DR RefSeq; YP_208974.1; NC_002946.2. DR ProteinModelPortal; Q5F5H5; -. DR SMR; Q5F5H5; 6-367. DR EnsemblBacteria; AAW90562; AAW90562; NGO_1951. DR GeneID; 3282670; -. DR KEGG; ngo:NGO1951; -. DR PATRIC; 20337645; VBINeiGon24812_2349. DR HOGENOM; HOG000074814; -. DR KO; K02836; -. DR OMA; RLYEHEM; -. DR OrthoDB; EOG6TN48J; -. DR BioCyc; NGON242231:GI2G-1852-MONOMER; -. DR Proteomes; UP000000535; 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_0000166833. FT MOD_RES 254 254 N5-methylglutamine. {ECO:0000255|HAMAP- FT Rule:MF_00094}. SQ SEQUENCE 367 AA; 41362 MW; 84353B9B5087066D CRC64; MEAEVINQLN NTLNDLEKRS EDIRVYMDYQ GKKDRLEEVI GLSEDPELWN DPKRAQEIGK ESKILEGIVL TLDNIASGIE DNRMLIEMAV EENDEEGFAA VKEDVAGLEK QMADLEFKRM FNQPADPNNC FIDITAGAGG TEAEDWAGML FRMYSRYAER KGFKIEILEE DDGEIAGINR ATIRVEGEYA YGLLRTETGV HRLVRYSPFD SNNKRHTSFA SVFVYPEIDD SIEIEINPAD LRIDTYRASG AGGQHINKTD SAVRITHEPT GIVVQCQNDR SQHANKAAAM EMLKSKLYEL EMRKRNEEKQ ALEEGKSDVG WGSQIRSYVL DSSRIKDLRT GYEVGNTKAV LDGDLDGFIE ASLKQGV // ID RL10_NEIG1 Reviewed; 166 AA. AC Q5F5R3; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00362}; GN Name=rplJ {ECO:0000255|HAMAP-Rule:MF_00362}; GN OrderedLocusNames=NGO1853; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000255|HAMAP-Rule:MF_00362}. 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. {ECO:0000255|HAMAP-Rule:MF_00362}. CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family. CC {ECO:0000255|HAMAP-Rule:MF_00362}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90474.1; -; Genomic_DNA. DR RefSeq; WP_003694346.1; NC_002946.2. DR RefSeq; YP_208886.1; NC_002946.2. DR ProteinModelPortal; Q5F5R3; -. DR PRIDE; Q5F5R3; -. DR EnsemblBacteria; AAW90474; AAW90474; NGO_1853. DR GeneID; 3282383; -. DR KEGG; ngo:NGO1853; -. DR PATRIC; 20337386; VBINeiGon24812_2228. DR HOGENOM; HOG000004851; -. DR KO; K02864; -. DR OMA; GVYIRVV; -. DR OrthoDB; EOG6DNTDR; -. DR BioCyc; NGON242231:GI2G-1754-MONOMER; -. DR Proteomes; UP000000535; 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_0000234862. SQ SEQUENCE 166 AA; 17622 MW; F7F51AC3185DE9FE CRC64; MSLNIETKKV AVEEISAAIA NAQTLVVAEY RGISVSSMTE LRANARKEGV YLRVLKNTLA RRAVQGTSFV ELADQMVGPL VYAASEDAVA AAKVLHQFAK KDDKIVVKAG SYNGEVMNAA QVAELASIPS REELLSKLLF VMQAPVSGFA RGLAALAEKK AGEEAA // ID RL13_NEIG1 Reviewed; 143 AA. AC Q5F5A5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rplM {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=NGO2024; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90632.1; -; Genomic_DNA. DR RefSeq; WP_003686944.1; NC_002946.2. DR RefSeq; YP_209044.1; NC_002946.2. DR ProteinModelPortal; Q5F5A5; -. DR SMR; Q5F5A5; 1-142. DR EnsemblBacteria; AAW90632; AAW90632; NGO_2024. DR GeneID; 3282723; -. DR KEGG; ngo:NGO2024; -. DR PATRIC; 20337831; VBINeiGon24812_2439. DR HOGENOM; HOG000225286; -. DR KO; K02871; -. DR OMA; GMLPHNR; -. DR OrthoDB; EOG628FBD; -. DR BioCyc; NGON242231:GI2G-1925-MONOMER; -. DR Proteomes; UP000000535; 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_0000261753. SQ SEQUENCE 143 AA; 16238 MW; 167FE75E741CFBDD CRC64; MKTFSAKPHE VKREWFVIDA QDKVLGRVAT EVASRLRGKH KPEYTPHVDT GDYIIVINAD KLRVTGAKFE DKKYFRHSGF PGGIYERTFR EMQDQFPGRA LEQAVKGMLP KGPLGYAMIK KLKVYAGAEH AHAAQQPKVL ELK // ID RL16_NEIG1 Reviewed; 138 AA. AC Q5F5T4; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=50S ribosomal protein L16 {ECO:0000255|HAMAP-Rule:MF_01342}; GN Name=rplP {ECO:0000255|HAMAP-Rule:MF_01342}; GN OrderedLocusNames=NGO1831.1; ORFNames=NGO18311; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90453.1; -; Genomic_DNA. DR RefSeq; WP_002215430.1; NC_002946.2. DR RefSeq; YP_208865.1; NC_002946.2. DR ProteinModelPortal; Q5F5T4; -. DR SMR; Q5F5T4; 1-136. DR PRIDE; Q5F5T4; -. DR EnsemblBacteria; AAW90453; AAW90453; NGO_18311. DR GeneID; 3282385; -. DR KEGG; ngo:NGO18311; -. DR PATRIC; 20337334; VBINeiGon24812_2202. DR HOGENOM; HOG000164573; -. DR KO; K02878; -. DR OMA; KGAVEYW; -. DR OrthoDB; EOG6WHNWS; -. DR BioCyc; NGON242231:GI2G-1733-MONOMER; -. DR Proteomes; UP000000535; 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_0000062151. SQ SEQUENCE 138 AA; 15519 MW; 7529F4E9F2131F9A CRC64; MLQPTRLKYR KQQKGRNTGI ATRGNKVSFG EFGLKAVGRG RLTARQIEAA RRAMTRHIKR GGRIWIRVFP DKPITEKPIQ VRMGGGKGNV EYYIAEIKPG KVLYEMDGVP EELAREAFEL AAAKLPIPTT FVVRQVGQ // ID RL11_NEIG1 Reviewed; 144 AA. AC Q5F5R1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rplK {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=NGO1855; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90476.1; -; Genomic_DNA. DR RefSeq; WP_003690112.1; NC_002946.2. DR RefSeq; YP_208888.1; NC_002946.2. DR ProteinModelPortal; Q5F5R1; -. DR SMR; Q5F5R1; 2-141. DR EnsemblBacteria; AAW90476; AAW90476; NGO_1855. DR GeneID; 3282315; -. DR KEGG; ngo:NGO1855; -. DR PATRIC; 20337390; VBINeiGon24812_2230. DR HOGENOM; HOG000082123; -. DR KO; K02867; -. DR OMA; CKQFNAK; -. DR OrthoDB; EOG69PQ9D; -. DR BioCyc; NGON242231:GI2G-1756-MONOMER; -. DR Proteomes; UP000000535; 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_0000258174. SQ SEQUENCE 144 AA; 14990 MW; 2CBDF810F8D1C5EE CRC64; MAKKIIGYIK LQIPAGKANP SPPVGPALGQ RGLNIMEFCK AFNAATQGME SGLPIPVVIT AFADKSFTFV MKTPPASILL KKAAGLQKGS SNPLTNKVGK LTRAQLEEIA KTKEPDLTAA DLDAAVRTIA GSARSMGLDV EGVV // ID RL17_NEIG1 Reviewed; 122 AA. AC Q5F5V3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=50S ribosomal protein L17 {ECO:0000255|HAMAP-Rule:MF_01368}; GN Name=rplQ {ECO:0000255|HAMAP-Rule:MF_01368}; GN OrderedLocusNames=NGO1817; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90434.1; -; Genomic_DNA. DR RefSeq; WP_002233417.1; NC_002946.2. DR RefSeq; YP_208846.1; NC_002946.2. DR ProteinModelPortal; Q5F5V3; -. DR SMR; Q5F5V3; 1-118. DR PRIDE; Q5F5V3; -. DR EnsemblBacteria; AAW90434; AAW90434; NGO_1817. DR GeneID; 3282135; -. DR KEGG; ngo:NGO1817; -. DR PATRIC; 20337294; VBINeiGon24812_2182. DR HOGENOM; HOG000019780; -. DR KO; K02879; -. DR OMA; KEGTLCA; -. DR OrthoDB; EOG6GR3GR; -. DR BioCyc; NGON242231:GI2G-1714-MONOMER; -. DR Proteomes; UP000000535; 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_0000267897. SQ SEQUENCE 122 AA; 13775 MW; C58B9EB738943357 CRC64; MRHRNGNRKL NRTSSHRAAM LRNMANSLLT HETIVTTLPK AKELRRVVEP LITLGKKPSL ASRRLAFDRT RDRDVVVKLF GDLGPRFTAR NGGYVRVLKY GFRKGDNAPL ALVELVDKPA AE // ID RL15_NEIG1 Reviewed; 144 AA. AC Q5F5U6; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 66. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rplO {ECO:0000255|HAMAP-Rule:MF_01341}; GN OrderedLocusNames=NGO1823; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90441.1; -; Genomic_DNA. DR RefSeq; WP_003690064.1; NC_002946.2. DR RefSeq; YP_208853.1; NC_002946.2. DR ProteinModelPortal; Q5F5U6; -. DR SMR; Q5F5U6; 3-143. DR EnsemblBacteria; AAW90441; AAW90441; NGO_1823. DR GeneID; 3282419; -. DR KEGG; ngo:NGO1823; -. DR PATRIC; 20337310; VBINeiGon24812_2190. DR HOGENOM; HOG000231262; -. DR KO; K02876; -. DR OMA; HKGQWAR; -. DR OrthoDB; EOG6CGCM5; -. DR BioCyc; NGON242231:GI2G-1721-MONOMER; -. DR Proteomes; UP000000535; 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_0000104768. SQ SEQUENCE 144 AA; 14954 MW; 667BBFBB9FF5B8C5 CRC64; MFLNTIQPAV GATHAGRRVG RGIGSGLGKT GGRGHKGQKS RSGGFHKVGF EGGQMPLQRR LPKRGFKSLT VSANAQLRLS ELESIAVNEI DILVLKQAGL IASTVSNVKV IASGEISKAV ALKGIKVTKG ARAAIEDVGG KIEM // ID RL18_NEIG1 Reviewed; 117 AA. AC Q5F5U3; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rplR {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=NGO1824.1; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90444.1; -; Genomic_DNA. DR RefSeq; WP_002215441.1; NC_002946.2. DR RefSeq; YP_208856.1; NC_002946.2. DR ProteinModelPortal; Q5F5U3; -. DR SMR; Q5F5U3; 2-117. DR EnsemblBacteria; AAW90444; AAW90444; NGO_18241. DR GeneID; 3282166; -. DR KEGG; ngo:NGO18241; -. DR PATRIC; 20337316; VBINeiGon24812_2193. DR KO; K02881; -. DR OMA; KSTRSHI; -. DR OrthoDB; EOG64NB48; -. DR BioCyc; NGON242231:GI2G-1724-MONOMER; -. DR Proteomes; UP000000535; 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_0000131306. SQ SEQUENCE 117 AA; 12798 MW; E1E329739EB3ED83 CRC64; MDKHTTRLRR ARKTRARIAD LKMVRLCVFR SNNHIYAQVI SAEGDKVLAQ ASTLEAEVRG SLKSGSNVEA AAIVGKRIAE KAKAAGVEKV AFDRSGFQYH GRVKALAEAA RENGLSF // ID RL19_NEIG1 Reviewed; 121 AA. AC Q5FA60; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=50S ribosomal protein L19 {ECO:0000255|HAMAP-Rule:MF_00402}; GN Name=rplS {ECO:0000255|HAMAP-Rule:MF_00402}; GN OrderedLocusNames=NGO0171; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW88927.1; -; Genomic_DNA. DR RefSeq; WP_002217809.1; NC_002946.2. DR RefSeq; YP_207339.1; NC_002946.2. DR ProteinModelPortal; Q5FA60; -. DR SMR; Q5FA60; 2-116. DR PRIDE; Q5FA60; -. DR EnsemblBacteria; AAW88927; AAW88927; NGO_0171. DR GeneID; 3281328; -. DR KEGG; ngo:NGO0171; -. DR PATRIC; 20333265; VBINeiGon24812_0215. DR HOGENOM; HOG000016264; -. DR KO; K02884; -. DR OMA; EAEQCAK; -. DR OrthoDB; EOG6DZF5W; -. DR BioCyc; NGON242231:GI2G-157-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 121 50S ribosomal protein L19. FT /FTId=PRO_0000226856. SQ SEQUENCE 121 AA; 13768 MW; 63E5A110F5F96E77 CRC64; MNLIQQLEQE EIARLNKEIP EFAPGDTVVV SVRVVEGTRS RLQAYEGVVI ARRNRGLNSN FIVRKISSGE GVERTFQLYS PTVEKIEVKR RGDVRRAKLY YLRGLTGKAA RIKEKLPARK G // ID RL22_NEIG1 Reviewed; 109 AA. AC Q5F5T2; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; GN OrderedLocusNames=NGO1833; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90455.1; -; Genomic_DNA. DR RefSeq; WP_002215424.1; NC_002946.2. DR RefSeq; YP_208867.1; NC_002946.2. DR ProteinModelPortal; Q5F5T2; -. DR SMR; Q5F5T2; 1-109. DR PRIDE; Q5F5T2; -. DR EnsemblBacteria; AAW90455; AAW90455; NGO_1833. DR GeneID; 3282436; -. DR KEGG; ngo:NGO1833; -. DR PATRIC; 20337338; VBINeiGon24812_2204. DR HOGENOM; HOG000205046; -. DR KO; K02890; -. DR OMA; MKRIQPR; -. DR OrthoDB; EOG6V4GKB; -. DR BioCyc; NGON242231:GI2G-1735-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 109 50S ribosomal protein L22. FT /FTId=PRO_0000243174. SQ SEQUENCE 109 AA; 11909 MW; 318AAFB9E515E7C2 CRC64; MRVNAQHKNA RISAQKARLV ADLIRGKDVA QALNILAFSP KKGAELIKKV LESAIANAEH NNGADIDELK VVTIFVDKGP SLKRFQARAK GRGNRIEKQT CHINVTVGN // ID RISB_NEIG1 Reviewed; 158 AA. AC Q5F9X9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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}; GN OrderedLocusNames=NGO0257; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89008.1; -; Genomic_DNA. DR RefSeq; WP_003687601.1; NC_002946.2. DR RefSeq; YP_207420.1; NC_002946.2. DR ProteinModelPortal; Q5F9X9; -. DR EnsemblBacteria; AAW89008; AAW89008; NGO_0257. DR GeneID; 3281556; -. DR KEGG; ngo:NGO0257; -. DR PATRIC; 20333471; VBINeiGon24812_0316. DR HOGENOM; HOG000229250; -. DR KO; K00794; -. DR OMA; SHVAMNS; -. DR OrthoDB; EOG6RC3WC; -. DR BioCyc; NGON242231:GI2G-240-MONOMER; -. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000000535; 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_1000040461. 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; 16968 MW; 0CA5502CB5690093 CRC64; MNTIAPNLDG KHLRIGIVQA RFTNEIGSQM LKVCCRTLQE LGVADENITV ATVPGALEIP IALMNFASSE KFDALIAIGV VIRGETYHFE LVANESGAGI GRVALDYNIP IANAVLTTEN DAQAIERIGE KASDAAKVAV ECANLVNLLL EEQFEDEE // ID RL14_NEIG1 Reviewed; 122 AA. AC Q5F5T7; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rplN {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=NGO1829; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90450.1; -; Genomic_DNA. DR RefSeq; WP_003690075.1; NC_002946.2. DR RefSeq; YP_208862.1; NC_002946.2. DR ProteinModelPortal; Q5F5T7; -. DR SMR; Q5F5T7; 2-122. DR EnsemblBacteria; AAW90450; AAW90450; NGO_1829. DR GeneID; 3282393; -. DR KEGG; ngo:NGO1829; -. DR PATRIC; 20337328; VBINeiGon24812_2199. DR HOGENOM; HOG000183702; -. DR KO; K02874; -. DR OMA; LRDKQFM; -. DR OrthoDB; EOG6GBMJ6; -. DR BioCyc; NGON242231:GI2G-1730-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 122 50S ribosomal protein L14. FT /FTId=PRO_0000266509. SQ SEQUENCE 122 AA; 13403 MW; 4CC72CA112E97891 CRC64; MIQMQTILDV ADNSGARRVM CIKVLGGSKR RYASVGDIIK VAVKDAVPRG RVKKGDVYNA VVVRTAKGVR RPDGALIKFD NNAAVLLNNK LEPLGTRIFG PVTRELRTER FMKIVSLAPE VL // ID RL23_NEIG1 Reviewed; 106 AA. AC Q5F5S9; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369}; GN Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=NGO1836; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90458.1; -; Genomic_DNA. DR RefSeq; WP_010951358.1; NC_002946.2. DR RefSeq; YP_208870.1; NC_002946.2. DR ProteinModelPortal; Q5F5S9; -. DR SMR; Q5F5S9; 3-94. DR EnsemblBacteria; AAW90458; AAW90458; NGO_1836. DR GeneID; 3282429; -. DR KEGG; ngo:NGO1836; -. DR PATRIC; 20337344; VBINeiGon24812_2207. DR HOGENOM; HOG000231364; -. DR KO; K02892; -. DR OMA; QISEKAT; -. DR OrthoDB; EOG6HTP4P; -. DR BioCyc; NGON242231:GI2G-1738-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 106 50S ribosomal protein L23. FT /FTId=PRO_0000272781. SQ SEQUENCE 106 AA; 11463 MW; 815E6F50AA0879CE CRC64; MGMNQQRLTQ VILVPVVSEK SNVLAEKCNQ MTFKVLANAT KPEIKAAVEL LFGVQVASVT TVTTKGKTKR FGRILGRRSD VKKAYVSLVD GQELDLEAAA AAADKE // ID RL28_NEIG1 Reviewed; 77 AA. AC Q5F682; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-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=NGO1680; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90305.1; -; Genomic_DNA. DR RefSeq; WP_002216391.1; NC_002946.2. DR RefSeq; YP_208717.1; NC_002946.2. DR ProteinModelPortal; Q5F682; -. DR SMR; Q5F682; 2-76. DR EnsemblBacteria; AAW90305; AAW90305; NGO_1680. DR GeneID; 25048560; -. DR GeneID; 3281200; -. DR KEGG; ngo:NGO1680; -. DR PATRIC; 20336918; VBINeiGon24812_2003. DR HOGENOM; HOG000040462; -. DR KO; K02902; -. DR OMA; WLPSERR; -. DR OrthoDB; EOG6W727M; -. DR BioCyc; NGON242231:GI2G-1575-MONOMER; -. DR Proteomes; UP000000535; 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_0000178514. SQ SEQUENCE 77 AA; 8818 MW; E3C08F654DF9871A CRC64; MARVCKVTGK RPMSGNNVSH ANNKTKRRFL PNLQSRRFWV ESENRWVRLR VSNAALRTID KVGIDVVLAD LRARGEA // ID RL24_NEIG1 Reviewed; 107 AA. AC Q5F5T8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=NGO1828; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90449.1; -; Genomic_DNA. DR RefSeq; WP_003690072.1; NC_002946.2. DR RefSeq; YP_208861.1; NC_002946.2. DR ProteinModelPortal; Q5F5T8; -. DR EnsemblBacteria; AAW90449; AAW90449; NGO_1828. DR GeneID; 3282433; -. DR KEGG; ngo:NGO1828; -. DR PATRIC; 20337326; VBINeiGon24812_2198. DR HOGENOM; HOG000039892; -. DR KO; K02895; -. DR OMA; NVNIVKR; -. DR OrthoDB; EOG6FFSDM; -. DR BioCyc; NGON242231:GI2G-1729-MONOMER; -. DR Proteomes; UP000000535; 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_0000241626. SQ SEQUENCE 107 AA; 11608 MW; E3AF59BF0A906423 CRC64; MNKIIKGDRV VVIAGKDKGK QGQVVRVLGG KVVVEGVNVV KRHQKPNPMR GIKGGIITKE MPLDISNIAI LNPETNKADR VGIKLIENEG KVKRVRFFKS NGSIIGA // ID RL25_NEIG1 Reviewed; 190 AA. AC Q5F9F4; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO0442; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89183.1; -; Genomic_DNA. DR RefSeq; WP_003687901.1; NC_002946.2. DR RefSeq; YP_207595.1; NC_002946.2. DR ProteinModelPortal; Q5F9F4; -. DR EnsemblBacteria; AAW89183; AAW89183; NGO_0442. DR GeneID; 3282298; -. DR KEGG; ngo:NGO0442; -. DR PATRIC; 20333910; VBINeiGon24812_0529. DR HOGENOM; HOG000214907; -. DR KO; K02897; -. DR OMA; CVLYGGD; -. DR OrthoDB; EOG6SZ1PC; -. DR BioCyc; NGON242231:GI2G-421-MONOMER; -. DR Proteomes; UP000000535; 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_0000181571. SQ SEQUENCE 190 AA; 20954 MW; DA86B23DAB20E438 CRC64; MTYEIQASVR EAQGTGASRR LRREGQIPGI LYGEGQEPVA IAVDHKTVFY ALEKESFHTA LIKLSLNGET KDVIVRDFQM HPFRREVQHI DFQAVKADQL VRIRVPLHIV NAENSQAVKL QGGRVSLLNT AVEVLALPAN IPAFLDLDCA EVVAGDILHL SDIKLPEGVE SVSLKRNENL AVATVTGKKR // ID RL29_NEIG1 Reviewed; 63 AA. AC Q5F5T5; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=50S ribosomal protein L29 {ECO:0000255|HAMAP-Rule:MF_00374}; GN Name=rpmC {ECO:0000255|HAMAP-Rule:MF_00374}; GN OrderedLocusNames=NGO1831; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L29P family. CC {ECO:0000255|HAMAP-Rule:MF_00374}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90452.1; -; Genomic_DNA. DR RefSeq; WP_002215432.1; NC_002946.2. DR RefSeq; YP_208864.1; NC_002946.2. DR ProteinModelPortal; Q5F5T5; -. DR EnsemblBacteria; AAW90452; AAW90452; NGO_1831. DR GeneID; 3282258; -. DR KEGG; ngo:NGO1831; -. DR PATRIC; 20337332; VBINeiGon24812_2201. DR HOGENOM; HOG000248754; -. DR KO; K02904; -. DR OMA; MRMQAST; -. DR OrthoDB; EOG6VTK8Z; -. DR BioCyc; NGON242231:GI2G-1732-MONOMER; -. DR Proteomes; UP000000535; 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_0000130425. SQ SEQUENCE 63 AA; 7078 MW; A7B1633418280B9B CRC64; MKANELKDKS VEQLNADLLD LLKAQFGLRM QNATGQLGKP SELKRVRRDI ARIKTVLTEK GAK // ID RL36_NEIG1 Reviewed; 41 AA. AC Q5F860; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE RecName: Full=50S ribosomal protein L36 {ECO:0000255|HAMAP-Rule:MF_00251}; GN Name=rpmJ {ECO:0000255|HAMAP-Rule:MF_00251}; GN OrderedLocusNames=NGO0931; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89627.1; -; Genomic_DNA. DR RefSeq; WP_003688377.1; NC_002946.2. DR RefSeq; YP_208039.1; NC_002946.2. DR ProteinModelPortal; Q5F860; -. DR EnsemblBacteria; AAW89627; AAW89627; NGO_0931. DR GeneID; 3282568; -. DR KEGG; ngo:NGO0931; -. DR PATRIC; 20335045; VBINeiGon24812_1092. DR HOGENOM; HOG000111585; -. DR KO; K02919; -. DR OrthoDB; EOG676ZC2; -. DR BioCyc; NGON242231:GI2G-869-MONOMER; -. DR Proteomes; UP000000535; 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. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 41 50S ribosomal protein L36. FT /FTId=PRO_0000302252. SQ SEQUENCE 41 AA; 4959 MW; BC026117293EAA31 CRC64; MQVLSSLKTA KQRHRDCQIV RRRGKVYVIC KSNPRFKSRQ R // ID RL1_NEIG1 Reviewed; 231 AA. AC Q5F5R2; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; GN OrderedLocusNames=NGO1854; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90475.1; -; Genomic_DNA. DR RefSeq; WP_003690110.1; NC_002946.2. DR RefSeq; YP_208887.1; NC_002946.2. DR ProteinModelPortal; Q5F5R2; -. DR SMR; Q5F5R2; 6-227. DR PRIDE; Q5F5R2; -. DR EnsemblBacteria; AAW90475; AAW90475; NGO_1854. DR GeneID; 3282369; -. DR KEGG; ngo:NGO1854; -. DR PATRIC; 20337388; VBINeiGon24812_2229. DR HOGENOM; HOG000207015; -. DR KO; K02863; -. DR OMA; NEGWTDF; -. DR OrthoDB; EOG6FBX2G; -. DR BioCyc; NGON242231:GI2G-1755-MONOMER; -. DR Proteomes; UP000000535; 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_0000230617. SQ SEQUENCE 231 AA; 24122 MW; CE8A16F25EC4A404 CRC64; MAKVSKRLKV LRSSVEANKL YAIDEAIALV KKAATAKFDE SVDVSFNLGV DSRKSDQVIR GSVVLPKGTG KTTRVAVFTQ GVNAEAAKEA GADVVGFEDL AAEIKAGNLN FDVVIASPDA MRIVGQLGTI LGPRGLMPNP KIGTVTPNVA EAVKNAKAGQ VQYRTDKAGI VHATIGRASF AEADLKENFD ALLDAIVKAK PAAAKGQYLK KVAVSSTMGL GVRVDTSSVN N // ID RL2_NEIG1 Reviewed; 277 AA. AC Q5F5T0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; GN OrderedLocusNames=NGO1835; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90457.1; -; Genomic_DNA. DR RefSeq; WP_003690083.1; NC_002946.2. DR RefSeq; YP_208869.1; NC_002946.2. DR ProteinModelPortal; Q5F5T0; -. DR SMR; Q5F5T0; 2-272. DR EnsemblBacteria; AAW90457; AAW90457; NGO_1835. DR GeneID; 3282423; -. DR KEGG; ngo:NGO1835; -. DR PATRIC; 20337342; VBINeiGon24812_2206. DR HOGENOM; HOG000232982; -. DR KO; K02886; -. DR OMA; HNRGVTM; -. DR OrthoDB; EOG6TR0J1; -. DR BioCyc; NGON242231:GI2G-1737-MONOMER; -. DR Proteomes; UP000000535; 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_0000237214. SQ SEQUENCE 277 AA; 30117 MW; 783A773394794987 CRC64; MAIVKMKPTS AGRRGMVRVV TEGLHKGAPY APLLEKKNST AGRNNNGHIT TRHKGGGHKH HYRVVDFKRN KDGISAKVER IEYDPNRTAF IALLCYADGE RRYIIAPRGI QAGVVLVSGA EAAIKVGNTL PIRNIPVGTT IHCIEMKPGK GAQIARSAGA SAVLLAKEGA YAQVRLRSGE VRKINVDCRA TIGEVGNEEQ SLKKIGKAGA NRWRGIRPTV RGVVMNPVDH PHGGGEGRTG EAREPVSPWG TPAKGYRTRN NKRTDNMIVR RRYSNKG // ID RL31B_NEIG1 Reviewed; 91 AA. AC Q5F861; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. 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=NGO0930; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89626.1; -; Genomic_DNA. DR RefSeq; WP_010951151.1; NC_002946.2. DR RefSeq; YP_208038.1; NC_002946.2. DR ProteinModelPortal; Q5F861; -. DR EnsemblBacteria; AAW89626; AAW89626; NGO_0930. DR GeneID; 3282614; -. DR KEGG; ngo:NGO0930; -. DR PATRIC; 20335043; VBINeiGon24812_1091. DR HOGENOM; HOG000284894; -. DR KO; K02909; -. DR OMA; YDASAQM; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; NGON242231:GI2G-868-MONOMER; -. DR Proteomes; UP000000535; 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_0000173238. SQ SEQUENCE 91 AA; 10425 MW; BD28932DF43BE3C2 CRC64; MKPNIHPDNY RTVLFFDSSA NEGWLIRSCA GTHGKTMVWT DGKEYLLFSL DTSSSSHPVY TGKQRNVNTE GRASKFNQRF QSVMSSFRKD K // ID RL33_NEIG1 Reviewed; 51 AA. AC Q5F683; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=50S ribosomal protein L33 {ECO:0000255|HAMAP-Rule:MF_00294}; GN Name=rpmG {ECO:0000255|HAMAP-Rule:MF_00294}; GN OrderedLocusNames=NGO1679; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L33P family. CC {ECO:0000255|HAMAP-Rule:MF_00294}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90304.1; -; Genomic_DNA. DR RefSeq; WP_003689824.1; NC_002946.2. DR RefSeq; YP_208716.1; NC_002946.2. DR ProteinModelPortal; Q5F683; -. DR SMR; Q5F683; 1-51. DR EnsemblBacteria; AAW90304; AAW90304; NGO_1679. DR GeneID; 3281231; -. DR KEGG; ngo:NGO1679; -. DR PATRIC; 20336916; VBINeiGon24812_2002. DR HOGENOM; HOG000004839; -. DR KO; K02913; -. DR OMA; ARKHVLY; -. DR OrthoDB; EOG60KNBM; -. DR BioCyc; NGON242231:GI2G-1574-MONOMER; -. DR Proteomes; UP000000535; 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_0000356581. SQ SEQUENCE 51 AA; 5907 MW; A991D01D6BB41701 CRC64; MRDKIKLESG AGTGHFYTTT KNKRTMPGKL EIKKFDPVAR KHVVYKETKL K // ID RL34_NEIG1 Reviewed; 44 AA. AC Q5F4W2; DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 55. DE RecName: Full=50S ribosomal protein L34 {ECO:0000255|HAMAP-Rule:MF_00391}; GN Name=rpmH {ECO:0000255|HAMAP-Rule:MF_00391}; GN OrderedLocusNames=NGO2182; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L34P family. CC {ECO:0000255|HAMAP-Rule:MF_00391}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90775.1; -; Genomic_DNA. DR RefSeq; WP_002214728.1; NC_002946.2. DR RefSeq; YP_209187.1; NC_002946.2. DR ProteinModelPortal; Q5F4W2; -. DR SMR; Q5F4W2; 1-44. DR EnsemblBacteria; AAW90775; AAW90775; NGO_2182. DR GeneID; 25048442; -. DR GeneID; 3282743; -. DR KEGG; ngo:NGO2182; -. DR PATRIC; 20338226; VBINeiGon24812_2635. DR HOGENOM; HOG000111572; -. DR KO; K02914; -. DR BioCyc; NGON242231:GI2G-2069-MONOMER; -. DR Proteomes; UP000000535; 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_0000187425. SQ SEQUENCE 44 AA; 5051 MW; 464395813C8808DA CRC64; MKRTYQPSVT KRKRTHGFLV RSKTRGGRAV LAARRAKGRK RLAV // ID RL4_NEIG1 Reviewed; 206 AA. AC Q5F5S8; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=NGO1837; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90459.1; -; Genomic_DNA. DR RefSeq; WP_003690088.1; NC_002946.2. DR RefSeq; YP_208871.1; NC_002946.2. DR ProteinModelPortal; Q5F5S8; -. DR SMR; Q5F5S8; 1-205. DR PRIDE; Q5F5S8; -. DR EnsemblBacteria; AAW90459; AAW90459; NGO_1837. DR GeneID; 3282415; -. DR KEGG; ngo:NGO1837; -. DR PATRIC; 20337346; VBINeiGon24812_2208. DR HOGENOM; HOG000248766; -. DR KO; K02926; -. DR OMA; VVRSHEH; -. DR OrthoDB; EOG6M0T9G; -. DR BioCyc; NGON242231:GI2G-1739-MONOMER; -. DR Proteomes; UP000000535; 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 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_0000242401. SQ SEQUENCE 206 AA; 23303 MW; 51A257365F6E569A CRC64; MELKVIDAKG QVSGSLSVSD ALFAREYNEA LVHQLVNAYL ANARSGNRAQ KTRAEVKHST KKPWRQKGTG RARSGMTSSP LWRKGGRAFP NKPDENFTQK VNRKMYRAGM ATILSQLARD ERLFVIEALT AETPKTKVFA EQVKNLALEQ VLFVTKRLDE NVYLASRNLP NVLVLEAQQV DPYSLLRYKK VIITKDAVAQ LEEQWV // ID RL20_NEIG1 Reviewed; 119 AA. AC Q5F9U1; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382}; GN Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; GN OrderedLocusNames=NGO0298; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89046.1; -; Genomic_DNA. DR RefSeq; WP_002214103.1; NC_002946.2. DR RefSeq; YP_207458.1; NC_002946.2. DR ProteinModelPortal; Q5F9U1; -. DR SMR; Q5F9U1; 3-117. DR PRIDE; Q5F9U1; -. DR EnsemblBacteria; AAW89046; AAW89046; NGO_0298. DR GeneID; 23782801; -. DR GeneID; 3281676; -. DR KEGG; ngo:NGO0298; -. DR PATRIC; 20333579; VBINeiGon24812_0369. DR HOGENOM; HOG000035046; -. DR KO; K02887; -. DR OMA; WIRNRGP; -. DR OrthoDB; EOG6CGCMB; -. DR BioCyc; NGON242231:GI2G-279-MONOMER; -. DR Proteomes; UP000000535; 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_0000243704. SQ SEQUENCE 119 AA; 13680 MW; 9B9859BB5550D650 CRC64; MPRVKRGVTA RARHQKIFAL AKGYRGRRKN VYRVAKQAVM KAGQYAYRDR RQRKRQFRQL WIVRINAGAR ENGLSYSKFM NGLKRASIEI DRKVLADLAV FDKAAFAQLV EKAKAALAA // ID RL30_NEIG1 Reviewed; 61 AA. AC Q5F5U5; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=50S ribosomal protein L30 {ECO:0000255|HAMAP-Rule:MF_01371}; GN Name=rpmD {ECO:0000255|HAMAP-Rule:MF_01371}; GN OrderedLocusNames=NGO1823.1; ORFNames=NGO18231; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90442.1; -; Genomic_DNA. DR RefSeq; WP_003690310.1; NC_002946.2. DR RefSeq; YP_208854.1; NC_002946.2. DR ProteinModelPortal; Q5F5U5; -. DR SMR; Q5F5U5; 5-61. DR EnsemblBacteria; AAW90442; AAW90442; NGO_18231. DR GeneID; 3282396; -. DR KEGG; ngo:NGO18231; -. DR PATRIC; 20337312; VBINeiGon24812_2191. DR HOGENOM; HOG000039916; -. DR KO; K02907; -. DR OMA; GMIQKVS; -. DR OrthoDB; EOG6BGP7P; -. DR BioCyc; NGON242231:GI2G-1722-MONOMER; -. DR Proteomes; UP000000535; 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_0000273810. SQ SEQUENCE 61 AA; 6936 MW; CB7B5D4D00DBEE32 CRC64; MAEQKKIRVT LVKSLIGTIE SHRACARGLG LRRREHTVEV LDTSENRGMI NKISYLLKVE S // ID RL7_NEIG1 Reviewed; 123 AA. AC Q5F5R4; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. 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=NGO1852; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90473.1; -; Genomic_DNA. DR RefSeq; WP_003690106.1; NC_002946.2. DR RefSeq; YP_208885.1; NC_002946.2. DR ProteinModelPortal; Q5F5R4; -. DR SMR; Q5F5R4; 3-123. DR PRIDE; Q5F5R4; -. DR EnsemblBacteria; AAW90473; AAW90473; NGO_1852. DR GeneID; 3282399; -. DR KEGG; ngo:NGO1852; -. DR PATRIC; 20337384; VBINeiGon24812_2227. DR HOGENOM; HOG000248813; -. DR KO; K02935; -. DR OMA; GLKETWG; -. DR OrthoDB; EOG6WMJ69; -. DR BioCyc; NGON242231:GI2G-1753-MONOMER; -. DR Proteomes; UP000000535; 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 CHAIN 1 123 50S ribosomal protein L7/L12. FT /FTId=PRO_0000243450. SQ SEQUENCE 123 AA; 12564 MW; 5F7207CA5CB6F535 CRC64; MAITKEDILE AVGSLTVMEL NDLVKAFEEK FGVSAAAVAV AGPAGAGAAD AEEKTEFDVV LASAGDQKVG VIKVVRAITG LGLKEAKDIV DGAPKTIKEG VSKAEAEDIQ KQLEAAGAKV EIK // ID RL21_NEIG1 Reviewed; 102 AA. AC Q5F686; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=50S ribosomal protein L21 {ECO:0000255|HAMAP-Rule:MF_01363}; GN Name=rplU {ECO:0000255|HAMAP-Rule:MF_01363}; GN OrderedLocusNames=NGO1676; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90301.1; -; Genomic_DNA. DR RefSeq; WP_003691838.1; NC_002946.2. DR RefSeq; YP_208713.1; NC_002946.2. DR ProteinModelPortal; Q5F686; -. DR EnsemblBacteria; AAW90301; AAW90301; NGO_1676. DR GeneID; 3281255; -. DR KEGG; ngo:NGO1676; -. DR PATRIC; 20336908; VBINeiGon24812_1998. DR HOGENOM; HOG000036265; -. DR KO; K02888; -. DR OMA; QGHRQPF; -. DR OrthoDB; EOG6TJ84X; -. DR BioCyc; NGON242231:GI2G-1571-MONOMER; -. DR Proteomes; UP000000535; 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_0000269347. SQ SEQUENCE 102 AA; 11447 MW; 26843557323AADE8 CRC64; MYAVVKTGGK QYKVSVGEKL KVEQIPAQLD SQIELTEVLM IADGESVKVG APFIEGAKVT AKVVAHGRGE KVRIFKMRRR KHYQKRQGHR QNFTQIEIVA IA // ID RL27_NEIG1 Reviewed; 90 AA. AC Q5F685; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=50S ribosomal protein L27 {ECO:0000255|HAMAP-Rule:MF_00539}; GN Name=rpmA {ECO:0000255|HAMAP-Rule:MF_00539}; GN OrderedLocusNames=NGO1677; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90302.1; -; Genomic_DNA. DR RefSeq; WP_003689821.1; NC_002946.2. DR RefSeq; YP_208714.1; NC_002946.2. DR ProteinModelPortal; Q5F685; -. DR SMR; Q5F685; 2-82. DR PRIDE; Q5F685; -. DR EnsemblBacteria; AAW90302; AAW90302; NGO_1677. DR GeneID; 3281215; -. DR KEGG; ngo:NGO1677; -. DR PATRIC; 20336910; VBINeiGon24812_1999. DR HOGENOM; HOG000111610; -. DR KO; K02899; -. DR OMA; NGRNNKK; -. DR OrthoDB; EOG6N94H6; -. DR BioCyc; NGON242231:GI2G-1572-MONOMER; -. DR Proteomes; UP000000535; 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 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_0000181131. SQ SEQUENCE 90 AA; 9699 MW; 0A919D6F59718295 CRC64; MASKKAGGST RNGRDSEAKR LGVKAYGNEL IPAGSIIVRQ RGTKFHAGDN VGMGKDHTLF AKIDGYVEFK TKGALNRKTV SIRPYTGSEE // ID RL35_NEIG1 Reviewed; 65 AA. AC Q5F9U2; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, 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=NGO0297; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89045.1; -; Genomic_DNA. DR RefSeq; WP_002232040.1; NC_002946.2. DR RefSeq; YP_207457.1; NC_002946.2. DR ProteinModelPortal; Q5F9U2; -. DR SMR; Q5F9U2; 2-65. DR EnsemblBacteria; AAW89045; AAW89045; NGO_0297. DR GeneID; 23782750; -. DR GeneID; 3281658; -. DR KEGG; ngo:NGO0297; -. DR PATRIC; 20333577; VBINeiGon24812_0368. DR HOGENOM; HOG000040108; -. DR KO; K02916; -. DR OMA; AYKRHIL; -. DR OrthoDB; EOG651T3B; -. DR BioCyc; NGON242231:GI2G-278-MONOMER; -. DR Proteomes; UP000000535; 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_0000258711. SQ SEQUENCE 65 AA; 7357 MW; EF7E775093C90473 CRC64; MPKMKTKSSA KKRFKVLGNG GVKRAHAFKR HILTKKTTKN KRQLRGTSMV NDRDLASVAK MLPYA // ID RL3_NEIG1 Reviewed; 214 AA. AC Q5F5S7; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-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=NGO1838; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90460.1; -; Genomic_DNA. DR RefSeq; WP_002215400.1; NC_002946.2. DR RefSeq; YP_208872.1; NC_002946.2. DR ProteinModelPortal; Q5F5S7; -. DR SMR; Q5F5S7; 3-211. DR PRIDE; Q5F5S7; -. DR EnsemblBacteria; AAW90460; AAW90460; NGO_1838. DR GeneID; 3282421; -. DR KEGG; ngo:NGO1838; -. DR PATRIC; 20337348; VBINeiGon24812_2209. DR HOGENOM; HOG000100368; -. DR KO; K02906; -. DR OMA; NVVMIKG; -. DR OrthoDB; EOG6WDSMH; -. DR BioCyc; NGON242231:GI2G-1740-MONOMER; -. DR Proteomes; UP000000535; 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_0000241374. 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 RL6_NEIG1 Reviewed; 177 AA. AC Q5F5U2; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; GN OrderedLocusNames=NGO1825; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW90445.1; -; Genomic_DNA. DR RefSeq; WP_010951357.1; NC_002946.2. DR RefSeq; YP_208857.1; NC_002946.2. DR ProteinModelPortal; Q5F5U2; -. DR SMR; Q5F5U2; 2-177. DR EnsemblBacteria; AAW90445; AAW90445; NGO_1825. DR GeneID; 3282450; -. DR KEGG; ngo:NGO1825; -. DR PATRIC; 20337318; VBINeiGon24812_2194. DR HOGENOM; HOG000039903; -. DR KO; K02933; -. DR OMA; TIGYSHP; -. DR OrthoDB; EOG67DPRD; -. DR BioCyc; NGON242231:GI2G-1725-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 177 50S ribosomal protein L6. FT /FTId=PRO_0000260899. SQ SEQUENCE 177 AA; 18940 MW; 83F4EB72BCC115AC CRC64; MSRVAKNPVT VPAGVEVKFG TEALVIKGKN GELSFPLHSD VAIEFNDGKL TFVANNSSKQ ANAMSGTARA LVSNMVKGVS EGFEKKLQLM GVGYRAQAQG KILNLSLGFS HPIVYEMPEG VSVQTPSQTE IVLTGSDKQV VGQVASEIRA FRAPEPYKGK GVRYVGEVVV MKEAKKK // ID RLMH_NEIG1 Reviewed; 156 AA. AC Q5F554; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO2082; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90683.1; -; Genomic_DNA. DR RefSeq; WP_003687038.1; NC_002946.2. DR RefSeq; YP_209095.1; NC_002946.2. DR ProteinModelPortal; Q5F554; -. DR EnsemblBacteria; AAW90683; AAW90683; NGO_2082. DR GeneID; 3282835; -. DR KEGG; ngo:NGO2082; -. DR PATRIC; 20337997; VBINeiGon24812_2521. DR HOGENOM; HOG000218434; -. DR KO; K00783; -. DR OMA; NGEPYHK; -. DR OrthoDB; EOG6S26HR; -. DR BioCyc; NGON242231:GI2G-1977-MONOMER; -. DR Proteomes; UP000000535; 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_0000198149. SQ SEQUENCE 156 AA; 17510 MW; 97488B9B289D9853 CRC64; MNITVLAVGT KMPRWVDEAV AEYAKRFGRD AAYAFKEIKP EKRGAGVNAV QGMAAEEKRI LEAIPQGAFL VVLDERGKAP TSVELAEHLK SWRQNGEHVC FVIGGADGMT DRLKQQARMM MRLSSLTLPH GMVRVLLTEQ LYRAVSILHN HPYHRE // ID RLME_NEIG1 Reviewed; 206 AA. AC Q5F9L0; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO0383; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89127.1; -; Genomic_DNA. DR RefSeq; WP_003698155.1; NC_002946.2. DR RefSeq; YP_207539.1; NC_002946.2. DR ProteinModelPortal; Q5F9L0; -. DR EnsemblBacteria; AAW89127; AAW89127; NGO_0383. DR GeneID; 3282537; -. DR KEGG; ngo:NGO0383; -. DR PATRIC; 20333771; VBINeiGon24812_0463. DR HOGENOM; HOG000162367; -. DR KO; K02427; -. DR OMA; ERQINDP; -. DR OrthoDB; EOG657JC0; -. DR BioCyc; NGON242231:GI2G-362-MONOMER; -. DR Proteomes; UP000000535; 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_0000155511. 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; 22726 MW; D48694E0D2C63718 CRC64; MAVRSKSSKA WLHEHINDQY VHMAQKDGYR ARAAYKLLEI NEKDKIIKPG TVLADLGSAP GSWSQVAAKL TGTSGAVFAL DILPMEAIGG VSFIQGDFRE NDVLAQFETL LDNRPLDLVI CDMAPNMSGN AVSDQARSFY LCELALDFAS QHLKTGGSFL VKVFQGAGYQ EYMAAMREIF GTVQTRKPEA SRNRSSEIYL LGKNKR // ID RL31_NEIG1 Reviewed; 71 AA. AC Q5F513; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=50S ribosomal protein L31 {ECO:0000255|HAMAP-Rule:MF_00501}; GN Name=rpmE {ECO:0000255|HAMAP-Rule:MF_00501}; GN OrderedLocusNames=NGO2126; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90724.1; -; Genomic_DNA. DR RefSeq; WP_010356285.1; NC_002946.2. DR RefSeq; YP_209136.1; NC_002946.2. DR ProteinModelPortal; Q5F513; -. DR EnsemblBacteria; AAW90724; AAW90724; NGO_2126. DR GeneID; 3282794; -. DR KEGG; ngo:NGO2126; -. DR PATRIC; 20338101; VBINeiGon24812_2573. DR HOGENOM; HOG000284895; -. DR KO; K02909; -. DR OMA; VETCSEC; -. DR OrthoDB; EOG6DVJZM; -. DR BioCyc; NGON242231:GI2G-2018-MONOMER; -. DR Proteomes; UP000000535; 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_0000173134. 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; 8165 MW; 55FB4ADC137D88CC CRC64; MKQGIHPNYR EVNVTCSCGN KFVTKSAMEK ENFNIEVCSL CHPFYTGTQK IVDTTGRVDK FNNKFGNLFK R // ID RL32_NEIG1 Reviewed; 59 AA. AC Q5F4X1; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE RecName: Full=50S ribosomal protein L32 {ECO:0000255|HAMAP-Rule:MF_00340}; GN Name=rpmF {ECO:0000255|HAMAP-Rule:MF_00340}; GN OrderedLocusNames=NGO2173; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L32P family. CC {ECO:0000255|HAMAP-Rule:MF_00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90766.1; -; Genomic_DNA. DR RefSeq; WP_003687186.1; NC_002946.2. DR RefSeq; YP_209178.1; NC_002946.2. DR ProteinModelPortal; Q5F4X1; -. DR SMR; Q5F4X1; 2-54. DR EnsemblBacteria; AAW90766; AAW90766; NGO_2173. DR GeneID; 3282752; -. DR KEGG; ngo:NGO2173; -. DR PATRIC; 20338210; VBINeiGon24812_2627. DR HOGENOM; HOG000040269; -. DR KO; K02911; -. DR OMA; HRAHDFL; -. DR OrthoDB; EOG6VMTT4; -. DR BioCyc; NGON242231:GI2G-2060-MONOMER; -. DR Proteomes; UP000000535; 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 CHAIN 1 59 50S ribosomal protein L32. FT /FTId=PRO_0000225742. SQ SEQUENCE 59 AA; 6533 MW; D2D71A906CD631F5 CRC64; MAVQQNKKSP SKRGMHRSHD ALTAPALFVD STTGEVHRPH HISPNGMYRG RKVVKAKGE // ID RL5_NEIG1 Reviewed; 179 AA. AC Q5F5T9; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rplE {ECO:0000255|HAMAP-Rule:MF_01333}; GN OrderedLocusNames=NGO1827; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90448.1; -; Genomic_DNA. DR RefSeq; WP_003690070.1; NC_002946.2. DR RefSeq; YP_208860.1; NC_002946.2. DR ProteinModelPortal; Q5F5T9; -. DR SMR; Q5F5T9; 2-178. DR EnsemblBacteria; AAW90448; AAW90448; NGO_1827. DR GeneID; 3282434; -. DR KEGG; ngo:NGO1827; -. DR PATRIC; 20337324; VBINeiGon24812_2197. DR HOGENOM; HOG000231311; -. DR KO; K02931; -. DR OMA; EQVMFHE; -. DR OrthoDB; EOG6M9F1R; -. DR BioCyc; NGON242231:GI2G-1728-MONOMER; -. DR Proteomes; UP000000535; 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_0000243027. SQ SEQUENCE 179 AA; 20379 MW; 3BD66654C1645899 CRC64; MARLREFYKE TVVPELVKQF GYKSVMEVPR IEKITLNMGV GEAVADKKVM EHAVSDLERI AGQRPVVTVA RKSIAGFKIR DNYPVGCKVT LRRDQMFEFL DRLITIALPR VRDFRGVSGK SFDGRGNYNM GVREQIIFPE IEYDKIDALR GLNITITTTA KTDEEAKALL SLFKFPFKG // ID RL9_NEIG1 Reviewed; 150 AA. AC Q5F922; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503}; GN Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503}; GN OrderedLocusNames=NGO0584; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89315.1; -; Genomic_DNA. DR RefSeq; WP_002232586.1; NC_002946.2. DR RefSeq; YP_207727.1; NC_002946.2. DR ProteinModelPortal; Q5F922; -. DR PRIDE; Q5F922; -. DR EnsemblBacteria; AAW89315; AAW89315; NGO_0584. DR GeneID; 3282246; -. DR KEGG; ngo:NGO0584; -. DR PATRIC; 20334236; VBINeiGon24812_0690. DR HOGENOM; HOG000040337; -. DR KO; K02939; -. DR OMA; AIRWTKG; -. DR OrthoDB; EOG6D8BH0; -. DR BioCyc; NGON242231:GI2G-555-MONOMER; -. DR Proteomes; UP000000535; 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_0000236548. SQ SEQUENCE 150 AA; 15703 MW; 799F82BFDD514C86 CRC64; MQIILLEKIG GLGNLGDIVT VKNGYARNFL IPAGKAKRAT EANMKEFEAR RAELEAKQAE ILADARARQE KLDGQTVTVA QKAGVDGRLF GSVTNADIAA AIVAAGIEAV KANVRLPNGP LKAVGEYEVE VALHTDAVAK ITVAVIAAAE // ID RNC_NEIG1 Reviewed; 239 AA. AC Q5F9X7; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO0259; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89010.1; -; Genomic_DNA. DR RefSeq; WP_010951018.1; NC_002946.2. DR RefSeq; YP_207422.1; NC_002946.2. DR ProteinModelPortal; Q5F9X7; -. DR EnsemblBacteria; AAW89010; AAW89010; NGO_0259. DR GeneID; 3281574; -. DR KEGG; ngo:NGO0259; -. DR PATRIC; 20333477; VBINeiGon24812_0319. DR HOGENOM; HOG000246809; -. DR KO; K03685; -. DR OMA; LTHKSCK; -. DR OrthoDB; EOG6T1WVS; -. DR BioCyc; NGON242231:GI2G-242-MONOMER; -. DR Proteomes; UP000000535; 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_0000228553. 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; 26948 MW; 5E3473B8FA9F899D CRC64; MKDDVLKRQA HTAIQKKLGY AFRDMSLLRR ALTHRSHHAK HNERFEFVGD SILNYTVARM LFDAFPKLTE GELSRLRASL VNEGVLAEMA AEMNVGDGLY LGAGELKSSG FRRPSILADA MEAMFAAVSF DADFNTAEKV VRHLFAERVR RADFQNQAKD GKTALQEALQ ARRFALPKYR IEEQIGHADD SMFVISCDLG ELGFVCRAKG TSRKAAEQEA AKEALKWLEE KLPLKKKKK // ID RNH2_NEIG1 Reviewed; 194 AA. AC Q5F5X9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Ribonuclease HII {ECO:0000255|HAMAP-Rule:MF_00052}; DE Short=RNase HII {ECO:0000255|HAMAP-Rule:MF_00052}; DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_00052}; GN Name=rnhB {ECO:0000255|HAMAP-Rule:MF_00052}; GN OrderedLocusNames=NGO1789; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. {ECO:0000255|HAMAP-Rule:MF_00052}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_00052}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00052}; 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:0000255|HAMAP-Rule:MF_00052}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00052}. CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000255|HAMAP- CC Rule:MF_00052}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90408.1; -; Genomic_DNA. DR RefSeq; WP_010359364.1; NC_002946.2. DR RefSeq; YP_208820.1; NC_002946.2. DR ProteinModelPortal; Q5F5X9; -. DR EnsemblBacteria; AAW90408; AAW90408; NGO_1789. DR GeneID; 3282466; -. DR KEGG; ngo:NGO1789; -. DR PATRIC; 20337222; VBINeiGon24812_2147. DR HOGENOM; HOG000100288; -. DR KO; K03470; -. DR OMA; LSWAYLD; -. DR OrthoDB; EOG6BKJC8; -. DR BioCyc; NGON242231:GI2G-1687-MONOMER; -. DR Proteomes; UP000000535; 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_0000111593. FT METAL 9 9 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00052}. FT METAL 10 10 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00052}. FT METAL 101 101 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00052}. SQ SEQUENCE 194 AA; 21175 MW; D5DB8376BD1EA1F5 CRC64; MHILTAGVDE AGRGPLVGSV FAAAVILPET FDLPGLTDSK KLSEKKRDAL AEMIKEQAVA WHVAASTPEE IASLNILHAT MLAMKRAVYG LAARPEKIFI DGNRIPEHLG IPAEAVVKGD SKIIEISAAS VLAKTARDAE MYALAQRRPQ YGFDKHKGYG TKQHLEALKQ YGVLPEHRRD FAPVRNLLAQ QALF // ID RNH_NEIG1 Reviewed; 145 AA. AC Q5F7K9; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_00042}; DE Short=RNase H {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=NGO1162; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89828.1; -; Genomic_DNA. DR RefSeq; WP_003689763.1; NC_002946.2. DR RefSeq; YP_208240.1; NC_002946.2. DR ProteinModelPortal; Q5F7K9; -. DR SMR; Q5F7K9; 5-141. DR EnsemblBacteria; AAW89828; AAW89828; NGO_1162. DR GeneID; 3282266; -. DR KEGG; ngo:NGO1162; -. DR PATRIC; 20335595; VBINeiGon24812_1361. DR HOGENOM; HOG000040465; -. DR KO; K03469; -. DR OMA; LVTDSQY; -. DR OrthoDB; EOG696BTR; -. DR BioCyc; NGON242231:GI2G-1075-MONOMER; -. DR Proteomes; UP000000535; 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 H. FT /FTId=PRO_0000195383. 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; 16196 MW; 985EAC0357B23C5B CRC64; MDTPVYLYTD GACKGNPGAG GWGVLMRYGS REKELFGGEA QTTNNRMELT AVIEGLKSLK RRCTVIICTD SQYVKNGMEN WIHGWKRNGW KTAAKQPVKN DDLWQELDAL VGQHQVSWTW VKGHAGHAEN ERADDLANRG AAQFS // ID RPOA_NEIG1 Reviewed; 328 AA. AC Q5F5V2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO1818; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90435.1; -; Genomic_DNA. DR RefSeq; WP_003690059.1; NC_002946.2. DR RefSeq; YP_208847.1; NC_002946.2. DR ProteinModelPortal; Q5F5V2; -. DR SMR; Q5F5V2; 2-230, 249-325. DR PRIDE; Q5F5V2; -. DR EnsemblBacteria; AAW90435; AAW90435; NGO_1818. DR GeneID; 3282252; -. DR KEGG; ngo:NGO1818; -. DR PATRIC; 20337296; VBINeiGon24812_2183. DR HOGENOM; HOG000218481; -. DR KO; K03040; -. DR OMA; LMKFRNF; -. DR OrthoDB; EOG68WR84; -. DR BioCyc; NGON242231:GI2G-1715-MONOMER; -. DR Proteomes; UP000000535; 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_0000225283. 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; 36001 MW; 0AB5CAFABBFFC403 CRC64; MQNSTTEFLK PRQIDVNTFS ATRAKVSMQP FERGFGHTLG NALRRILLSS MNGFAPTEVA IAGVLHEYST VGGVQEDVVD ILLNIKGIVF KLHGRSQVQL VLKKSGSGVV SAGDIELPHD VEILNPGHVI CHLADNGQIE MEIKVEQGRG YQSVSGRQVV RDENRQIGAI QLDASFSPIS RVSFEVEPAR VEQRTDLDKL VLDIETDGSI DPEEAVRSAA RILIDQMSIF ADLQGTPVEE VEEKSPPIDP VLLHPVDDLE LTVRSANCLK AEDIYYIGDL IQRTETELLK TPNLGRKSLN EIKEVLASKG LTLGSKLEAW PPVGLEKP // ID RNFH_NEIG1 Reviewed; 92 AA. AC Q5F9L3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE RecName: Full=Protein RnfH {ECO:0000255|HAMAP-Rule:MF_00460}; GN Name=rnfH {ECO:0000255|HAMAP-Rule:MF_00460}; GN OrderedLocusNames=NGO0380; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0125 (RnfH) family. CC {ECO:0000255|HAMAP-Rule:MF_00460}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89124.1; -; Genomic_DNA. DR RefSeq; WP_003687804.1; NC_002946.2. DR RefSeq; YP_207536.1; NC_002946.2. DR ProteinModelPortal; Q5F9L3; -. DR EnsemblBacteria; AAW89124; AAW89124; NGO_0380. DR GeneID; 3282112; -. DR KEGG; ngo:NGO0380; -. DR PATRIC; 20333765; VBINeiGon24812_0460. DR HOGENOM; HOG000261719; -. DR KO; K09801; -. DR OMA; GRINKIT; -. DR OrthoDB; EOG6Q8J4M; -. DR BioCyc; NGON242231:GI2G-359-MONOMER; -. DR Proteomes; UP000000535; 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 Protein RnfH. FT /FTId=PRO_1000013582. SQ SEQUENCE 92 AA; 10373 MW; 261EF4CFE21D464A CRC64; MLEIEIVYGL PDRQVLKTMQ LAEGTTVRTA ALQSGLDGIF ENLNLHSAPL GIFGKAVKDD TPLRDGDRIE VYRPLLIDPK EARRKRVQNQ EE // ID RNPH_NEIG1 Reviewed; 242 AA. AC Q5F840; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO0958; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89647.1; -; Genomic_DNA. DR RefSeq; WP_003688342.1; NC_002946.2. DR RefSeq; YP_208059.1; NC_002946.2. DR ProteinModelPortal; Q5F840; -. DR SMR; Q5F840; 7-240. DR EnsemblBacteria; AAW89647; AAW89647; NGO_0958. DR GeneID; 3282178; -. DR KEGG; ngo:NGO0958; -. DR PATRIC; 20335102; VBINeiGon24812_1120. DR HOGENOM; HOG000229516; -. DR KO; K00989; -. DR OMA; KGKGQGW; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NGON242231:GI2G-889-MONOMER; -. DR Proteomes; UP000000535; 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_1000024838. SQ SEQUENCE 242 AA; 25646 MW; D9989475EB823800 CRC64; MPDYIRTSRA ADSLRDIKIT PHFLPHTDGS CLIECGNTKV ICTASVDENA PPFLHGKNQG WVTAEYGMLP ASTALRMRRE ASAGKQSGRT QEIQRLIGRS LRAVVDMEKL GERQILIDCD VIQADGGTRT ASITGAFVAL QIAVGKLVSD GILSENPILE AVAAVSAGVV NGVPLLDLDY PEDSGCDSDV NIVMTASGKI IEIQGTAEGA PFSLDELGKL VALAQKGIGE LLRYQQNALS VA // ID RLMN_NEIG1 Reviewed; 364 AA. AC Q5F911; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO0596; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89326.1; -; Genomic_DNA. DR RefSeq; WP_003688948.1; NC_002946.2. DR RefSeq; YP_207738.1; NC_002946.2. DR ProteinModelPortal; Q5F911; -. DR EnsemblBacteria; AAW89326; AAW89326; NGO_0596. DR GeneID; 3281098; -. DR KEGG; ngo:NGO0596; -. DR PATRIC; 20334266; VBINeiGon24812_0705. DR HOGENOM; HOG000217992; -. DR KO; K06941; -. DR OMA; IYHFGVS; -. DR OrthoDB; EOG6DJZ2N; -. DR BioCyc; NGON242231:GI2G-566-MONOMER; -. DR Proteomes; UP000000535; 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_0000350276. 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; 41072 MW; F24758D71493199D CRC64; MKTNLLNYDL QGLTRHFADM GEKPFRAKQV MRWMHQSGAQ NFDEMTDLAK SLRHKLNEQA SIEIPKLMMS QESSDGTRKW LLDVGTGNGV ETVFIPESDR GTLCISSQVG CALECTFCST GRQGFNRNLT AAEIIGQLWW ANKAMGVTPK NERVISNVVM MGMGEPMANF DNVVTALSIM LDDHGYGLSR RRVTVSTSGM VPQMDRLRDV MPVALAVSLH ASNDEVRNQI VPLNKKYPLK ELMAACQRYL VKAPRDFITF EYVMLDGVND KAQHAYELIE LVKDVPCKFN LIPFNPFPNS GYERSSNENI RIFRDILQQA EFVVTVRKTR GDDIDAACGQ LAGQVQDKTR RQQKWQQILI GQQG // ID RPOZ_NEIG1 Reviewed; 68 AA. AC Q5F776; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=DNA-directed RNA polymerase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366}; DE Short=RNAP omega subunit {ECO:0000255|HAMAP-Rule:MF_00366}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00366}; DE AltName: Full=RNA polymerase omega subunit {ECO:0000255|HAMAP-Rule:MF_00366}; DE AltName: Full=Transcriptase subunit omega {ECO:0000255|HAMAP-Rule:MF_00366}; GN Name=rpoZ {ECO:0000255|HAMAP-Rule:MF_00366}; GN OrderedLocusNames=NGO1309; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000255|HAMAP- CC Rule:MF_00366}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00366}. 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_00366}. CC -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family. CC {ECO:0000255|HAMAP-Rule:MF_00366}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89961.1; -; Genomic_DNA. DR RefSeq; WP_002212665.1; NC_002946.2. DR RefSeq; YP_208373.1; NC_002946.2. DR EnsemblBacteria; AAW89961; AAW89961; NGO_1309. DR GeneID; 3281864; -. DR KEGG; ngo:NGO1309; -. DR PATRIC; 20335979; VBINeiGon24812_1540. DR HOGENOM; HOG000245721; -. DR KO; K03060; -. DR OMA; CLKRIPN; -. DR OrthoDB; EOG6Q5NV5; -. DR BioCyc; NGON242231:GI2G-1224-MONOMER; -. DR Proteomes; UP000000535; 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_0000237477. SQ SEQUENCE 68 AA; 7500 MW; D317176466D0D1D9 CRC64; MARITTEDCT GKISNHFDLT LVAARRARQL ENGNTPLVDD VRNNKPTVTA LREIAAGHIG TELLTRNK // ID RPOB_NEIG1 Reviewed; 1392 AA. AC Q5F5R5; DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO1851; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90472.1; -; Genomic_DNA. DR RefSeq; WP_003705329.1; NC_002946.2. DR RefSeq; YP_208884.1; NC_002946.2. DR ProteinModelPortal; Q5F5R5; -. DR PRIDE; Q5F5R5; -. DR EnsemblBacteria; AAW90472; AAW90472; NGO_1851. DR GeneID; 3282372; -. DR KEGG; ngo:NGO1851; -. DR PATRIC; 20337382; VBINeiGon24812_2226. DR HOGENOM; HOG000218612; -. DR KO; K03043; -. DR OMA; YFNPKRY; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; NGON242231:GI2G-1752-MONOMER; -. DR Proteomes; UP000000535; 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: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 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_0000224081. SQ SEQUENCE 1392 AA; 155749 MW; D0ABA85EFC2C2F8C CRC64; MNYSFTEKKR IRKSFAKREN VLEVPFLLAT QIDSYAKFLQ LENAFDKRTD DGLQAAFNSI FPIVSHNGYA RLEFVYYTLG EPLFDIPECQ LRGITYAAPL RARIRLVILD KEASKPTVKE VRENEVYMGE IPLMTPSGSF VINGTERVIV SQLHRSPGVF FEHDKGKTHS SGKLLFSARI IPYRGSWLDF EFDPKDLLYF RIDRRRKMPV TILLKALGYN NEQILDIFYD KETFYLSSNG VQTDLVAGRL KGETAKVDIL DKEGNVLVAK GKRITAKNIR DITNAGLTRL DVEQESLLGK 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 ADGASTDLGE LALGQNMTIA FMPWNGYNYE DSILISEKVA ADDRYTSIHI EELNVVARDT KLGAEDITRD IPNLSERMQN RLDESGIVYI GAEVEAGDVL VGKVTPKGET QLTPEEKLLR AIFGEKASDV KDTSLRMPTG MSGTVIDVQV FTREGIQRDK RAQSIIDSEL KRYRLDLNDQ LRIFDNDAFD RIERMIVGQK ANGGPMKLTK GSEITTEYLA GLPSRHDWFD IRLTDEDLAK QLELIKLSLQ QKREEADELY EIKKKKLTQG DELQPGVQKM VKVFIAIKRR LQAGDKMAGR HGNKGVVSRI LPVEDMPYMA DGRPVDIVLN PLGVPSRMNI GQILEVHLGW AAKGIGERID RMLKERRKAG ELREFLNKLY NGSGKKEDLD SLTDEEIIEL ASNLRKGASF ASPVFDGAKE SEIREMLNLA YPSEDPEVEK LGFNDSKTQI TLYDGRSGEA FDRKVTVGVM HYLKLHHLVD EKMHARSTGP YSLVTQQPLG GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYENIVK GEHKIDAGMP ESFNVLVKEI RSLGLDIDLE RY // ID RNPA_NEIG1 Reviewed; 121 AA. AC Q5F4W3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO2181; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90774.1; -; Genomic_DNA. DR RefSeq; WP_003687193.1; NC_002946.2. DR RefSeq; YP_209186.1; NC_002946.2. DR ProteinModelPortal; Q5F4W3; -. DR EnsemblBacteria; AAW90774; AAW90774; NGO_2181. DR GeneID; 3282744; -. DR KEGG; ngo:NGO2181; -. DR PATRIC; 20338224; VBINeiGon24812_2634. DR HOGENOM; HOG000266301; -. DR KO; K03536; -. DR OMA; SVFNFRK; -. DR OrthoDB; EOG6S52QN; -. DR BioCyc; NGON242231:GI2G-2068-MONOMER; -. DR Proteomes; UP000000535; 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_0000198496. SQ SEQUENCE 121 AA; 14217 MW; 991703EF4865E0F2 CRC64; MDYRFGRQYR LLKTDDFSSV FAFRNRRSRD LLQVSRSNGN GLDHPRIGLV VGKKTAKRAN ERNYMKRVIR DWFRLNKNRL PPQDFVVRVR RKFDRATAKQ ARAELAQLMF GNPATGCGKQ V // ID RS11_NEIG1 Reviewed; 131 AA. AC Q5F5V0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rpsK {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=NGO1820; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90437.1; -; Genomic_DNA. DR RefSeq; WP_002216249.1; NC_002946.2. DR RefSeq; YP_208849.1; NC_002946.2. DR ProteinModelPortal; Q5F5V0; -. DR SMR; Q5F5V0; 15-131. DR EnsemblBacteria; AAW90437; AAW90437; NGO_1820. DR GeneID; 25048807; -. DR GeneID; 3282289; -. DR KEGG; ngo:NGO1820; -. DR PATRIC; 20337300; VBINeiGon24812_2185. DR HOGENOM; HOG000111597; -. DR KO; K02948; -. DR OMA; NTPYASQ; -. DR OrthoDB; EOG6ZSPF3; -. DR BioCyc; NGON242231:GI2G-1717-MONOMER; -. DR Proteomes; UP000000535; 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_0000230409. SQ SEQUENCE 131 AA; 13919 MW; DE7BDB80F3A9CFE9 CRC64; MAKANTASRV RKKVRKTVSE GIVHVHASFN NTIITITDRQ GNALSWATSG GAGFKGSRKS TPFAAQVAAE AAGKVAQEYG VKNLEVRIKG PGPGRESSVR ALNALGFKIT SITDVTPLPH NGCRPPKKRR I // ID RPOC_NEIG1 Reviewed; 1391 AA. AC Q5F5R6; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO1850; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90471.1; -; Genomic_DNA. DR RefSeq; WP_003700598.1; NC_002946.2. DR RefSeq; YP_208883.1; NC_002946.2. DR ProteinModelPortal; Q5F5R6; -. DR PRIDE; Q5F5R6; -. DR EnsemblBacteria; AAW90471; AAW90471; NGO_1850. DR GeneID; 3282397; -. DR KEGG; ngo:NGO1850; -. DR PATRIC; 20337378; VBINeiGon24812_2224. DR HOGENOM; HOG000218386; -. DR KO; K03046; -. DR OMA; YDLVNQN; -. DR OrthoDB; EOG6M9DS6; -. DR BioCyc; NGON242231:GI2G-1751-MONOMER; -. DR Proteomes; UP000000535; 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_0000225555. SQ SEQUENCE 1391 AA; 153794 MW; C11BB9E3FDC12382 CRC64; MNLLNLFNPL QTAGMEEEFD AIKIGIASPE TIRSWSYGEV KKPETINYRT FKPERDGLFC AKIFGPVKDY ECLCGKYKRL KFKGVTCEKC GVEVTLSKVR RERMGHIELA APVAHIWFLK SLPSRLGMVL NMTLRDIERV LYFEAFVVTD PGMTPLQRRQ LLTEDDYYNK LDEYGDDFDA KMGAEGIREL LRTLDVAGEI 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 RDGNEVDQES 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 ENMEEGVTVA KQTDDVTGLS TLVVIDGKRR SSSASKLLRP TVKLLDENGV EICIPGTSTP VSMAFPVGAV ITVREGQEIG KGDVLARIPQ ASSKTRDITG GLPRVAELFE ARVPKDAGML AEITGTVSFG KETKGKQRLI ITDVDGVAYE TLISKEKQIL VHDGQVVNRG ETIVDGAVDP HDILRLQGIE ALARYIVQEV QEVYRLQGVK ISDKHIEVII RQMLRRVNIA DAGETGFITG EQVERGDVMA ANEKALEEGK EPARYENILL GITKASLSTD SFISAASFQE TTRVLTEAAI MGKQDELRGL KENVIVGRLI PAGTGLTYHR SRHQQWQGVE QETAETQVTD E // ID RPPH_NEIG1 Reviewed; 174 AA. AC Q5F753; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 09-DEC-2015, entry version 61. 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=NGO1334; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89984.1; 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; AE004969; AAW89984.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_208396.1; NC_002946.2. DR ProteinModelPortal; Q5F753; -. DR DNASU; 3282046; -. DR EnsemblBacteria; AAW89984; AAW89984; NGO_1334. DR GeneID; 3282046; -. DR KEGG; ngo:NGO1334; -. DR PATRIC; 20336037; VBINeiGon24812_1568. DR HOGENOM; HOG000066723; -. DR KO; K08311; -. DR OrthoDB; EOG6Q2SKR; -. DR BioCyc; NGON242231:GI2G-1248-MONOMER; -. DR Proteomes; UP000000535; 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_0000231917. FT DOMAIN 6 149 Nudix hydrolase. {ECO:0000255|HAMAP- FT Rule:MF_00298}. FT MOTIF 38 59 Nudix box. SQ SEQUENCE 174 AA; 21044 MW; 843034C69554F1EF CRC64; MLDREGYRPN VGIILINERN EVFWGKRVRE HSWQFPQGGI KPGESPETAM YRELYEEVGL LPQHVKIVGR TRDWLRYDVP NNWVRREWRG SYRGQKQIWY LLRLTGRDCD VNLRATRHPE FDGWRWHQYW APVDEVIDFK RDVYLEALKE LSSRFLRGME SYEDFAARQP SGNR // ID RS13_NEIG1 Reviewed; 120 AA. AC Q5F5U9; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=NGO1821; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90438.1; -; Genomic_DNA. DR RefSeq; WP_002215453.1; NC_002946.2. DR RefSeq; YP_208850.1; NC_002946.2. DR ProteinModelPortal; Q5F5U9; -. DR SMR; Q5F5U9; 2-116. DR EnsemblBacteria; AAW90438; AAW90438; NGO_1821. DR GeneID; 3282445; -. DR KEGG; ngo:NGO1821; -. DR PATRIC; 20337302; VBINeiGon24812_2186. DR HOGENOM; HOG000039879; -. DR KO; K02952; -. DR OMA; RTKNNSR; -. DR OrthoDB; EOG618R01; -. DR BioCyc; NGON242231:GI2G-1718-MONOMER; -. DR Proteomes; UP000000535; 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_0000230531. SQ SEQUENCE 120 AA; 13360 MW; 0CA46DB81385B657 CRC64; MARIAGVNIP NNAHIVIGLQ AIYGIGATRA KLICEAANIA PDTKAKDLDE TQLDALRDQV AKYEVEGDLR REVTMSIKRL MDMGCYRGFR HRRGLPCRGQ RTRTNARTRK GPRKAIAGKK // ID RPIA_NEIG1 Reviewed; 223 AA. AC Q5F831; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO0970; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89656.1; -; Genomic_DNA. DR RefSeq; WP_003688327.1; NC_002946.2. DR RefSeq; YP_208068.1; NC_002946.2. DR ProteinModelPortal; Q5F831; -. DR SMR; Q5F831; 3-218. DR EnsemblBacteria; AAW89656; AAW89656; NGO_0970. DR GeneID; 3281118; -. DR KEGG; ngo:NGO0970; -. DR PATRIC; 20335134; VBINeiGon24812_1136. DR HOGENOM; HOG000276368; -. DR KO; K01807; -. DR OMA; GACHVQE; -. DR OrthoDB; EOG67MF61; -. DR BioCyc; NGON242231:GI2G-898-MONOMER; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000000535; 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_0000158437. 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; 23890 MW; 4F781726C0F0B73F CRC64; MTTQDELKRI AAEKAVEFVP ENEYIGIGTG STINFFIEAL GKSGKKIKGA VSTSKKSGEL LARYDIPVVS LNEVSGLAVY IDGADEVNHA LQMIKGGGGA HLNEKIVASA SEKFVCIADE SKYVSRLGKF PLPVEAVESA RSLVSRKLLA MGGQPELRIG YTTFYGNQIV DVHGLNIDQP LTMEDEINKI TGVLENGIFA RDAADVLILG TEEGAKVIYP CQG // ID RS17_NEIG1 Reviewed; 87 AA. AC Q5F5T6; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=30S ribosomal protein S17 {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rpsQ {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=NGO1830; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90451.1; -; Genomic_DNA. DR RefSeq; WP_003690077.1; NC_002946.2. DR RefSeq; YP_208863.1; NC_002946.2. DR ProteinModelPortal; Q5F5T6; -. DR SMR; Q5F5T6; 7-84. DR EnsemblBacteria; AAW90451; AAW90451; NGO_1830. DR GeneID; 3282162; -. DR KEGG; ngo:NGO1830; -. DR PATRIC; 20337330; VBINeiGon24812_2200. DR HOGENOM; HOG000231339; -. DR KO; K02961; -. DR OMA; LKAHDEQ; -. DR OrthoDB; EOG63JRH2; -. DR BioCyc; NGON242231:GI2G-1731-MONOMER; -. DR Proteomes; UP000000535; 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_0000233516. SQ SEQUENCE 87 AA; 9820 MW; 0D90FDD2F3B79C46 CRC64; MSETKNVRTL QGKVVSDKMD KTVTVLVERK VKHSLYGKII RLSTKIHAHD ENNQYGIGDV VVISESRPLS KTKSWVVSEL VEKARSI // ID RS18_NEIG1 Reviewed; 76 AA. AC Q5F923; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=30S ribosomal protein S18 {ECO:0000255|HAMAP-Rule:MF_00270}; GN Name=rpsR {ECO:0000255|HAMAP-Rule:MF_00270}; GN OrderedLocusNames=NGO0583; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89314.1; -; Genomic_DNA. DR RefSeq; WP_002213306.1; NC_002946.2. DR RefSeq; YP_207726.1; NC_002946.2. DR ProteinModelPortal; Q5F923; -. DR SMR; Q5F923; 8-76. DR EnsemblBacteria; AAW89314; AAW89314; NGO_0583. DR GeneID; 3283073; -. DR KEGG; ngo:NGO0583; -. DR PATRIC; 20334234; VBINeiGon24812_0689. DR HOGENOM; HOG000218466; -. DR KO; K02963; -. DR OMA; YKRPDIL; -. DR OrthoDB; EOG6PCQ4R; -. DR BioCyc; NGON242231:GI2G-554-MONOMER; -. DR Proteomes; UP000000535; 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_1000003543. SQ SEQUENCE 76 AA; 8993 MW; 0842C771DC9CAD5A CRC64; MARQSFKRRK FCRFTAEKIQ EVDYKQVDLL KDFISENGKI IPARITGTKA FYQRQLAVAV KRARFLALLP YTDQHK // ID RS19_NEIG1 Reviewed; 92 AA. AC Q5F5T1; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=30S ribosomal protein S19 {ECO:0000255|HAMAP-Rule:MF_00531}; GN Name=rpsS {ECO:0000255|HAMAP-Rule:MF_00531}; GN OrderedLocusNames=NGO1834; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90456.1; -; Genomic_DNA. DR RefSeq; WP_003690082.1; NC_002946.2. DR RefSeq; YP_208868.1; NC_002946.2. DR ProteinModelPortal; Q5F5T1; -. DR SMR; Q5F5T1; 3-88. DR PRIDE; Q5F5T1; -. DR EnsemblBacteria; AAW90456; AAW90456; NGO_1834. DR GeneID; 3282438; -. DR KEGG; ngo:NGO1834; -. DR PATRIC; 20337340; VBINeiGon24812_2205. DR HOGENOM; HOG000111560; -. DR KO; K02965; -. DR OMA; VHNGRQF; -. DR OrthoDB; EOG61S365; -. DR BioCyc; NGON242231:GI2G-1736-MONOMER; -. DR Proteomes; UP000000535; 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_0000265388. SQ SEQUENCE 92 AA; 10390 MW; 53390EA759C41EA5 CRC64; MARSLKKGPY VDLHLLKKVD AVRASNDKRP IKTWSRRSTI LPDFIGLTIA VHNGRTHVPV FISDNMVGHK LGEFSLTRTF KGHLADKKAK KK // ID RRF_NEIG1 Reviewed; 185 AA. AC Q5F5X3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO1796; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90414.1; -; Genomic_DNA. DR RefSeq; WP_003690026.1; NC_002946.2. DR RefSeq; YP_208826.1; NC_002946.2. DR ProteinModelPortal; Q5F5X3; -. DR SMR; Q5F5X3; 1-185. DR EnsemblBacteria; AAW90414; AAW90414; NGO_1796. DR GeneID; 3282506; -. DR KEGG; ngo:NGO1796; -. DR PATRIC; 20337242; VBINeiGon24812_2156. DR HOGENOM; HOG000040143; -. DR KO; K02838; -. DR OMA; VQPWEKK; -. DR OrthoDB; EOG6SV5F9; -. DR BioCyc; NGON242231:GI2G-1694-MONOMER; -. DR Proteomes; UP000000535; 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_0000167501. SQ SEQUENCE 185 AA; 20643 MW; 6F0CAD2889846603 CRC64; MINDIQKTAE GKMQRSVEVL KENLAKVRTG RAHTGLLDQV EVEYWGSMVP VSQVANVTLL DARTIGVKPF EGNMAAKVEK AIRDSNLGLN PAAVGDLIRV PMPMLTEERR KDLIKVVRGE AEEGRVSIRN VRRDANDHIK KLLKDKEISE DEARRGEEAV QKLTDKYIAE ADKVLAAKEE DLMAV // ID RS12_NEIG1 Reviewed; 123 AA. AC Q5F5S1; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN Name=rpsL {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=NGO1845; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90466.1; -; Genomic_DNA. DR RefSeq; WP_003690100.1; NC_002946.2. DR RefSeq; YP_208878.1; NC_002946.2. DR ProteinModelPortal; Q5F5S1; -. DR SMR; Q5F5S1; 3-123. DR EnsemblBacteria; AAW90466; AAW90466; NGO_1845. DR GeneID; 3282376; -. DR KEGG; ngo:NGO1845; -. DR PATRIC; 20337364; VBINeiGon24812_2217. DR HOGENOM; HOG000040063; -. DR KO; K02950; -. DR OMA; LKSCPER; -. DR OrthoDB; EOG61ZTNF; -. DR BioCyc; NGON242231:GI2G-1746-MONOMER; -. DR Proteomes; UP000000535; 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; Methylation; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 123 30S ribosomal protein S12. FT /FTId=PRO_0000226397. FT MOD_RES 89 89 3-methylthioaspartic acid. {ECO:0000250}. SQ SEQUENCE 123 AA; 13736 MW; C9C8D691DBD67949 CRC64; MPTINQLVRK GRQKPVYVNK VPALEACPQK RGVCTRVYTT TPRKPNSALR KVCKVRLTNG FEVISYIGGE GHNLQEHSVV LIRGGRVKDL PGVRYHTVRG SLDTAGVKDR KQARSKYGAK RPK // ID RS15_NEIG1 Reviewed; 89 AA. AC Q5FA41; DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rpsO {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=NGO0191; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88946.1; -; Genomic_DNA. DR RefSeq; WP_002217790.1; NC_002946.2. DR RefSeq; YP_207358.1; NC_002946.2. DR ProteinModelPortal; Q5FA41; -. DR SMR; Q5FA41; 2-89. DR EnsemblBacteria; AAW88946; AAW88946; NGO_0191. DR GeneID; 3281588; -. DR KEGG; ngo:NGO0191; -. DR PATRIC; 20333311; VBINeiGon24812_0238. DR HOGENOM; HOG000040097; -. DR KO; K02956; -. DR OMA; TEHFKSH; -. DR OrthoDB; EOG6B368J; -. DR BioCyc; NGON242231:GI2G-176-MONOMER; -. DR Proteomes; UP000000535; 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_0000115487. SQ SEQUENCE 89 AA; 10386 MW; CF29ABE602503B01 CRC64; MALTVEQKAQ IVKDFQRKEG DTGSSEVQVA LLTFRINDLT PHFKANPKDH HSRRGLLKMV SQRRRLLAYL RRTQPDTYRA LITRLGLRK // ID RS2_NEIG1 Reviewed; 242 AA. AC Q5F5F3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=30S ribosomal protein S2 {ECO:0000255|HAMAP-Rule:MF_00291}; GN Name=rpsB {ECO:0000255|HAMAP-Rule:MF_00291}; GN OrderedLocusNames=NGO1975; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90584.1; -; Genomic_DNA. DR RefSeq; WP_003686861.1; NC_002946.2. DR RefSeq; YP_208996.1; NC_002946.2. DR ProteinModelPortal; Q5F5F3; -. DR SMR; Q5F5F3; 9-226. DR PRIDE; Q5F5F3; -. DR EnsemblBacteria; AAW90584; AAW90584; NGO_1975. DR GeneID; 3282648; -. DR KEGG; ngo:NGO1975; -. DR PATRIC; 20337715; VBINeiGon24812_2384. DR HOGENOM; HOG000071892; -. DR KO; K02967; -. DR OMA; RIPDILY; -. DR OrthoDB; EOG6XWV6P; -. DR BioCyc; NGON242231:GI2G-1874-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 242 30S ribosomal protein S2. FT /FTId=PRO_1000004004. SQ SEQUENCE 242 AA; 26917 MW; 59E694E1E9B826E4 CRC64; MSQITMRQMI EAGVHFGHQT RFWNPKMAQY IFGARNKIHI VNLEKTLPMF QEAQEAVRRL VANKGTVLFV GTKRQARDII REEATRAGMP FVDHRWLGGM LTNYKTVKQS IKRLEEKTAA LENAAESGFS KKEILEMQRD VEKLERSLGG IKNMKGLPDA IFVIDTGYQK GTLVEAEKLG IPVIAVVDTN NSPDGVKYVI PGNDDSAKAI RLYCRGIADA VLEGKNQALQ ETVAAAQETA AE // ID RS7_NEIG1 Reviewed; 156 AA. AC Q5F5S2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rpsG {ECO:0000255|HAMAP-Rule:MF_00480}; GN OrderedLocusNames=NGO1844; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90465.1; -; Genomic_DNA. DR RefSeq; WP_003690099.1; NC_002946.2. DR RefSeq; YP_208877.1; NC_002946.2. DR ProteinModelPortal; Q5F5S2; -. DR SMR; Q5F5S2; 3-154. DR EnsemblBacteria; AAW90465; AAW90465; NGO_1844. DR GeneID; 3282420; -. DR KEGG; ngo:NGO1844; -. DR PATRIC; 20337362; VBINeiGon24812_2216. DR HOGENOM; HOG000039067; -. DR KO; K02992; -. DR OMA; EVHRMAD; -. DR OrthoDB; EOG6P5ZKW; -. DR BioCyc; NGON242231:GI2G-1745-MONOMER; -. DR Proteomes; UP000000535; 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_0000226510. SQ SEQUENCE 156 AA; 17645 MW; 67289A059C8025CF CRC64; MPRRREVPKR DVLPDPKFGS VELTKFMNVL MIDGKKSVAE RIVYGALEQI EKKTGKAAIE VFNEAIANSK PIVEVKSRRV GGANYQVPVE VRPSRRLALA MRWVRDAARK RGEKSMDLRL AGELIDASEG RGGALKKREE VHRMAEANKA FSHFRF // ID RS10_NEIG1 Reviewed; 103 AA. AC Q5F5S5; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rpsJ {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=NGO1841; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90462.1; -; Genomic_DNA. DR RefSeq; WP_002215394.1; NC_002946.2. DR RefSeq; YP_208874.1; NC_002946.2. DR ProteinModelPortal; Q5F5S5; -. DR SMR; Q5F5S5; 5-102. DR PRIDE; Q5F5S5; -. DR EnsemblBacteria; AAW90462; AAW90462; NGO_1841. DR GeneID; 3282416; -. DR KEGG; ngo:NGO1841; -. DR PATRIC; 20337356; VBINeiGon24812_2213. DR HOGENOM; HOG000270246; -. DR KO; K02946; -. DR OMA; QQKIRIK; -. DR OrthoDB; EOG6VXFHB; -. DR BioCyc; NGON242231:GI2G-1742-MONOMER; -. DR Proteomes; UP000000535; 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_0000237067. SQ SEQUENCE 103 AA; 11807 MW; 7A112084E44867EF CRC64; MANQKIRIRL KAYDYALIDR SAQEIVETAK RTGAVVKGPI PLPTKIERFN ILRSPHVNKT SREQLEIRTH LRLMDIVDWT DKTTDALMKL DLPAGVDVEI KVQ // ID RS14_NEIG1 Reviewed; 101 AA. AC Q5F5U0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE RecName: Full=30S ribosomal protein S14 {ECO:0000255|HAMAP-Rule:MF_00537}; GN Name=rpsN {ECO:0000255|HAMAP-Rule:MF_00537}; ORFNames=NGO18261; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90447.1; -; Genomic_DNA. DR RefSeq; WP_002216244.1; NC_002946.2. DR RefSeq; YP_208859.1; NC_002946.2. DR ProteinModelPortal; Q5F5U0; -. DR SMR; Q5F5U0; 41-101. DR EnsemblBacteria; AAW90447; AAW90447; NGO_18261. DR GeneID; 3282440; -. DR KEGG; ngo:NGO18261; -. DR PATRIC; 20337322; VBINeiGon24812_2196. DR HOGENOM; HOG000039864; -. DR KO; K02954; -. DR OMA; NRCVLTS; -. DR OrthoDB; EOG6BCT0K; -. DR BioCyc; NGON242231:GI2G-1727-MONOMER; -. DR Proteomes; UP000000535; 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_1000128460. SQ SEQUENCE 101 AA; 11518 MW; DDC3585439E26E9C CRC64; MAKKALINRD LKRQALAKKY AAKRAAIKAV INDSNATEEE RFEARLRFQS IPRNAAPVRQ RRRCALTGRP RGTFRKFGLG RIKIREIAMR GEIPGVVKAS W // ID RS16_NEIG1 Reviewed; 81 AA. AC Q5FA57; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=30S ribosomal protein S16 {ECO:0000255|HAMAP-Rule:MF_00385}; GN Name=rpsP {ECO:0000255|HAMAP-Rule:MF_00385}; GN OrderedLocusNames=NGO0174; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88930.1; -; Genomic_DNA. DR RefSeq; WP_003687476.1; NC_002946.2. DR RefSeq; YP_207342.1; NC_002946.2. DR ProteinModelPortal; Q5FA57; -. DR SMR; Q5FA57; 1-77. DR EnsemblBacteria; AAW88930; AAW88930; NGO_0174. DR GeneID; 3281160; -. DR KEGG; ngo:NGO0174; -. DR PATRIC; 20333271; VBINeiGon24812_0218. DR HOGENOM; HOG000246720; -. DR KO; K02959; -. DR OMA; TRMGRNK; -. DR OrthoDB; EOG6CVVKH; -. DR BioCyc; NGON242231:GI2G-160-MONOMER; -. DR Proteomes; UP000000535; 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_0000243833. SQ SEQUENCE 81 AA; 9320 MW; F8419DA9D9BFA23A CRC64; MVVIRLARGG SKHRPFYNVI VTDSRSRRDG RFIERVGFYN PVANEKQERV RLNADRLNHW IAQGAQVSDS VAKLIKEQKA V // ID RS20_NEIG1 Reviewed; 87 AA. AC Q5F6Q6; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=30S ribosomal protein S20 {ECO:0000255|HAMAP-Rule:MF_00500}; GN Name=rpsT {ECO:0000255|HAMAP-Rule:MF_00500}; GN OrderedLocusNames=NGO1493; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90131.1; -; Genomic_DNA. DR RefSeq; WP_002212556.1; NC_002946.2. DR RefSeq; YP_208543.1; NC_002946.2. DR ProteinModelPortal; Q5F6Q6; -. DR SMR; Q5F6Q6; 3-87. DR EnsemblBacteria; AAW90131; AAW90131; NGO_1493. DR GeneID; 25048215; -. DR GeneID; 3281600; -. DR KEGG; ngo:NGO1493; -. DR PATRIC; 20336440; VBINeiGon24812_1767. DR HOGENOM; HOG000097048; -. DR KO; K02968; -. DR OMA; ARRAHNI; -. DR OrthoDB; EOG6HMXNQ; -. DR BioCyc; NGON242231:GI2G-1397-MONOMER; -. DR Proteomes; UP000000535; 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_0000224973. SQ SEQUENCE 87 AA; 9508 MW; F7C297D93537B4F0 CRC64; MANSAQARKR ARQSVKQRAH NASLRTAFRT AVKKVLKAVE AGDKAAAQAV YQESVKVIDR IADKGVFHKN KAARHKSRLS AKVKALA // ID RS3_NEIG1 Reviewed; 230 AA. AC Q5F5T3; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rpsC {ECO:0000255|HAMAP-Rule:MF_01309}; GN OrderedLocusNames=NGO1832; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90454.1; -; Genomic_DNA. DR RefSeq; WP_003690079.1; NC_002946.2. DR RefSeq; YP_208866.1; NC_002946.2. DR ProteinModelPortal; Q5F5T3; -. DR SMR; Q5F5T3; 2-203. DR PRIDE; Q5F5T3; -. DR EnsemblBacteria; AAW90454; AAW90454; NGO_1832. DR GeneID; 3282435; -. DR KEGG; ngo:NGO1832; -. DR PATRIC; 20337336; VBINeiGon24812_2203. DR HOGENOM; HOG000210610; -. DR KO; K02982; -. DR OMA; KTNPIGN; -. DR OrthoDB; EOG6K13X3; -. DR BioCyc; NGON242231:GI2G-1734-MONOMER; -. DR Proteomes; UP000000535; 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_0000230706. FT DOMAIN 39 107 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 230 AA; 25826 MW; AD81FEB1B90CA9B2 CRC64; MGQKINPTGF RLAVTKDWAS KWFAKSTDFS TVLKQDIDVR NYLRQKLANA SVGRVIIERP AKSARITIHS ARPGVVIGKK GEDIEVLKRD LQVLMGVPIH VNIEEIRRPE LDAQIIADGI AQQLEKRVQF RRAMKRAMQN AMRSGAKGIK IMTSGRLNGA DIARSEWYRE GRVPLHTLRA NVDYATSEAH TTYGVLGLKV WVYTEGNIKS SKPEHESKQR KAGRRNAAAN // ID RS5_NEIG1 Reviewed; 172 AA. AC Q5F5U4; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rpsE {ECO:0000255|HAMAP-Rule:MF_01307}; GN OrderedLocusNames=NGO1824; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90443.1; -; Genomic_DNA. DR RefSeq; WP_002215445.1; NC_002946.2. DR RefSeq; YP_208855.1; NC_002946.2. DR ProteinModelPortal; Q5F5U4; -. DR SMR; Q5F5U4; 13-160. DR PRIDE; Q5F5U4; -. DR EnsemblBacteria; AAW90443; AAW90443; NGO_1824. DR GeneID; 3282448; -. DR KEGG; ngo:NGO1824; -. DR PATRIC; 20337314; VBINeiGon24812_2192. DR HOGENOM; HOG000072595; -. DR KO; K02988; -. DR OMA; PHEQKGK; -. DR OrthoDB; EOG6FJNM5; -. DR BioCyc; NGON242231:GI2G-1723-MONOMER; -. DR Proteomes; UP000000535; 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_0000131558. 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 RS21_NEIG1 Reviewed; 70 AA. AC Q5F506; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=30S ribosomal protein S21 {ECO:0000255|HAMAP-Rule:MF_00358}; GN Name=rpsU {ECO:0000255|HAMAP-Rule:MF_00358}; GN OrderedLocusNames=NGO2134; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein S21P family. CC {ECO:0000255|HAMAP-Rule:MF_00358}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90731.1; -; Genomic_DNA. DR RefSeq; WP_002214819.1; NC_002946.2. DR RefSeq; YP_209143.1; NC_002946.2. DR ProteinModelPortal; Q5F506; -. DR SMR; Q5F506; 4-54. DR DNASU; 3282787; -. DR EnsemblBacteria; AAW90731; AAW90731; NGO_2134. DR GeneID; 23784015; -. DR GeneID; 3282787; -. DR KEGG; ngo:NGO2134; -. DR PATRIC; 20338117; VBINeiGon24812_2581. DR HOGENOM; HOG000157460; -. DR KO; K02970; -. DR OMA; KRHFKRL; -. DR OrthoDB; EOG6FBX3Z; -. DR BioCyc; NGON242231:GI2G-2025-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 70 30S ribosomal protein S21. FT /FTId=PRO_0000266711. SQ SEQUENCE 70 AA; 8355 MW; 1A80F0A6CEC081D6 CRC64; MPAIRVKENE PFEVAMRRFK RAVEKTGLLT ELRAREAYEK PTTERKRKKA AAVKRLQKRL RSQQLPPKMY // ID RS4_NEIG1 Reviewed; 206 AA. AC Q5F5V1; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rpsD {ECO:0000255|HAMAP-Rule:MF_01306}; GN OrderedLocusNames=NGO1819; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90436.1; -; Genomic_DNA. DR RefSeq; WP_002215455.1; NC_002946.2. DR RefSeq; YP_208848.1; NC_002946.2. DR ProteinModelPortal; Q5F5V1; -. DR SMR; Q5F5V1; 2-206. DR PRIDE; Q5F5V1; -. DR EnsemblBacteria; AAW90436; AAW90436; NGO_1819. DR GeneID; 3282442; -. DR KEGG; ngo:NGO1819; -. DR PATRIC; 20337298; VBINeiGon24812_2184. DR HOGENOM; HOG000221003; -. DR KO; K02986; -. DR OMA; VYEWITW; -. DR OrthoDB; EOG6N3CXM; -. DR BioCyc; NGON242231:GI2G-1716-MONOMER; -. DR Proteomes; UP000000535; 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_0000228904. 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 RSMA_NEIG1 Reviewed; 259 AA. AC Q5F9W4; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO0272; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89023.1; -; Genomic_DNA. DR RefSeq; WP_003706653.1; NC_002946.2. DR RefSeq; YP_207435.1; NC_002946.2. DR ProteinModelPortal; Q5F9W4; -. DR EnsemblBacteria; AAW89023; AAW89023; NGO_0272. DR GeneID; 3283045; -. DR KEGG; ngo:NGO0272; -. DR PATRIC; 20333513; VBINeiGon24812_0337. DR HOGENOM; HOG000227962; -. DR KO; K02528; -. DR OMA; HYPGRLE; -. DR OrthoDB; EOG66F08Z; -. DR BioCyc; NGON242231:GI2G-255-MONOMER; -. DR Proteomes; UP000000535; 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_0000101570. 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; 29236 MW; EF5B414C43C8091A CRC64; MKEHKARKRF GQNFLQDTRI IGDIVNAVRP QADDVVIEIG PGLAAITEPL AKKLNRLHVV EIDRDIVCRL KTLPFADKLV IHEGDVLQFD FNGISGKKKI VGNLPYNIST PLLFKLAEVA DDVADMHFML QKEVVERMVA APKSNDYGRL GVMLQYFFDM ELLIDVPPES FDPAPKIDSA VVRMIPVKHR IGKADDFDHF AKLVKLAFRQ RRKTIRNNLK ELADDDDLQA VGISPQDRAE HIAPEKYVAL SNYLADKAV // ID RS8_NEIG1 Reviewed; 130 AA. AC Q5F5U1; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=30S ribosomal protein S8 {ECO:0000255|HAMAP-Rule:MF_01302}; GN Name=rpsH {ECO:0000255|HAMAP-Rule:MF_01302}; GN OrderedLocusNames=NGO1826; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90446.1; -; Genomic_DNA. DR RefSeq; WP_002215438.1; NC_002946.2. DR RefSeq; YP_208858.1; NC_002946.2. DR ProteinModelPortal; Q5F5U1; -. DR SMR; Q5F5U1; 2-130. DR EnsemblBacteria; AAW90446; AAW90446; NGO_1826. DR GeneID; 3282449; -. DR KEGG; ngo:NGO1826; -. DR PATRIC; 20337320; VBINeiGon24812_2195. DR HOGENOM; HOG000204095; -. DR KO; K02994; -. DR OMA; KYKGNQS; -. DR OrthoDB; EOG6Z0QH1; -. DR BioCyc; NGON242231:GI2G-1726-MONOMER; -. DR Proteomes; UP000000535; 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_0000126450. SQ SEQUENCE 130 AA; 14124 MW; 6420D912297511E6 CRC64; MSMHDPISDM LTRIRNAQRA NKAAVAMPSS KLKCAIAKVL KEEGYIEDFA VSSDVKSILE IQLKYYAGRP VIEQIKRVSR PGLRIYKASS EIPSVMNGLG IAIVSTSKGV MTDRKARSQG VGGELLCIVA // ID RSMG_NEIG1 Reviewed; 207 AA. AC Q5F5X7; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1791; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90410.1; -; Genomic_DNA. DR RefSeq; WP_003690016.1; NC_002946.2. DR RefSeq; YP_208822.1; NC_002946.2. DR ProteinModelPortal; Q5F5X7; -. DR EnsemblBacteria; AAW90410; AAW90410; NGO_1791. DR GeneID; 3282541; -. DR KEGG; ngo:NGO1791; -. DR PATRIC; 20337228; VBINeiGon24812_2150. DR HOGENOM; HOG000221012; -. DR KO; K03501; -. DR OMA; NTRWLAM; -. DR OrthoDB; EOG6HF639; -. DR BioCyc; NGON242231:GI2G-1689-MONOMER; -. DR Proteomes; UP000000535; 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_0000184291. 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; 22774 MW; 9C6E7D01F7576704 CRC64; MERKERLRAG IAAMGPDISE TAQDRLLAYV DLLKKWNKTY NLTALRDEEK MIVHHLLDSL TLLPYIEGAQ TMLDVGSGGG QPGIPAAVCR PDVQITLLDA NTKKTAFLRQ AAIELGLDNV RVVSGRVEAV SDVRADVVTS RAFAELADFV SWTAHLLKDG GYWAAMKGVY PQGEIGRLPQ DVCVEKVQRL DVPGLDAERH IVILSKR // ID RSGA_NEIG1 Reviewed; 307 AA. AC Q5F633; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO1733; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90354.1; -; Genomic_DNA. DR RefSeq; WP_003694242.1; NC_002946.2. DR RefSeq; YP_208766.1; NC_002946.2. DR ProteinModelPortal; Q5F633; -. DR EnsemblBacteria; AAW90354; AAW90354; NGO_1733. DR GeneID; 3281155; -. DR KEGG; ngo:NGO1733; -. DR PATRIC; 20337064; VBINeiGon24812_2072. DR HOGENOM; HOG000006957; -. DR KO; K06949; -. DR OMA; TARLFHF; -. DR OrthoDB; EOG69SKDD; -. DR BioCyc; NGON242231:GI2G-1629-MONOMER; -. DR Proteomes; UP000000535; 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; 3.40.50.300; -; 1. DR HAMAP; MF_01820; GTPase_RsgA; 1. DR InterPro; IPR030378; G_CP_dom. 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_1000188106. 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; 33508 MW; CE9254323E738BAF CRC64; MPSEHPFSDG ISTPNPKETM NDTAQITAGY GRRYIVRTPD GTTYEASTRK KRVDFACGDR VRISPVNAEQ VVIEDFLPRQ SLLYRQDAWK TKLIAANVTQ LLIVTAAVPS PSVRLLQRAL LAAEAAGIRA VIVLNKADLP ETALWLEKLK FYETLGYPVI ETRVLENADS LRPVLQGHSN ILLGQSGMGK STLANALLGS QTARTGDISA ALDSGKHTTT HARLYDLNGE TQLIDSPGLQ EFGLHHLQAA DLPHYFPDFR HLVGQCRFHN CTHRAEPGCA FKAAAETGAA SPERLAFLQG ITDELLG // ID RS6_NEIG1 Reviewed; 122 AA. AC Q5F925; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=30S ribosomal protein S6 {ECO:0000255|HAMAP-Rule:MF_00360}; GN Name=rpsF {ECO:0000255|HAMAP-Rule:MF_00360}; GN OrderedLocusNames=NGO0581; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds together with S18 to 16S ribosomal RNA. CC {ECO:0000255|HAMAP-Rule:MF_00360}. CC -!- SIMILARITY: Belongs to the ribosomal protein S6P family. CC {ECO:0000255|HAMAP-Rule:MF_00360}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89312.1; -; Genomic_DNA. DR RefSeq; WP_003688967.1; NC_002946.2. DR RefSeq; YP_207724.1; NC_002946.2. DR ProteinModelPortal; Q5F925; -. DR SMR; Q5F925; 1-100. DR PRIDE; Q5F925; -. DR EnsemblBacteria; AAW89312; AAW89312; NGO_0581. DR GeneID; 3282311; -. DR KEGG; ngo:NGO0581; -. DR PATRIC; 20334230; VBINeiGon24812_0687. DR HOGENOM; HOG000040438; -. DR KO; K02990; -. DR OMA; ITEASPM; -. DR OrthoDB; EOG6P33DH; -. DR BioCyc; NGON242231:GI2G-552-MONOMER; -. DR Proteomes; UP000000535; 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_0000229555. SQ SEQUENCE 122 AA; 13861 MW; AE2DAB2209392FD2 CRC64; MRHYEIVFIV HPDQSEQVPA MVERYKTMIT EANGKIHRLE DWGRRQLAYP INKIHKAHYV LMNIETTPEV VGELETAFRF NDAVLRHLTI KTKHAVTEAS PMLGGEKAKN LLVGAAEEAA AQ // ID RSMH_NEIG1 Reviewed; 318 AA. AC Q5F6K7; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO1544; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90180.1; -; Genomic_DNA. DR RefSeq; WP_003697441.1; NC_002946.2. DR RefSeq; YP_208592.1; NC_002946.2. DR ProteinModelPortal; Q5F6K7; -. DR EnsemblBacteria; AAW90180; AAW90180; NGO_1544. DR GeneID; 3281471; -. DR KEGG; ngo:NGO1544; -. DR PATRIC; 20336586; VBINeiGon24812_1841. DR HOGENOM; HOG000049778; -. DR KO; K03438; -. DR OMA; HVPVMLQ; -. DR OrthoDB; EOG6X9MQ1; -. DR BioCyc; NGON242231:GI2G-1446-MONOMER; -. DR Proteomes; UP000000535; 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 1 318 Ribosomal RNA small subunit FT methyltransferase H. FT /FTId=PRO_0000108669. 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 318 AA; 34829 MW; 3AD24D09D91161AF CRC64; MSGAESYRHI TVLLNEAVDA LAVREDGVYV DGTFGRGGHS RLILSRLGDA GRLIVFDKDP QAIAVAEELA RSDKRVGVVH GGFASFQTAL DGLGIGKVDG ALFDLGISSP QIDDGSRGFS FRFDAPLDMR MDTTRGMSAA EWIAVASEQD LHEVIKNYGE ERFSRQIVRA IVAQRAESPI DTTRKLAQIV AQNVRTRERG QDPATRTFQA IRIFINRELE EVGAVLPQVM CRLKEGGRLA VIAFHSLEDR IVKQFVKKYS QHEPLPSWAA VREADLPDPP LKIVGRALKP GEAEIAANPR ARSAVLRVAE RTAGPIPE // ID RS9_NEIG1 Reviewed; 130 AA. AC Q5F5A4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=30S ribosomal protein S9 {ECO:0000255|HAMAP-Rule:MF_00532}; GN Name=rpsI {ECO:0000255|HAMAP-Rule:MF_00532}; GN OrderedLocusNames=NGO2025; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90633.1; -; Genomic_DNA. DR RefSeq; WP_003686946.1; NC_002946.2. DR RefSeq; YP_209045.1; NC_002946.2. DR ProteinModelPortal; Q5F5A4; -. DR SMR; Q5F5A4; 6-130. DR PRIDE; Q5F5A4; -. DR EnsemblBacteria; AAW90633; AAW90633; NGO_2025. DR GeneID; 3282722; -. DR KEGG; ngo:NGO2025; -. DR PATRIC; 20337833; VBINeiGon24812_2440. DR HOGENOM; HOG000019802; -. DR KO; K02996; -. DR OMA; IKQGAAR; -. DR OrthoDB; EOG6MWNH0; -. DR BioCyc; NGON242231:GI2G-1926-MONOMER; -. DR Proteomes; UP000000535; 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_1000051265. SQ SEQUENCE 130 AA; 14380 MW; BE69A470F05BDD8B CRC64; MNGKYYYGTG RRKSSVARVF LTKGTGQIIV NGRPVDEFFA RETSRMVVRQ PLVLTENAES LDIKVNVVGG GETGQSGAIR HGITRALIDF DAALKPALSQ AGFVTRDARE VERKKPGLRK ARRAKQFSKR // ID RSMJ_NEIG1 Reviewed; 250 AA. AC Q5F7B7; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. 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=NGO1261; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89920.1; -; Genomic_DNA. DR RefSeq; WP_003689730.1; NC_002946.2. DR RefSeq; YP_208332.1; NC_002946.2. DR ProteinModelPortal; Q5F7B7; -. DR SMR; Q5F7B7; 2-250. DR EnsemblBacteria; AAW89920; AAW89920; NGO_1261. DR GeneID; 3282590; -. DR KEGG; ngo:NGO1261; -. DR PATRIC; 20335853; VBINeiGon24812_1481. DR HOGENOM; HOG000218236; -. DR KO; K15984; -. DR OMA; SSRYDIY; -. DR OrthoDB; EOG657J92; -. DR BioCyc; NGON242231:GI2G-1178-MONOMER; -. DR Proteomes; UP000000535; 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_0000212076. 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; 27316 MW; FC749D6B91985763 CRC64; MTDILIDDTA TEAVRTLIRA FPLVPVSQPP EQGSYLLAEH DTVSLRLVGE KSNVIVDFTS GAAQYRRTKG GGELIAKAVN HTAHPTVWDA TAGLGRDSFV LASLGLTVTA FEQHPAVACL LSDGIRRALL NPETQDTAAR INLHFGNAAE QMPALVKTQG KPDIVYLDPM YPERRKSAAV KKEMAYFHRL VGEAQDEVVL LHTARQTAKK RVVVKRPRLG EHLAGQAPAY QYTGKSTRFD VYLPYGADKG // ID RUVB_NEIG1 Reviewed; 343 AA. AC Q5F8L2; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. 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=NGO0760; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89475.1; -; Genomic_DNA. DR RefSeq; WP_003691202.1; NC_002946.2. DR RefSeq; YP_207887.1; NC_002946.2. DR ProteinModelPortal; Q5F8L2; -. DR SMR; Q5F8L2; 31-341. DR EnsemblBacteria; AAW89475; AAW89475; NGO_0760. DR GeneID; 3282478; -. DR KEGG; ngo:NGO0760; -. DR PATRIC; 20334668; VBINeiGon24812_0906. DR HOGENOM; HOG000218623; -. DR KO; K03551; -. DR OMA; YEPYLMQ; -. DR OrthoDB; EOG6SR93S; -. DR BioCyc; NGON242231:GI2G-715-MONOMER; -. DR Proteomes; UP000000535; 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_0000235381. FT NP_BIND 71 78 ATP. {ECO:0000255|HAMAP-Rule:MF_00016}. SQ SEQUENCE 343 AA; 37638 MW; C286F51F25DD7C9A CRC64; MLQTDNLTAA QPQRIVAAQT ASAQEELLER ALRPKTLDDY IGQHKAKEQL AIFIQAAKKR GEALDHVLLF GPPGLGKTTL AHIIAKELGV NLRQTSGPVL ERAGDLAALL TNLDPHDVLF IDEIHRLSPV VEEILYPALE DYRLDIMIGE GPAARSVKID LPPFTLVGAT TRAGMLTNPL RDRFGIVSRL EFYENRDLTT IVSRSAQLLQ LDMGEEGAME VAKRSRGTPR IANRLLRRVR DFADVKNNGV IDAAVADAAL SMLDVDAQGL DVMDRKFLEA VLHKFGGGPV GLDNVAAAIG ESTDTIEDVI EPYLIQQGFL QRTPRGRMAT ERAYLHFGLP VEK // ID RUVC_NEIG1 Reviewed; 178 AA. AC Q5FA76; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 09-DEC-2015, entry version 77. 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=NGO0153; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW88911.1; 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; AE004969; AAW88911.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003687445.1; NC_002946.2. DR RefSeq; YP_207323.2; NC_002946.2. DR ProteinModelPortal; Q5FA76; -. DR SMR; Q5FA76; 6-158. DR EnsemblBacteria; AAW88911; AAW88911; NGO_0153. DR GeneID; 3281312; -. DR KEGG; ngo:NGO0153; -. DR PATRIC; 20333229; VBINeiGon24812_0197. DR HOGENOM; HOG000012181; -. DR KO; K01159; -. DR OrthoDB; EOG6RG044; -. DR BioCyc; NGON242231:GI2G-141-MONOMER; -. DR Proteomes; UP000000535; 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_0000225154. 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; 18721 MW; 376D0685A8E41582 CRC64; MSATVRILGI DPGSRVTGFG IIDVRGRDHF YVASGCIKTP ADEPLADRIA VIVRHIGEVV AVYKPQQAAV EQVFVNVNPA STLMLGQARG AALAALVSHK LPVSEYTALQ VKQAVVGKGK AAKEQVQHMV VQMLGLSGTP QADAADGLAV ALTHALRNHG LAAKLNPSGM QVKRGRFQ // ID SECA_NEIG1 Reviewed; 916 AA. AC Q5F807; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382}; GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; GN OrderedLocusNames=NGO0996; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89680.1; -; Genomic_DNA. DR RefSeq; WP_003706354.1; NC_002946.2. DR RefSeq; YP_208092.1; NC_002946.2. DR ProteinModelPortal; Q5F807; -. DR SMR; Q5F807; 9-833. DR EnsemblBacteria; AAW89680; AAW89680; NGO_0996. DR GeneID; 3282574; -. DR KEGG; ngo:NGO0996; -. DR PATRIC; 20335196; VBINeiGon24812_1166. DR HOGENOM; HOG000218168; -. DR KO; K03070; -. DR OMA; IATERHE; -. DR OrthoDB; EOG654P48; -. DR BioCyc; NGON242231:GI2G-923-MONOMER; -. DR Proteomes; UP000000535; 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_0000320861. 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; 103203 MW; 4DFB10335D2D5CBD CRC64; MLTNIAKKIF GSRNDRLLKQ YRKSVARINA LEEQMQALSD ADLQAKTAEF KQRLADGQTL DGILPEAFAV CREASRRVLG MRHFDVQLIG GMVLHDGKIA EMRTGEGKTL VATLAVYLNA LAGKGVHVVT VNDYLASRDA GIMEPLYNFL GLTVGVIISD MQPFDRQNAY AADITYGTNN EFGFDYLRDN MVTDQYDKVQ RELNFAVVDE VDSILIDEAR TPLIISGQAD DNIQLYQIMN TVPPHLVRQE TEEGEGDYWV DEKAHQVILS ETGHEHAEQI LTQMGLLAEN DSLYSAANIS LMHHLMAALR AHSLFHKDQH YVIQDGEIVI VDEFTGRLMS GRRWSEGLHQ AVEAKEGVEI KRENQTLASI TFQNYFRLYT KLSGMTGTAD TEAFEFQSIY NLETVIIPTN RPVQRKDLND QIFRSAEEKF EAVVKDIEEC HKRGQPVLVG TTSIENSELV SRLLQKAGLP HNVLNAKEHE REALIVAQAG KVGAITVATN MAGRGTDIVL GGNLKHQTDA IRADETLSDE EKQAQIAALE NGWQAEHDKV MEAGGLHIIG TERHESRRID NQLRGRSGRQ GDPGSSRFYL SFEDPLLRLF ALDRAAAILN RLAPERGVAI EHNLLTRQIE GAQRKVEGRN FDMRKQVLEY DDVANEQRKV IYSQRNEILT SKDIGDLMQE IRSDAVSDLV DTYMPPDSME EQWDIPTLEN RLAAEFRLQE DIQSWLKADN AIDGQDIKER LIERIENEYA AKTELVGKQA MADFERNVML QAIDNQWREH LAAMDYLRQG IHLRSYAQKN PKQEYKREAF TMFQDLWNGI KFHIASLLTS VQIEQNPVAA VEEQPVGNIQ SIHSESPDIE ELLGQSQTDL VTEAFNPDGT DFSPEALEAR GQIVHRNDPC PCGSGLKYKQ CHGKLA // ID RUVA_NEIG1 Reviewed; 194 AA. AC Q5F636; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO1730; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90351.1; -; Genomic_DNA. DR RefSeq; WP_003689924.1; NC_002946.2. DR RefSeq; YP_208763.1; NC_002946.2. DR ProteinModelPortal; Q5F636; -. DR EnsemblBacteria; AAW90351; AAW90351; NGO_1730. DR GeneID; 3281203; -. DR KEGG; ngo:NGO1730; -. DR PATRIC; 20337058; VBINeiGon24812_2069. DR HOGENOM; HOG000057116; -. DR KO; K03550; -. DR OMA; VGYQVHC; -. DR OrthoDB; EOG679THG; -. DR BioCyc; NGON242231:GI2G-1626-MONOMER; -. DR Proteomes; UP000000535; 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_0000224884. SQ SEQUENCE 194 AA; 20730 MW; 14F3D2BD6DBAC5E2 CRC64; MISRLTGKLV EKNPPQIVID VNGVGYEADV SMQTFYNLPP VGESVQLFTQ LIIREDAHLL FGFATAEERK TFRQLIKVGG IGAKTALGIL SAMTADELAR AVAEEDVKRL SSAPGIGKKT AERMVLELRG KLVAHTVTDG LFAASPAADE TEDIVSTLLA LGYNEREAKA AVKGVPKGTD VGEGVRLALK NLLK // ID SERC_NEIG1 Reviewed; 368 AA. AC Q5F7A0; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO1283; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89937.1; -; Genomic_DNA. DR RefSeq; WP_003695923.1; NC_002946.2. DR RefSeq; YP_208349.1; NC_002946.2. DR ProteinModelPortal; Q5F7A0; -. DR EnsemblBacteria; AAW89937; AAW89937; NGO_1283. DR GeneID; 3282008; -. DR KEGG; ngo:NGO1283; -. DR PATRIC; 20335907; VBINeiGon24812_1508. DR HOGENOM; HOG000088965; -. DR KO; K00831; -. DR OMA; GAQKNMG; -. DR OrthoDB; EOG60CWP3; -. DR BioCyc; NGON242231:GI2G-1195-MONOMER; -. DR UniPathway; UPA00135; UER00197. DR UniPathway; UPA00244; UER00311. DR Proteomes; UP000000535; 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_0000150190. 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; 41294 MW; AA458E96016B0D60 CRC64; MSLYPIYNFS AGPAVLPEAV LRTAQQEMSD YNGTGFSVME MSHRSEMFLS ILHHAEQDLR QLLKVPDNYK ILFLQGGATT QFNMAAMNLA HGFRTADAVV TGNWSRIAYE QMSRLTDTEI RLAAHGGEQF DYLDLPPVET WDVAPDSAFV HFAVNETVNG LQYREVPRLS DGMPPLVCDM SSEILSREFD VADYGLIYAG AQKNIGPAGV TVVIVREDLL ERCPNDIPDV FNYRSHLNRD GMYNTPSTYA IYMSGLVFRW LQAQGGVKKI EAVNRLKAQT LYETIDGSGG FYINDIHPDA RSKMNVVFKT ASEDLDRRFV LEAELQGLCL LKGYKSVGGM RASIYNAMPL EGVRALADFM RDFQRRYG // ID SECB_NEIG1 Reviewed; 147 AA. AC Q5FAB1; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821}; GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; GN OrderedLocusNames=NGO0116; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88876.1; -; Genomic_DNA. DR RefSeq; WP_003687381.1; NC_002946.2. DR RefSeq; YP_207288.1; NC_002946.2. DR ProteinModelPortal; Q5FAB1; -. DR PRIDE; Q5FAB1; -. DR EnsemblBacteria; AAW88876; AAW88876; NGO_0116. DR GeneID; 3282400; -. DR KEGG; ngo:NGO0116; -. DR PATRIC; 20333133; VBINeiGon24812_0150. DR HOGENOM; HOG000218192; -. DR KO; K03071; -. DR OMA; CPNVLFP; -. DR OrthoDB; EOG6DVJZZ; -. DR BioCyc; NGON242231:GI2G-105-MONOMER; -. DR Proteomes; UP000000535; 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_0000055386. SQ SEQUENCE 147 AA; 16333 MW; AD16FB4BCED1E558 CRC64; MSEELQPVFS IERLYVKDLS LEVPHAPQIF LEQGDPEVDM RVSTGSQKLE DGYYDVDVTV TVTAKLDNER TMFLNEVTQS GIFRLENIPE EDVQLLLGVA CPNILFPYAR EAVSGTVTRA GFPPVLLAPI NFEAIYQQQQ EAEAAGA // ID SMG_NEIG1 Reviewed; 153 AA. AC Q5F5Q3; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE RecName: Full=Protein Smg homolog {ECO:0000255|HAMAP-Rule:MF_00598}; GN Name=smg {ECO:0000255|HAMAP-Rule:MF_00598}; OrderedLocusNames=NGO1864; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90484.1; -; Genomic_DNA. DR RefSeq; WP_003690120.1; NC_002946.2. DR RefSeq; YP_208896.1; NC_002946.2. DR EnsemblBacteria; AAW90484; AAW90484; NGO_1864. DR GeneID; 3282390; -. DR KEGG; ngo:NGO1864; -. DR PATRIC; 20337422; VBINeiGon24812_2242. DR HOGENOM; HOG000137865; -. DR KO; K03747; -. DR OMA; HWSTGIE; -. DR OrthoDB; EOG6X6RDW; -. DR BioCyc; NGON242231:GI2G-1768-MONOMER; -. DR Proteomes; UP000000535; 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_0000209173. SQ SEQUENCE 153 AA; 17047 MW; 5EEF256F0FE7C816 CRC64; MTEVIAYLIE HFQDFDTCPP PEDLGMLLEE AGFDTMEIGN TLMMMEVLLN SSEFSAEPAG SGALRVYSKE ETDNLPQEVM GLMQYLIEEK AVSCEQREII IHALMHIPGD EITVDTAKVL TLLLLWANKS ELPVLVGDEL MSALLLDNKP TMN // ID SLYX_NEIG1 Reviewed; 74 AA. AC Q5F5B2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE RecName: Full=Protein SlyX homolog {ECO:0000255|HAMAP-Rule:MF_00715}; GN Name=slyX {ECO:0000255|HAMAP-Rule:MF_00715}; GN OrderedLocusNames=NGO2017; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90625.1; -; Genomic_DNA. DR RefSeq; WP_003686929.1; NC_002946.2. DR RefSeq; YP_209037.1; NC_002946.2. DR EnsemblBacteria; AAW90625; AAW90625; NGO_2017. DR GeneID; 3282695; -. DR KEGG; ngo:NGO2017; -. DR PATRIC; 20337817; VBINeiGon24812_2432. DR HOGENOM; HOG000273046; -. DR KO; K03745; -. DR OMA; EGLECRI; -. DR OrthoDB; EOG6WT8KM; -. DR BioCyc; NGON242231:GI2G-1918-MONOMER; -. DR Proteomes; UP000000535; 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_0000227069. SQ SEQUENCE 74 AA; 8679 MW; 7141CFE5AD724F5A CRC64; MDAVQELERR IVELEIQTAL QEDVISGLNA MVAELRQTLD LQQAQLRLLY QKMQDRNPDA QEPYSLRDEI PPHY // ID SSRP_NEIG1 Reviewed; 148 AA. AC Q5F816; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 16-MAR-2016, entry version 74. 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=NGO0986; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89671.1; 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; AE004969; AAW89671.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q5F816; -. DR EnsemblBacteria; AAW89671; AAW89671; NGO_0986. DR PATRIC; 20335174; VBINeiGon24812_1156. DR HOGENOM; HOG000009628; -. DR OrthoDB; EOG6HXJ9P; -. DR BioCyc; NGON242231:GI2G-913-MONOMER; -. DR Proteomes; UP000000535; 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_0000102992. SQ SEQUENCE 148 AA; 17193 MW; B80FDCF5661B6A1C CRC64; MAIANNKKAF HDFFIEDRIE AGLVLEGWEV KAIRAARVQL KESYIYWKKD AFYLVGCHIT ALPTASTHIK PDAVRPRKLL LKQSEINKLI GKTERAGYTI VPLDLHFSRG KIKMEIGLAK GKKQHDKRQS MKEADWKREK QRLIKHTR // ID SPEB_NEIG1 Reviewed; 307 AA. AC Q5F6R3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO1486; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90124.1; -; Genomic_DNA. DR RefSeq; WP_003689368.1; NC_002946.2. DR RefSeq; YP_208536.1; NC_002946.2. DR ProteinModelPortal; Q5F6R3; -. DR EnsemblBacteria; AAW90124; AAW90124; NGO_1486. DR GeneID; 3281617; -. DR KEGG; ngo:NGO1486; -. DR PATRIC; 20336423; VBINeiGon24812_1759. DR HOGENOM; HOG000204320; -. DR KO; K01480; -. DR OMA; YELTTIM; -. DR OrthoDB; EOG6R2GW5; -. DR BioCyc; NGON242231:GI2G-1390-MONOMER; -. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000000535; 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_0000173734. 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; 33966 MW; 17311EED7B5B9DDA CRC64; MQYSTLAGQT DNSLVSNNFG FLRLPLNFMP YESHADWVIT GVPYDMAVSG RSGARFGPEA IRRASVNLAW EHRRFPWTFD VRERLNIIDC GDLVFSFGDS RDFVEKMEAH AGKLLSFGKR CLSLGGDHFI TLPLLRAHAR YFGKLALIHF DAHTDTYDNG SEYDHGTMFY TAPKEGLIDP SRSVQIGIRT EHSKKLPFTV LSAPKVNEDS VEETVRKIKE TVGNMPVYLT FDIDCLDPSF APGTGTPVCG GLSSDRALKI LRGLTDLDIV GMDVVEVAPS YDQSDITALA GATIALEMLY LQGAKKD // ID SYA_NEIG1 Reviewed; 874 AA. AC Q5F7C4; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO1254; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89913.1; -; Genomic_DNA. DR RefSeq; WP_010951224.1; NC_002946.2. DR RefSeq; YP_208325.1; NC_002946.2. DR ProteinModelPortal; Q5F7C4; -. DR SMR; Q5F7C4; 1-460. DR EnsemblBacteria; AAW89913; AAW89913; NGO_1254. DR GeneID; 3281829; -. DR KEGG; ngo:NGO1254; -. DR PATRIC; 20335843; VBINeiGon24812_1476. DR HOGENOM; HOG000156964; -. DR KO; K01872; -. DR OMA; FSITDGQ; -. DR OrthoDB; EOG6Q2SQ2; -. DR BioCyc; NGON242231:GI2G-1171-MONOMER; -. DR Proteomes; UP000000535; 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_0000075159. 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; 95927 MW; B5248B2696CC5610 CRC64; MKTSELRQKF LKFFETKGHT VVRSSSLVPH DDPTLLFTNA GMNQFKDVFL GFDKRPYSRA TTAQKCVRAG GKHNDLENVG YTARHHTFFE MMGNFSFGDY FKRDAIHFAW EFLTSPEWLN IPKDKLLATV YAEDDEAYNI WLNEIGMPSE RIVRIGDNKG AKYASDNFWQ MGDTGPCGPC SEIFYDHGKE IWGGIPGSPE EDGDRWIEIW NCVFMQFNRD EQGNMNPLPK PSVDTGMGLE RMAAVMQHVH SNYEIDLFQD LLKAVARETG APFSMEEPSL KVIADHIRSC SFLIADGVLP SNEGRGYVLR RIIRRAVRHG YKLGQSKPFF HKLVADLVQE MGGAYPELKE KQAQIEEALK NEESRFAQTL ETGMALLENA LAKGGKTLGG EIIFKLYDTY GFPYDLTADI CRERNIEPDE AGFEREMEAQ RARARAAQSF KANAQLPYDG QDTEFKGYSE RQTESKVLAL YKDGEQVVEL NEGDSGAVVI DFTPFYAESG GQVGDVGYIF AGENRFEVRD TQKIKAAVFG QFGVQTSGRL KVGDSITAKV DDEIRNANMR NHSATHLMHK ALRDVLGGHV EQKGSLVTAE STRFDISHPQ AVTAEEIAEV ERRVNEAILA NVAVNAAIMS MEDAQKTDAM MLFGEKYGDE VRVLQMGGFS TELCGGTHVS RTGDIGLFKI ISEGGIAAGV RRIEAITGLN ALKWAQEQER LVKDIIAETK AQTEKDVLAK IQAGAAHAKA LEKELARAKA ELAVHAGAKL LDDAKDLGAA KLVAAQIEAD AAALRETVTD LTGKSDNAVI LLAAVNEGKV SLCAGVSKAL TGKVKAGDLV KFAAEQVGGK GGGRPDLAQA GGTDADKLPE MLASAEGWLC QKLS // ID SSTT_NEIG1 Reviewed; 409 AA. AC Q5F5G9; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO1957; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90568.1; -; Genomic_DNA. DR RefSeq; WP_002215131.1; NC_002946.2. DR RefSeq; YP_208980.1; NC_002946.2. DR ProteinModelPortal; Q5F5G9; -. DR EnsemblBacteria; AAW90568; AAW90568; NGO_1957. DR GeneID; 3282664; -. DR KEGG; ngo:NGO1957; -. DR PATRIC; 20337661; VBINeiGon24812_2357. DR HOGENOM; HOG000218252; -. DR KO; K07862; -. DR OMA; WIINVAP; -. DR OrthoDB; EOG63Z78S; -. DR BioCyc; NGON242231:GI2G-1858-MONOMER; -. DR Proteomes; UP000000535; 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_0000309099. 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 292 312 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 319 339 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. FT TRANSMEM 365 385 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01582}. SQ SEQUENCE 409 AA; 41929 MW; 0CBBB3AEA737D322 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 KIRRNPYPLV FTCLRESGVY AFFTRSSAAN IPVNMALAKK LGLHEDTYSI SIPLGATVNM GGAAITITVL AMAAAHTQGI QVDFATALLL SLVATVSACG ASGVAGGSLL LIPLACSLFG ISNDVAMQVV AVGFIIGVIQ DSAETALNSS TDVLFTAAAD LGRQRNRAE // ID SYC_NEIG1 Reviewed; 473 AA. AC Q5F5D6; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 78. 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=NGO1993; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90601.1; -; Genomic_DNA. DR RefSeq; WP_010355798.1; NC_002946.2. DR RefSeq; YP_209013.1; NC_002946.2. DR ProteinModelPortal; Q5F5D6; -. DR SMR; Q5F5D6; 1-414. DR EnsemblBacteria; AAW90601; AAW90601; NGO_1993. DR GeneID; 3282631; -. DR KEGG; ngo:NGO1993; -. DR PATRIC; 20337755; VBINeiGon24812_2404. DR HOGENOM; HOG000245250; -. DR KO; K01883; -. DR OMA; HENEACQ; -. DR OrthoDB; EOG6RVFXC; -. DR BioCyc; NGON242231:GI2G-1891-MONOMER; -. DR Proteomes; UP000000535; 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_0000240924. 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; 52804 MW; 43042DFF3BD373E8 CRC64; MTAIYNTLTR QKEPFAPIDP ENVRMYVCGM TVYDYCHLGH ARVMVVFDMI ARWLRECGYP LTYVRNITDI DDKIIARAAE NGETIGELNA RFIQAMHEDA DALGVLRPDI EPKATENIPQ MIAMIETLIQ NGKAYPAANG DVYYAVREFA AYGQLSGKSL DDLRAGERVE VDGFKRDPLD FVLWKAAKAG EPAWESPWGN GRPGWHIECS AMSENLFGDT FDIHGGGADL QFPHHENEIA QSVGASGHTC GHDHAQTHHG QSIASHVKYW LHNGFIRVDG EKMSKSLGNF FTIREVLKQY DPEVVRFFIL RAHYRSPLNY SDAHLDDAKG ALTRLYTTLK NTPAAEFDLS ENANGYTRRF YAAMNDDFGT VEAVAVLFEL AGEVNKTNDA HLAGCLKALG GIIGLLQRNP IEFLQGGAVS DGLSNEEIED LIARRKQARA DKNWAESDRI RDLLNEHKII LEDSAGGTTW RRG // ID SURE_NEIG1 Reviewed; 248 AA. AC Q5F7V9; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. 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=NGO1058; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89728.1; -; Genomic_DNA. DR RefSeq; WP_010951167.1; NC_002946.2. DR RefSeq; YP_208140.1; NC_002946.2. DR ProteinModelPortal; Q5F7V9; -. DR EnsemblBacteria; AAW89728; AAW89728; NGO_1058. DR GeneID; 3281758; -. DR KEGG; ngo:NGO1058; -. DR PATRIC; 20335348; VBINeiGon24812_1240. DR HOGENOM; HOG000122500; -. DR KO; K03787; -. DR OMA; NLNIPPC; -. DR OrthoDB; EOG68WR45; -. DR BioCyc; NGON242231:GI2G-973-MONOMER; -. DR Proteomes; UP000000535; 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_0000235627. 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; 27057 MW; 16CA6A2CECD221A2 CRC64; MNVLISNDDG YLAEGIAILA RVASEFANVR VVAPERDRSG VSNSVTLDRP LQLKQAQNGF YYVNGTPTDC IHVGQFALPD FKPDVVFSGI NRGANMGDDT LYSGTVAAAT EAYLMGMPAV AFSLNDASGR YWATAEKALW TLLAHFFKKP PSAPVLWNVN IPAVAPEDVR GIKITRLGRR HHEQNIVPSR NPRGEQIYWI GPVGEVSDRE EGTDFGECGA GFITVTPLQI DLTAYPDMAE TAAFWHTD // ID SUCC_NEIG1 Reviewed; 388 AA. AC Q5F878; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. 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=NGO0913; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89609.1; -; Genomic_DNA. DR RefSeq; WP_003701280.1; NC_002946.2. DR RefSeq; YP_208021.1; NC_002946.2. DR ProteinModelPortal; Q5F878; -. DR SMR; Q5F878; 1-386. DR PRIDE; Q5F878; -. DR EnsemblBacteria; AAW89609; AAW89609; NGO_0913. DR GeneID; 3281695; -. DR KEGG; ngo:NGO0913; -. DR PATRIC; 20335009; VBINeiGon24812_1074. DR HOGENOM; HOG000007059; -. DR KO; K01903; -. DR OMA; YIESGCD; -. DR OrthoDB; EOG644ZT0; -. DR BioCyc; NGON242231:GI2G-851-MONOMER; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000000535; 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_1000082137. 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; 41308 MW; E036CE9E2233435A CRC64; MNLHEYQAKE LLASYGLPVQ GGILAHNGEE AAAAYDKLGG KFAVVKAQVH AGGRGKAGGV KVVKSREKAK EVAESLIGTN LVTYQTDANG QPVNSVLVCE DMYPVQTELY LGAVVDRSTR RVTFMASTEG GVEIEKVAAE TPEKIFKVTV DPLVGLQPCQ AREVAFQLGL KDKQINEFAK LMTGAYKAFV ENDFALFEVN PLAVRENGAL ACVDGKIGID SNALYRLPKI AELRDKSQEN ERELKASEFD LNYVALEGKI GCMVNGAGLA MATMDIIKLK GGQPANFLDV GGGATKDRVV EAFKLILEDK SVKGVLINIF GGIVRCDMIA EAIVAAVKEI NVNVPVVVRL EGNNAELGAK ILNESGLKLT SADGLNDAAE KIVAAVNA // ID SYH_NEIG1 Reviewed; 431 AA. AC Q5F9G8; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO0426; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89169.1; -; Genomic_DNA. DR RefSeq; WP_003696863.1; NC_002946.2. DR RefSeq; YP_207581.1; NC_002946.2. DR ProteinModelPortal; Q5F9G8; -. DR EnsemblBacteria; AAW89169; AAW89169; NGO_0426. DR GeneID; 3282181; -. DR KEGG; ngo:NGO0426; -. DR PATRIC; 20333865; VBINeiGon24812_0510. DR HOGENOM; HOG000018072; -. DR KO; K01892; -. DR OMA; CGGGNFK; -. DR OrthoDB; EOG6BPDH4; -. DR BioCyc; NGON242231:GI2G-404-MONOMER; -. DR Proteomes; UP000000535; 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_0000136208. SQ SEQUENCE 431 AA; 48342 MW; 97ED66F818D1B259 CRC64; MAQKIQSVKG MNDLLPVGQK DFKLTAVFWQ AFEDTVNRWT RAYGYQQIRT PIVEQTGLFV RSIGEETDVV GKEMYTFSDS NDSLSLSLRP EGTASCLRAV VEHNLLYNSP QKLWYMGPMF RRERPQKGRY RQFHQVGIEA LGFEGPDIDA EIIAMSADLW EKLGIREYLT LEINSLGNRE ERAAHRAALV EYLTRYEAQL DEDSKRRLKT NPLRVLDTKN PDLQEICNAA PRLVDYLGEA SQNHYARFKA MLDGLGIQYI ENSRLVRGLD YYNQTVFEWT TDKLGAQATV CGGGRYDGLI EELGGKPAPS IGFAMGIERL LLLVSEYGSL EVNAAPDVYA MHQGEGADLQ VMKYAQALRA QGFNVIQHSG YQSLKAQMKK ADNSGARFAL IVAQDELADG TVTLKDMNGA HGQQTVSATD LTDTLQQWKN A // ID SYI_NEIG1 Reviewed; 929 AA. AC Q5FAF5; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. 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=NGO0069; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88832.1; -; Genomic_DNA. DR RefSeq; WP_003699451.1; NC_002946.2. DR RefSeq; YP_207244.1; NC_002946.2. DR ProteinModelPortal; Q5FAF5; -. DR EnsemblBacteria; AAW88832; AAW88832; NGO_0069. DR GeneID; 3282308; -. DR KEGG; ngo:NGO0069; -. DR PATRIC; 20333002; VBINeiGon24812_0085. DR HOGENOM; HOG000246402; -. DR KO; K01870; -. DR OMA; PIPFFLH; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; NGON242231:GI2G-61-MONOMER; -. DR Proteomes; UP000000535; 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_0000098427. 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; 104224 MW; D90218720A650D5E CRC64; MTDYSKTVNL LESPFPMRGN LAKREPAWLK SWYEQKRYQK LREIAKGRPK FILHDGPPYA NGDIHIGHAV NKILKDIIIR SKTQAGFDAP YVPGWDCHGL PIEVMVEKLH GKDMPKARFR ELCREYAAEQ IARQKKDFIR LGVLGDWDNP YLTMDFKTEA DTVRMLGEIY KSGYLYRGAK PVQFCLDCGS SLAEAEVEYK DKVSPAIDVA YPFKNTVALA AAFGLAGIEG KAFAVIWTTT PWTLPASQAV SAGADVVYQL IDTPKGKLVL AKDLAEGALK RYGFSDGIAI LAETTGDKLE NLHMNHPFLE RDIPMLNGEH VTTDAGTGLV HTAPAHGLED YAVCNKYGIE LYNPVNAEGK YISETPRVAG MSVWEANPVI LQWPEETGNL LASSKIEHSY AHCWRHKTPL IYRATGQWFV GMDKAGSDGK TLRDKAIKAV DDTEFFPPWG RARLESMIEG RPDWVVSRQR YWGTPMTFFV HKETGELHPN SAELLEKVAQ RIEEKGIEAW FSLDKSELLS AEDCEHYDKL PDTMDVWFDS GSTHYSVVKQ REELEWPADL YLEGSDQHRG WFQSSMLTGC ASSMGRAPYK QLLTHGFVVD QNGRKMSKSI GNVVAPQEVY NEFGADILRL WAASTDYSGE LAISKEILKR VTESYRRIRN TLSFLFANLS DFNPIEDAVQ QADMVEIDRY ALVLARRLQE RLAGGYYPRY AFHFAVKDIV SFCSEDLGAF YLDILKDRLY TTKADSRARR SAQTALYHIT RSLVLLIAPI LCFTGEEAWD IIGGGEEDSV LFHTWHEFPA INEKAEAELV KKWTAIREAR EAVTAAIEPL RADKTVGSSL QAEAEITAPE EMAGYLNALG EELRFALLVS KAEVKVGDEL AVAAKASDGE KCERCWHYTR DVGAVAGYET VCKRCAENVG GEGETRHYA // ID SYL_NEIG1 Reviewed; 876 AA. AC Q5FAJ3; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 13-APR-2016, entry version 98. 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=NGO0006; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SEQUENCE CAUTION: CC Sequence=AAW88778.1; 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; AE004969; AAW88778.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_025456399.1; NC_002946.2. DR RefSeq; YP_207190.2; NC_002946.2. DR ProteinModelPortal; Q5FAJ3; -. DR EnsemblBacteria; AAW88778; AAW88778; NGO_0006. DR GeneID; 3283053; -. DR KEGG; ngo:NGO0006; -. DR PATRIC; 20332842; VBINeiGon24812_0007. DR HOGENOM; HOG000200747; -. DR KO; K01869; -. DR OrthoDB; EOG63Z74X; -. DR BioCyc; NGON242231:GI2G-5-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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_0000334780. 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; 98049 MW; E2B73DC55263D03E CRC64; MQEHYQPAAI EPAAQKKWDD ARISNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID WEREVATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS KQGLEGDYAK FLQVYTTRPD TLMGATYVAV AAEHPLATAA AADKPELQAF IAECKAGSVA EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK YNLPKKQVIA VGDNAFDANR WQEWYGDKEN GVLVNSGDLD GLDFQTAFDA VAAKLQSQGA GEPKTQYRLR DWGISRQRYW GCPIPIVHCE KCGDVPVPAD QLPVVLPENV VPDGMGSPLA KMPEFYETSC PCCGGAAKRE TDTMDTFMES SWYFFRYMSP KFSDGMVSAE SAKYWGAVDQ YIGGIEHAIL HLLYARFFTK LMRDEGLVNV DEPFERLLTQ GMVVCETYYR ENDKGGKDWI NPADVELTFD DKGRPVSAVL KADGLPVVIS GTEKMSKSKN NGVDPQELIN AYGADTARLF MMFAAPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYLKQGG AVKAFAGNQD GLSKELKDLR HKLHSTTAKV SDDYGRRQQF NTAIAAVMEL LNQYDKTDTG SEQGRAVAQE VLEAAVRLLW PIVPHICETL WSELNGAKLW EAGWPTVDEA ALVKSEIEVM VQVNGKLRGK ITVAADASKA DLEAAALANE GAVKFMEGKP AKKIIVVPGR LVNIVV // ID SYFB_NEIG1 Reviewed; 787 AA. AC Q5F9T6; DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283}; DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00283}; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00283}; DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00283}; GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00283}; GN OrderedLocusNames=NGO0304; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000255|HAMAP- CC Rule:MF_00283}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00283}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP- CC Rule:MF_00283}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00283}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00283}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00283}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000255|HAMAP- CC Rule:MF_00283}. CC -!- SIMILARITY: Contains 1 FDX-ACB domain. {ECO:0000255|HAMAP- CC Rule:MF_00283}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00283}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89051.1; -; Genomic_DNA. DR RefSeq; WP_003687684.1; NC_002946.2. DR RefSeq; YP_207463.1; NC_002946.2. DR ProteinModelPortal; Q5F9T6; -. DR EnsemblBacteria; AAW89051; AAW89051; NGO_0304. DR GeneID; 3281687; -. DR KEGG; ngo:NGO0304; -. DR PATRIC; 20333589; VBINeiGon24812_0374. DR HOGENOM; HOG000292085; -. DR KO; K01890; -. DR OMA; MKFSEQW; -. DR OrthoDB; EOG6CCH1J; -. DR BioCyc; NGON242231:GI2G-284-MONOMER; -. DR Proteomes; UP000000535; 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_0000126917. FT DOMAIN 39 149 tRNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_00283}. FT DOMAIN 400 475 B5. {ECO:0000255|HAMAP-Rule:MF_00283}. FT DOMAIN 694 786 FDX-ACB. {ECO:0000255|HAMAP- FT Rule:MF_00283}. FT METAL 453 453 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00283}. FT METAL 459 459 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00283}. FT METAL 462 462 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00283}. FT METAL 463 463 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00283}. SQ SEQUENCE 787 AA; 85989 MW; C80D9B4D4464B2D1 CRC64; MQFSYSWLKT QANPDLSADK LEHLLTMAGL EVEEIDTAAP AFSGVVVAEV KSVEKHPDAD RLNVTQVDAG TGELVQIVCG APNVKPGIKV PCSLPVAVLP GNFKIKPTKM RGVPSNGMLC STNELGLPDD GVDGLHILPE DAPVGTNIRE YLDLDDMLFT LKITPNRADC LSVKGIAREV SALTQCAFTP VEIQTAPIGS EKKQAVRIDA PADCGRFISR VIENVNAKAA TPDWMKQRLE RSGIRSISAL VDIGNYVMLE IGQPMHVFDA DKLSGSLIVR RAQNGETLAC LNEKTVTLAD NTLVVADEKG ALSLAGLMGG AASAVSDGTQ NIVLEAAWFE PEIIVGKSRQ YGFGSDSSFR FERGVDYRLQ ADAIERATEL VLQICGGAAG EMVEAQGKLP EAKQVGLRLG RLKTVLGVDI PAEQVETILQ HLGLQPEKTA EGFRITAPSF RFDIEIEADL IEEIGRVYGY ENIPDDYTSG RLKMSELPET RRPRFAVYNE MAARGYREVI SYAFVDEQWE LDFAANAAPI RLQNPLAAQY AVMRSTLIGG LVEILQNNLN RKQNRVRVFE IACVFGKGSD GRFVQNERIG GLWYGAAMPE QWGEKTRNAD FYDIKADVEN LLKNKAVEFV KTGHPALHPG RAANIVSDGK VIGFVGELHP KWLQKYDLPQ APLVFEIDMA AVLECGKTRY RAVSKFQPVR RDLAFVMPEV MNHDDLLLVL KGAANKLVQE ISVFDVYRGT GLPEGMKSVA VKVILQDMEN TLTDEAVEPL IGKLIGVATE AGARLRS // ID SYGA_NEIG1 Reviewed; 298 AA. AC Q5F4Y8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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=NGO2153; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90749.1; -; Genomic_DNA. DR RefSeq; WP_003692424.1; NC_002946.2. DR RefSeq; YP_209161.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y8; -. DR SMR; Q5F4Y8; 2-286. DR EnsemblBacteria; AAW90749; AAW90749; NGO_2153. DR GeneID; 3282769; -. DR KEGG; ngo:NGO2153; -. DR PATRIC; 20338157; VBINeiGon24812_2601. DR HOGENOM; HOG000264291; -. DR KO; K01878; -. DR OMA; LGSYYQF; -. DR OrthoDB; EOG661H9S; -. DR BioCyc; NGON242231:GI2G-2043-MONOMER; -. DR Proteomes; UP000000535; 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 1 298 Glycine--tRNA ligase alpha subunit. FT /FTId=PRO_1000047449. SQ SEQUENCE 298 AA; 33996 MW; 6D151C79672D1E39 CRC64; MLTFQQIIFK LQTFWADKGC TVIQPFDMEV GAGTSHPATC LRALGPEPWF AAYVQPSRRP KDGRYGDNPN RLQHYYQFQV ALKPAPANIQ DLYLDSLREL GIDPKVHDIR FVEDDWENPT LGAWGLGWEV WLNGMEVTQF TYFQQVGGID CTPVLGEITY GIERLAMYLQ GVENVYDLVW AKTPDGNTVS YGDVYHQNEV EQSTYNFEYS DADWLLRQFN DYEAQAKRLF AEENAGLALP AYELVLKAGH TFNLLDARGA ISVTERATYI GRIRALSRAV AQKYIESREK LGFPLIKK // ID SYFA_NEIG1 Reviewed; 329 AA. AC Q5F9U0; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 09-DEC-2015, entry version 77. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281}; DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00281}; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00281}; DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00281}; GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00281}; GN OrderedLocusNames=NGO0299; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000255|HAMAP- CC Rule:MF_00281}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00281}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP- CC Rule:MF_00281}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00281}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00281}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00281}. CC -!- SEQUENCE CAUTION: CC Sequence=AAW89047.1; 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; AE004969; AAW89047.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_010951025.1; NC_002946.2. DR RefSeq; YP_207459.2; NC_002946.2. DR ProteinModelPortal; Q5F9U0; -. DR EnsemblBacteria; AAW89047; AAW89047; NGO_0299. DR GeneID; 3281671; -. DR KEGG; ngo:NGO0299; -. DR PATRIC; 20333583; VBINeiGon24812_0371. DR HOGENOM; HOG000242675; -. DR KO; K01889; -. DR OrthoDB; EOG6WX4QN; -. DR BioCyc; NGON242231:GI2G-280-MONOMER; -. DR Proteomes; UP000000535; 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 1 329 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000231998. FT METAL 254 254 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00281}. SQ SEQUENCE 329 AA; 37221 MW; 93B12A4F95F247FF CRC64; MENVNRIVAE GIAAVEAAQD FNALEQIKAR YLGKTGELTG LLKTLGQMSP EERKTIGAHI NECKNRFQTA FNAKRDALNE AKLQARLAAE ALDITLPGRA QEGGSLHPVT LTLQRVVELF HGMGFEVADG PEIEDDFHNF QALNIPANHP ARAMQDTFYV ENGDVLRTHT SPIQIRYMLD KKEPPIRIIA PGRVYRVDSD ATHSPMFHQA EGLWVEEGVT FADLKAVFTD FIRRFFERDD LQVRFRPSFF PFTEPSAEID IMGENGKWLE VGGCGMVHPN VLKNVNIDPE KYTGFAFGIG LDRFAMLRYN VNDLRLFFDN DLNFLKQFE // ID SYGB_NEIG1 Reviewed; 687 AA. AC Q5F4Y7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 84. 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=NGO2154; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90750.1; -; Genomic_DNA. DR RefSeq; WP_010951416.1; NC_002946.2. DR RefSeq; YP_209162.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y7; -. DR EnsemblBacteria; AAW90750; AAW90750; NGO_2154. DR GeneID; 3282768; -. DR KEGG; ngo:NGO2154; -. DR PATRIC; 20338159; VBINeiGon24812_2602. DR HOGENOM; HOG000264302; -. DR KO; K01879; -. DR OMA; LPIPKRM; -. DR OrthoDB; EOG661H9S; -. DR BioCyc; NGON242231:GI2G-2044-MONOMER; -. DR Proteomes; UP000000535; 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_1000101306. SQ SEQUENCE 687 AA; 74451 MW; BE39A8066422A986 CRC64; MTTQTLLIEL LTEELPPKAL NNLGNHFAAS VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV KNVKAVQADQ KIVKKGPAVA NAVKDGTPTK ALEGFARGAG AKIEDLTIVH DGRQDVYAYE YVQTGRPLGG LLENIINQAV KKLPIPKVMR WGSSTFTFVR PVHGLIVLHG GDVVNVSVLG LQSGNQTLGH RFLSDGEIII ENADSYAAQM RGQGKVVASF AGRKAAIQTA LEGQARRLNA TVAADEALLD EVTALVEWPV VLEAGFEEHF LAVPQECLIL TMQQNQKYFP LLDQNGKLMN RFLLVSNLQT EDPSHIIRGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL ANVVYHNKIG SQAERIERLQ SIAAHIAKAL GADAAAAERA ARLAKADLVT EMVGEFPELQ GTMGKYYARL DGETEEIAEA IEQHYQPRFA GDKLPESKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA LRRAALGILR MLMQYGLDVN ELIQTAFDSF PQGLLNEKTP SETADFMQAR LAVLLQNDYP QDIVAAVLAK QPRRLDDLTA KLQAVAVFKQ LPEAAALAAA NKRVQNLLKK ADAELGAVNE SLLQQDEEKA LYAAAQGLQP KIAAAVAEGN FQTALSELAS VKPQVDAFFD GVMVMAEDAA VKQNRLNLLN RLAGQMNAVA DIALLGE // ID SYR_NEIG1 Reviewed; 572 AA. AC Q5F835; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO0963; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89652.1; -; Genomic_DNA. DR RefSeq; WP_010951154.1; NC_002946.2. DR RefSeq; YP_208064.1; NC_002946.2. DR ProteinModelPortal; Q5F835; -. DR DNASU; 3282609; -. DR EnsemblBacteria; AAW89652; AAW89652; NGO_0963. DR GeneID; 3282609; -. DR KEGG; ngo:NGO0963; -. DR PATRIC; 20335116; VBINeiGon24812_1127. DR HOGENOM; HOG000247212; -. DR KO; K01887; -. DR OMA; KLVGNYY; -. DR OrthoDB; EOG6JB13C; -. DR BioCyc; NGON242231:GI2G-894-MONOMER; -. DR Proteomes; UP000000535; 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_0000242053. FT MOTIF 122 132 "HIGH" region. SQ SEQUENCE 572 AA; 62620 MW; B69F0239F7253087 CRC64; MNLHQTVEHE AAAAFAAAGI AGSPVVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK VADALAGNAV IESAEVAGPG FINLRLRHEF LAQNIHAALN DARFGVAKTA QPQTVVIDYS SPNLAKEMHV GHLRSSIIGD SISRVLEFTG NTVIRQNHVG DWGTQFGMLV AYLVEQQKDN AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA VYDTLGLKLR PEDVAGESKY NDDLQPVADD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA FIVQKQGGGF LYASTDLACL RYRIGRLKAG RLLYVVDHRQ ALHFEQLFTT SRKAGYLPED AKAEFIGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA TALVKEKNPE LGADEAAKIG KTVGIGAVKY ADLSKNRTSD YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDATA PTVLTEPLEK QLAAELLKFE NVLQSVADTA YPHYLAAYLY QAATLFSRFY EACPILKAEG ASRNSRLQLA KLTGNTLKQG LDLLGIDVLD VM // ID SYV_NEIG1 Reviewed; 945 AA. AC Q5F5W0; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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=NGO1809; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90427.1; -; Genomic_DNA. DR RefSeq; WP_003690041.1; NC_002946.2. DR RefSeq; YP_208839.1; NC_002946.2. DR ProteinModelPortal; Q5F5W0; -. DR EnsemblBacteria; AAW90427; AAW90427; NGO_1809. DR GeneID; 3282861; -. DR KEGG; ngo:NGO1809; -. DR PATRIC; 20337270; VBINeiGon24812_2170. DR HOGENOM; HOG000020094; -. DR KO; K01873; -. DR OMA; SQYRFDL; -. DR OrthoDB; EOG644ZM1; -. DR BioCyc; NGON242231:GI2G-1707-MONOMER; -. DR Proteomes; UP000000535; 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; 5. 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_0000224516. 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; 106333 MW; 4C6FC95AD43CF380 CRC64; MLDKYSPAEI ESKHYQNWES QGYFRPDMDL TKPSFSIQLP PPNVTGTLHM GHAFNQTIMD GLTRYYRMKG CNTAWIPGTD HAGIATQIVV ERQLAAQNVS RHDLGREKFL EKVWEWKEVS GGTITQQMRR VGCSADWTRE YFTMDGVRAE TVTEVFVRLY EQGLIYRGKR LVNWDPVLGT AVSDLEVESM EEQGSMWHIR YPLADNPTEA VIVATTRPET LLGDAAVAVN PEDERYTHLI GKELILPLTG RTIPVIADEY VEKDFGTGCV KITPAHDFND YEVGKRHDTR LINVFDLEAK VLANAEVFNF KGEAQPGFSL PEKYAGLDRF AARKQMVADL QEQGFLVEIK PHTLMTPKGD RTGSVIEPML TSQWFVAMSA TPNGGEPDNE FKGLSLADKA KKAVDSGAVR FIPENWVNTY NQWMNNIQDW CISRQLWWGH QIPAWYDEAG NVYVARNQAE AEKQAGKTGL TREEDVLDTW FSSALVPFST LGWPSETDEL KAFLPSNVLV TGYEIIFFWV ARMIMMTTHF TGKVPFKAVY IHGIVRDHEG KKMSKSEGNV IDPVDLIDGI GLDKLLMKRT TGLRKPETAP KVEEATKKLF PEGIPSMGAD ALRFTMASYA SLGRSVNFDF KRAEGYRNFC NKIWNATNFV LMNTENQDCG YGATAAEPRG HSFPDMWIIG RLNQTIEQVT QAYETYRFDL AAETLYSFVW NDYCDWYLEL AKVQLQTGCA SRQRATRHTL LRVLEAALRL LHPIIPFITE ELWQTVAPMC DAKTADSIML ARFPETDGGE IVQTAFGQMT VLQDLIGAVR NLRGETGIQP NVKAPLFVES ADDLADYLKY LPMMTRLTEA RQVAALPESG DAPVAVCNGA RLMLKVEIDK AAETARLSKE AEKLQKALDK LNAKLSKPGY TEKAPAHLVE KDKADLAELE DKMAKVQNQL AKLKD // ID SYE_NEIG1 Reviewed; 464 AA. AC Q5F5J8; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1926; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90539.1; -; Genomic_DNA. DR RefSeq; WP_010951371.1; NC_002946.2. DR RefSeq; YP_208951.1; NC_002946.2. DR ProteinModelPortal; Q5F5J8; -. DR EnsemblBacteria; AAW90539; AAW90539; NGO_1926. DR GeneID; 3282693; -. DR KEGG; ngo:NGO1926; -. DR PATRIC; 20337590; VBINeiGon24812_2322. DR HOGENOM; HOG000252722; -. DR KO; K01885; -. DR OMA; QLCYMPL; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NGON242231:GI2G-1829-MONOMER; -. DR Proteomes; UP000000535; 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_0000119611. 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; 52329 MW; 6B0536380D4FD19A CRC64; MTVKTRFAPS PTGYLHIGGV RTALFSWAFA RHHKGEFLLR IEDTDLARST AESVNIILDG MKWVGLDYDN ADNVVYQTRR FDRYKEVIAE LLAKGDAYYC YCSKEELEAM REKAEKEGTA TYDRRWRPEA GKTLPEIPAG VQPVVRFKTP LDGVTKWTDL VKGEISIPNE ALDDLIIARA DGTPTYNFCA VVDDYDMGVT HIIRGDDHVN NTPKQINILK AIGANLPEYG HLPMILNEQG KKISKRSGDT VAITDFGAMG ILPEAMLNYL ARLGWAHGDD EFFTTEQFIE WFDLKDVSPS PSRMDLKKLY WINGEHIKIT PDGKLTELVK PRLALRDIHE TEKPALEDVL ALVKDRAQDL NALADECLYF YKKQVPAEAD VAKHWDDEAA ARMLRFAERL EGLEDWNAKA IHDLFKPFCD EEGIKMGKLG MPLRLAVCGT AKTPSVDAVL ALISKEKVLK RIRA // ID SYK_NEIG1 Reviewed; 503 AA. AC Q5F6U2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO1454; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90095.1; -; Genomic_DNA. DR RefSeq; WP_003689332.1; NC_002946.2. DR RefSeq; YP_208507.1; NC_002946.2. DR ProteinModelPortal; Q5F6U2; -. DR SMR; Q5F6U2; 13-502. DR EnsemblBacteria; AAW90095; AAW90095; NGO_1454. DR GeneID; 3281692; -. DR KEGG; ngo:NGO1454; -. DR PATRIC; 20336329; VBINeiGon24812_1713. DR HOGENOM; HOG000236578; -. DR KO; K04567; -. DR OMA; DMMNLTE; -. DR OrthoDB; EOG69PQ2M; -. DR BioCyc; NGON242231:GI2G-1360-MONOMER; -. DR Proteomes; UP000000535; 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_1000012897. 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; 57380 MW; 6D45F2F5B87A830D CRC64; MSEQNHPQTE PQLDENQIIA LRREKLNNIR QQRNAYPNDF KRDSFAADLQ AQYGEIGKEE LDPQAVPVKI AGRMMLKRQM GKASFATIQD VTGQIQLYLN NKGVSQEVLD DFNHWDLGDI VGAEGTLFKT NHGELTVRVS DIRLLSKSLR 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 SQVAQKDAGD DEAMHYDADY IRAMEFGLPP TGGCGIGIDR LVMLLTDLQT IRDVILFPQM RPE // ID SYQ_NEIG1 Reviewed; 562 AA. AC Q5F7G0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 16-MAR-2016, entry version 77. DE RecName: Full=Glutamine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00126}; DE EC=6.1.1.18 {ECO:0000255|HAMAP-Rule:MF_00126}; DE AltName: Full=Glutaminyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00126}; DE Short=GlnRS {ECO:0000255|HAMAP-Rule:MF_00126}; GN Name=glnS {ECO:0000255|HAMAP-Rule:MF_00126}; GN OrderedLocusNames=NGO1218; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamine + tRNA(Gln) = AMP + CC diphosphate + L-glutaminyl-tRNA(Gln). {ECO:0000255|HAMAP- CC Rule:MF_00126}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00126}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00126}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89877.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F7G0; -. DR SMR; Q5F7G0; 11-558. DR PRIDE; Q5F7G0; -. DR EnsemblBacteria; AAW89877; AAW89877; NGO_1218. DR PATRIC; 20335747; VBINeiGon24812_1432. DR HOGENOM; HOG000259232; -. DR OrthoDB; EOG6DRPF7; -. DR BioCyc; NGON242231:GI2G-1129-MONOMER; -. DR Proteomes; UP000000535; 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_0000242871. FT MOTIF 35 45 "HIGH" region. FT MOTIF 271 275 "KMSKS" region. FT BINDING 274 274 ATP. {ECO:0000255|HAMAP-Rule:MF_00126}. SQ SEQUENCE 562 AA; 64572 MW; 0E28E106DAF63762 CRC64; MLNKDQFADN HFIRTIIEDD LKSGKHEAVQ TRFPPEPNGY LHIGHAKSIC LNFGLAYIYD GLCNLRFDDT NPEKENDEYV NAIKEDVEWL GFHWAGEPRF ASDYFDRLYD YAVGLIKDGK AYVDDLTPEE MREYRGTLTE AGKNSPYRDR SIEENLDLFT RMKNGEFPDG SKTLRLKIDM AAGNINMRDP VIYRIRRAHH HNTGDKWCIY PMYDYTHCIS DAIEGITHSL CTLEFEAHRP LYDWVLDNIP ALHATRPRQY EFSRLELLYT ITSKRKLNQL VVEKHVSGWD DPRMPTISGM RRRGYTPEGV RLFAKRAGIS KSENIVDMSV LEGAIREELE NSAPRLMAVL NPLKVTLTNF QAGKTQSRRA AFHPNHEEMG DREVPVSQTI YIEADDFAEN PPKGFKRLIP GGEVRLRHGY VIKCGEVVKD EAGNVVELKC SIDHDTLGKN PEGRKVKGVI HWVSAEHAAE IKVRLYDRLF TVERPGAVRG EDGEYLPFTD FLNPESVKEI TAYAEPAAKD LPAESRWQFE RIGYFVTDRQ DHGKDTPVFN RTVTLKDSWQ PK // ID TAL_NEIG1 Reviewed; 351 AA. AC Q5F6E9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493}; DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493}; GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=NGO1610; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. {ECO:0000255|HAMAP- CC Rule:MF_00493}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00493}. 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. {ECO:0000255|HAMAP-Rule:MF_00493}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00493}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90238.1; -; Genomic_DNA. DR RefSeq; WP_003689551.1; NC_002946.2. DR RefSeq; YP_208650.1; NC_002946.2. DR PDB; 3CLM; X-ray; 1.14 A; A=1-351. DR PDBsum; 3CLM; -. DR ProteinModelPortal; Q5F6E9; -. DR SMR; Q5F6E9; 1-351. DR EnsemblBacteria; AAW90238; AAW90238; NGO_1610. DR GeneID; 3281445; -. DR KEGG; ngo:NGO1610; -. DR PATRIC; 20336758; VBINeiGon24812_1924. DR HOGENOM; HOG000226074; -. DR KO; K00616; -. DR OMA; GLTSNPT; -. DR OrthoDB; EOG6T1WSN; -. DR BioCyc; NGON242231:GI2G-1507-MONOMER; -. DR UniPathway; UPA00115; UER00414. DR EvolutionaryTrace; Q5F6E9; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Pentose shunt; KW Reference proteome; Schiff base; Transferase. FT CHAIN 1 351 Transaldolase. FT /FTId=PRO_1000026529. FT ACT_SITE 138 138 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00493}. FT HELIX 3 9 {ECO:0000244|PDB:3CLM}. FT STRAND 12 17 {ECO:0000244|PDB:3CLM}. FT HELIX 21 25 {ECO:0000244|PDB:3CLM}. FT HELIX 28 33 {ECO:0000244|PDB:3CLM}. FT TURN 34 36 {ECO:0000244|PDB:3CLM}. FT HELIX 44 53 {ECO:0000244|PDB:3CLM}. FT HELIX 57 64 {ECO:0000244|PDB:3CLM}. FT HELIX 71 96 {ECO:0000244|PDB:3CLM}. FT STRAND 99 101 {ECO:0000244|PDB:3CLM}. FT STRAND 104 107 {ECO:0000244|PDB:3CLM}. FT HELIX 110 112 {ECO:0000244|PDB:3CLM}. FT HELIX 116 130 {ECO:0000244|PDB:3CLM}. FT STRAND 135 140 {ECO:0000244|PDB:3CLM}. FT HELIX 143 154 {ECO:0000244|PDB:3CLM}. FT STRAND 159 164 {ECO:0000244|PDB:3CLM}. FT HELIX 167 186 {ECO:0000244|PDB:3CLM}. FT STRAND 196 201 {ECO:0000244|PDB:3CLM}. FT HELIX 203 209 {ECO:0000244|PDB:3CLM}. FT HELIX 210 212 {ECO:0000244|PDB:3CLM}. FT HELIX 215 217 {ECO:0000244|PDB:3CLM}. FT TURN 218 220 {ECO:0000244|PDB:3CLM}. FT HELIX 221 238 {ECO:0000244|PDB:3CLM}. FT HELIX 240 246 {ECO:0000244|PDB:3CLM}. FT TURN 247 249 {ECO:0000244|PDB:3CLM}. FT STRAND 254 259 {ECO:0000244|PDB:3CLM}. FT HELIX 271 275 {ECO:0000244|PDB:3CLM}. FT STRAND 281 285 {ECO:0000244|PDB:3CLM}. FT HELIX 287 296 {ECO:0000244|PDB:3CLM}. FT TURN 303 306 {ECO:0000244|PDB:3CLM}. FT HELIX 307 319 {ECO:0000244|PDB:3CLM}. FT HELIX 324 347 {ECO:0000244|PDB:3CLM}. FT HELIX 348 350 {ECO:0000244|PDB:3CLM}. SQ SEQUENCE 351 AA; 37502 MW; 7278146C5F695095 CRC64; MTILSDVKAL GQQIWLDNLS RSLVQSGELA QMLKQGVCGV TSNPAIFQKA FAGDALYADE VAALKRQNLS PKQRYETMAV ADVRAACDVC LAEHESTGGK TGFVSLEVSP ELAKDAQGTV EEARRLHAAI ARKNAMIKVP ATDAGIDALE TLVSDGISVN LTLLFSRAQT LKAYAAYARG IAKRLAAGQS VAHIQVVASF FISRVDSALD ATLPDRLKGK TAIALAKAAY QDWEQYFTAP EFAALEAQGA NRVQLLWAST GVKNPAYPDT LYVDSLIGVH TVNTVPDATL KAFIDHGTAK ATLTESADEA RARLAEIAAL GIDVETLAAR LQEDGLKQFE EAFEKLLAPL V // ID SYM_NEIG1 Reviewed; 684 AA. AC Q5F585; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO2044; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90652.1; -; Genomic_DNA. DR RefSeq; WP_010951390.1; NC_002946.2. DR RefSeq; YP_209064.1; NC_002946.2. DR ProteinModelPortal; Q5F585; -. DR SMR; Q5F585; 2-556. DR EnsemblBacteria; AAW90652; AAW90652; NGO_2044. DR GeneID; 3282703; -. DR KEGG; ngo:NGO2044; -. DR PATRIC; 20337883; VBINeiGon24812_2464. DR HOGENOM; HOG000200400; -. DR KO; K01874; -. DR OMA; CHEAARG; -. DR OrthoDB; EOG6CVV9B; -. DR BioCyc; NGON242231:GI2G-1946-MONOMER; -. DR Proteomes; UP000000535; 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 1 684 Methionine--tRNA ligase. FT /FTId=PRO_0000139144. FT DOMAIN 581 684 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 684 AA; 76944 MW; CDD3A107B20A8BB4 CRC64; MTRKILVTSA LPYANGSIHL GHMVEHIQTD VWVRFQKLRG HECYYCCADD THGTPVMLAA QKQGIAPEDM IAKVRKEHLA DFTGFFIGYD NYYSTHSTEN KQFSQDIYRA LKANGKIESR VIEQLFDPEK QMFLPDRFVK GECPKCHAQD QYGDNCEVCG TTYSPTELIN PYSAVSGAKP ELRESEHFFF KLGECADFLK AWTSGNNPHD GKPHLQPEAL NKMKEWLGEG EETTLSDWDI SRDAPYFGFE IPDAPGKYFY VWLDAPVGYM ASFKNLCDRI GIDFDEYFKA DSQTEMYHFI GKDILYFHAL FWPAMLHFSG HRAPTGVYAH GFLTVDGQKM SKSRGTFITA KSYLEQGLNP EWMRYYIAAK LNGKIEDTDL NLQDFISRVN SDLVGKYVNI AARASGFIAK RFEGRPKDVS GSALLAKLAA ESDTIAEQYE NREYARALRD IMALADIVNE YVDANKPWEL AKQEGQDERL HEVCSELINA FTMLTAYLAP VLPQTAANAA RFLNLDAITW KNTRETLGEH AINKYEHLMQ RVEQKQVDDL IEANKQSIQT ASAPVEEGKY EKVAEQAGFD DFMKIDMRVA KVLNCEAVEG STKLLKFDLD FGFEKRIIFS GIAASYPNPA ELNGRMVIAV ANFAPRKMAK FGVSEGMILS AATADGKLKL LDVDAGAQPG DKVG // ID SYT_NEIG1 Reviewed; 637 AA. AC Q5F9U4; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. 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=NGO0295; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. 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; AE004969; AAW89043.1; -; Genomic_DNA. DR RefSeq; WP_010951023.1; NC_002946.2. DR RefSeq; YP_207455.1; NC_002946.2. DR ProteinModelPortal; Q5F9U4; -. DR SMR; Q5F9U4; 4-630. DR EnsemblBacteria; AAW89043; AAW89043; NGO_0295. DR GeneID; 3281668; -. DR KEGG; ngo:NGO0295; -. DR PATRIC; 20333573; VBINeiGon24812_0366. DR HOGENOM; HOG000003880; -. DR KO; K01868; -. DR OMA; FYYDFAY; -. DR OrthoDB; EOG61KBFJ; -. DR BioCyc; NGON242231:GI2G-276-MONOMER; -. DR Proteomes; UP000000535; 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_0000101014. 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; 72726 MW; 0AD6BADF8ECF3046 CRC64; MLNITLPDCS VRQYESPVTV AQIAASIGAG LAKAAVAGKV NGKLVDACDP IVEDSAVQII TPKDQEGIEI IRHSCAHLVG HAVKQLYPNA KMVIGPVIEE GFYYDIATEK PFTPEDVAAI EARMKELIAQ DYDVVKIMTP RAEAIKIFQE RGEEYKLRLI DDMPEVEAMG IYHHQEYVDM CRGPHVPNTR FLKNFKLTKL AGAYWRGDSN NEMLQRIYGT AWATKDELKD YIQRIEEAEK RDHRKLGKQL DLFHLQDEAP GMVFWHPKGW ALWQTIEQHM RKELNAAGYK EVKTPQIMDK TFWEKSGHWD NYKDNMFVTS SEKREYAVKP MNCPGHVQIF NNGLRSYRDL PMRLAEFGSC HRNEPSGALH GLMRVRGFVQ DDAHIFCTED QIVSEARAFN ELLVRIYKQF GFHDVSVRLS LRPEKRAGSD DVWDKAEQGL REALTACGVE WGELPGEGAF YGPKIEYHVK DALGRSWQCG TLQLDFVLPE RLDAEYVTEN NDRARPVMLH RAILGSLERF IGILIENHAG SFPLWLAPVQ MVIMNITENQ ADYCREVAAK LQAAGFRAEL DLRNEKIGYK IRDNSQYRFP YQIVIGDKEK QENKVAVRRK AEDLGSLDLD DFIAQLQQEI TDALVNH // ID SYP_NEIG1 Reviewed; 570 AA. AC Q5F938; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. 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=NGO0566; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89299.1; -; Genomic_DNA. DR RefSeq; WP_010951084.1; NC_002946.2. DR RefSeq; YP_207711.1; NC_002946.2. DR ProteinModelPortal; Q5F938; -. DR EnsemblBacteria; AAW89299; AAW89299; NGO_0566. DR GeneID; 3282489; -. DR KEGG; ngo:NGO0566; -. DR PATRIC; 20334194; VBINeiGon24812_0669. DR HOGENOM; HOG000076893; -. DR KO; K01881; -. DR OMA; IQPAELW; -. DR OrthoDB; EOG6TTVMR; -. DR BioCyc; NGON242231:GI2G-539-MONOMER; -. DR Proteomes; UP000000535; 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_0000248726. SQ SEQUENCE 570 AA; 62868 MW; 5B03A02AF87AFB51 CRC64; MKASQFFIST LKEAPAEAAF ASHKLMIRAG LIKANASGLY TWMPMGLRVL RKVENVVREE MARAGSVELL MPVVQPAELW QESGRWEFYG KELLRLKDRH ERDFCMGPTC EEVIADIVRK EINSYKQLPK NFYHIQTKFR DEVRPRFGVM RAREFVMKDA YSFHADYASL QATYDAMYDA HCRIFTRLGL AFRPVAADTG SIGGTGSHEF QVLAESGEDV IAYSDTSDYA ANIELAPTLP LKGERAAAQA VLTKVHTPNV KTIESLVEFL NIPVEQTLKS IVVEGENEGE LVLLLLRGDH EFNDIKAEKL AGVKSPLTMA SPAAIVEQFG ANGGSLGPVG FTGKVYADFA TEKGADWVIG ANEDDYHYTG FNFGRDAAEP EFVDLRNVVE GDESPDGQGR LKLARGIEVG HVFQLRGKYT QAMNVSFLDN NGKSQIMEMG CYGIGITRVV AAAIEQNNDE KGIIWTKAMA PFEVVIVPMN YKKSDTVREA ADRIYAELLA AGADVLLDDR DERAGVLLND SELLGIPHRI VIGDRALKEG NVEYAERRGN EAQAVAIGEI VARVTASLNA // ID SYS_NEIG1 Reviewed; 431 AA. AC Q5F752; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO1335; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89985.1; -; Genomic_DNA. DR RefSeq; WP_003700216.1; NC_002946.2. DR RefSeq; YP_208397.1; NC_002946.2. DR ProteinModelPortal; Q5F752; -. DR SMR; Q5F752; 1-428. DR EnsemblBacteria; AAW89985; AAW89985; NGO_1335. DR GeneID; 3282013; -. DR KEGG; ngo:NGO1335; -. DR PATRIC; 20336039; VBINeiGon24812_1569. DR HOGENOM; HOG000035938; -. DR KO; K01875; -. DR OMA; YRPERHE; -. DR OrthoDB; EOG61KBH9; -. DR BioCyc; NGON242231:GI2G-1249-MONOMER; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000535; 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_0000122088. 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; 47828 MW; 88934F437A3FC8D3 CRC64; MLDIQLLRSN TAAVAERLAR RGYDFDTARF DALEERRKSV QVKTEELQAS RNSISKQIGA LKGQGKHEEA QAAMDQVAQI KTDLEQAAAD LDAVQKELDA WLLSIPNLPH ESVPPGKDET ENVEVRKVGT PREFDFEIKD HVDLGEPLGL DFEGGAKLSG ARFTVMRGQI ARLHRALAQF MLDTHMLQHG YTEHYTPYIV DDTTLQGTGQ LPKFAEDLFH VTRGGDETKT TQYLIPTAEV TLTNTVAGSI IPSEQLPLKL TAHSPCFRSE AGSYGKDTRG LIRQHQFDKV EMVQIVHPEK SYGALEEMVG HAENILKALE LPYRVITLCT GDMGFSAAKT YDLEVWVPAQ NTYREISSCS NCEDFQARRM KARFKDENGK NRLVHTLNGS GLAVGRTLVA VLENHQNADG SINIPAALQP YMGGVTKLEV K // ID SYY_NEIG1 Reviewed; 431 AA. AC Q5FAF7; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO0066; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88830.1; -; Genomic_DNA. DR RefSeq; WP_003687313.1; NC_002946.2. DR RefSeq; YP_207242.1; NC_002946.2. DR ProteinModelPortal; Q5FAF7; -. DR SMR; Q5FAF7; 2-318. DR EnsemblBacteria; AAW88830; AAW88830; NGO_0066. DR GeneID; 3282277; -. DR KEGG; ngo:NGO0066; -. DR PATRIC; 20332984; VBINeiGon24812_0076. DR HOGENOM; HOG000242790; -. DR KO; K01866; -. DR OMA; GKHFPVN; -. DR OrthoDB; EOG6B09VR; -. DR BioCyc; NGON242231:GI2G-59-MONOMER; -. DR Proteomes; UP000000535; 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_0000234739. 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; 47182 MW; 952804AFCB48CBEC CRC64; MSVIQDLQSR GLIAQTTDIE ALDALLNEQK IALYCGFDPT ADSLHIGHLL PVLALRRFQQ AGHTPIALVG GATGMIGDPS FKAAERSLNS AETVAGWVGS IRSQLTPFLS FEGGNAAIMA NNADWFGSMN CLDFLRDIGK HFSVNAMLNK ESVKQRIDRD GAGISFTEFA YSLLQGYDFA ELNKRHGAVL EIGGSDQWGN ITAGIDLTRR LNQKQVFGLT LPLVTKSDGT KFGKTEGGAV WLNAKKTSPY QFYQFWLKVA DADVYKFLKY FTFLSIEEIG VVEAKDKASG SKPEAQRILA EEMTRLIHGE EALAAAQRIS ESLFAEDQSR LTESDFEQLA LDGLPAFEVS DGINAVEALV KTGLAASNKE ARGFVNAKAV LLNGKPAEAN NPNHAAERPD DAYLLIGEYK RFGKYTILRR GKRNHALLVW K // ID TATA_NEIG1 Reviewed; 67 AA. AC Q5FA49; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. 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=NGO0183; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88938.1; -; Genomic_DNA. DR RefSeq; WP_002214303.1; NC_002946.2. DR RefSeq; YP_207350.1; NC_002946.2. DR EnsemblBacteria; AAW88938; AAW88938; NGO_0183. DR GeneID; 3281482; -. DR KEGG; ngo:NGO0183; -. DR PATRIC; 20333293; VBINeiGon24812_0229. DR HOGENOM; HOG000245363; -. DR KO; K03116; -. DR OMA; HKVIDAD; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NGON242231:GI2G-168-MONOMER; -. DR Proteomes; UP000000535; 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_1000044408. 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 TATB_NEIG1 Reviewed; 228 AA. AC Q5FA50; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. 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=NGO0182; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88937.1; -; Genomic_DNA. DR RefSeq; WP_003687486.1; NC_002946.2. DR RefSeq; YP_207349.1; NC_002946.2. DR EnsemblBacteria; AAW88937; AAW88937; NGO_0182. DR GeneID; 3281448; -. DR KEGG; ngo:NGO0182; -. DR PATRIC; 20333291; VBINeiGon24812_0228. DR HOGENOM; HOG000027889; -. DR KO; K03117; -. DR OMA; HAAGTHP; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NGON242231:GI2G-167-MONOMER; -. DR Proteomes; UP000000535; 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_0000301195. FT TRANSMEM 1 21 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00237}. SQ SEQUENCE 228 AA; 25219 MW; B9854FFF60ED8D98 CRC64; MFDFGLGELI FVGIIALIVL GPERLPEAAR TAGRLIGRLQ RFVGSVKQEL DTQIELEELR KVKQAFEAAA AQVRDSLKET DTDMQNSLHD ISDGLKPWEK LPEQRTPADF GVDENGNPLP DTANTVSDGI SDVMPSERSD TSAETLGDDR QTGSTAEPAE TDKDRAWREY LTASAAAPVV QAVEVSYIDT AVETPVPHTT SLRKQAINRK RDFRPKHRAK PKLRVRKS // ID TGT_NEIG1 Reviewed; 371 AA. AC Q5F9U5; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO0294; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89042.1; -; Genomic_DNA. DR RefSeq; WP_010951022.1; NC_002946.2. DR RefSeq; YP_207454.1; NC_002946.2. DR ProteinModelPortal; Q5F9U5; -. DR SMR; Q5F9U5; 2-365. DR EnsemblBacteria; AAW89042; AAW89042; NGO_0294. DR GeneID; 3281620; -. DR KEGG; ngo:NGO0294; -. DR PATRIC; 20333569; VBINeiGon24812_0365. DR HOGENOM; HOG000223473; -. DR KO; K00773; -. DR OMA; MGVGKPD; -. DR OrthoDB; EOG6SNDVG; -. DR BioCyc; NGON242231:GI2G-274-MONOMER; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000000535; 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_0000135494. 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; 41962 MW; 744DFB6DD14647AE CRC64; MLKFTLHKKD GLARRGTLEL NHGKIETPVF MPVGTYGSVK AMNPQNLHDI KAQIILGNTY HLWLRPGLEV VEQFGGLHGF IGWDKPILTD SGGFQVFSLS DMRKLTEEGC TFKSPINGDK LFLSPEISMK IQTVLNSDIA MQLDECTPGE TTREQARKSL QMSLRWAERS KKAFEDLKNP NALFGIVQGA MYEDLREESL RGLEEFDFPG LAVGGLSVGE PKPEMYRMLH AVGPMLPERK PHYLMGVGTP EDLVYGVAHG IDMFDCVMPT RNARNGWLFT RFGDLKIKNA KHKPDKRPID ESCTCYACQN FSRAYLHHLH RAGEILGAQL NTIHNLHFYQ VIMAEMRDAV EQGKFADWQA QFHENRARGV D // ID THIG_NEIG1 Reviewed; 262 AA. AC Q5F5C4; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO2005; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90613.1; -; Genomic_DNA. DR RefSeq; WP_003692011.1; NC_002946.2. DR RefSeq; YP_209025.1; NC_002946.2. DR ProteinModelPortal; Q5F5C4; -. DR EnsemblBacteria; AAW90613; AAW90613; NGO_2005. DR GeneID; 3282619; -. DR KEGG; ngo:NGO2005; -. DR PATRIC; 20337787; VBINeiGon24812_2417. DR HOGENOM; HOG000248049; -. DR KO; K03149; -. DR OMA; AQYPSPA; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NGON242231:GI2G-1906-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000535; 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_0000162833. 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; 28169 MW; E14137232900EB6D CRC64; MLTLYGETFP SRLLLGTAAY PTPEILKQSV RTARPAMITV SLRRTGCGGE AHGQGFWSLL QETGVPVLPN TAGCQSVQEA VTTAQMAREV FETDWIKLEL IGDDDTLQPD VFQLVEAAEI LIKDGFKVLP YCTEDLIACR RLLDAGCQAL MPWAAPIGTG LGAVHAYALK ILRERLPDTP LIIDAGLGLP SQAAQVMEWG FDGVLLNTAV SRSGDPVNMA RAFALAVESG RLAFEAGPVE ARTKAQASTP TVGQPFWHSA EY // ID TIG_NEIG1 Reviewed; 437 AA. AC Q5F915; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303}; DE Short=TF {ECO:0000255|HAMAP-Rule:MF_00303}; DE EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303}; DE AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303}; GN Name=tig {ECO:0000255|HAMAP-Rule:MF_00303}; OrderedLocusNames=NGO0592; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000255|HAMAP-Rule:MF_00303}. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000255|HAMAP-Rule:MF_00303}. 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:0000255|HAMAP-Rule:MF_00303}. 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:0000255|HAMAP- CC Rule:MF_00303}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00303}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00303}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89322.1; -; Genomic_DNA. DR RefSeq; WP_003706141.1; NC_002946.2. DR RefSeq; YP_207734.1; NC_002946.2. DR ProteinModelPortal; Q5F915; -. DR EnsemblBacteria; AAW89322; AAW89322; NGO_0592. DR GeneID; 3282902; -. DR KEGG; ngo:NGO0592; -. DR PATRIC; 20334258; VBINeiGon24812_0701. DR HOGENOM; HOG000218239; -. DR KO; K03545; -. DR OMA; FRNDATK; -. DR OrthoDB; EOG63VBX3; -. DR BioCyc; NGON242231:GI2G-562-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm; KW Isomerase; Reference proteome; Rotamase. FT CHAIN 1 437 Trigger factor. FT /FTId=PRO_0000179392. FT DOMAIN 163 248 PPIase FKBP-type. {ECO:0000255|HAMAP- FT Rule:MF_00303}. SQ SEQUENCE 437 AA; 48368 MW; 9A38D62D514B4966 CRC64; MMSVTVEILE NLERKVVLSL PWSEINAETD KKLKQTQRRA KIDGFRPGKA PLKMIAQMYG ASAQNDVINE LVQRRFYDVA VAQELKVAGY PRFEGVEEQD DKESFKVAAI FEVFPEVVIG DLSAQEVEKV TASVGDAEVD QTVEILRKQR TRFNHVDREA RNGDRVIIDF EGKIDGEPFA GGTSKNYAFV LGAGQMLPEF EAGVVGMKAG ESKDVTVNFP EEYHGKDVAG KTAVFTITLN NVSEPTLPEV DADFAKALGI ADGDVAKMRE EVKKNVSREV ERRVNEQTKE SVMNALIKAV ELKVPVALVN EEAARLANEM KQNFVNQGMT DAANLDLPLD MFKEQAERRV SLGLILAKLV DENKLEPTEG QIKAVVANFA ESYEDPQEVI DWYYADTSRL QAPTSLAVES NVVDFVLGKA KVNKKALSFD EVMGAQA // ID THIC_NEIG1 Reviewed; 633 AA. AC Q5F588; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. 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=NGO2041; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90649.1; -; Genomic_DNA. DR RefSeq; WP_003686973.1; NC_002946.2. DR RefSeq; YP_209061.1; NC_002946.2. DR ProteinModelPortal; Q5F588; -. DR EnsemblBacteria; AAW90649; AAW90649; NGO_2041. DR GeneID; 3282706; -. DR KEGG; ngo:NGO2041; -. DR PATRIC; 20337867; VBINeiGon24812_2456. DR HOGENOM; HOG000224484; -. DR KO; K03147; -. DR OMA; TWELFRD; -. DR OrthoDB; EOG6NWBM5; -. DR BioCyc; NGON242231:GI2G-1943-MONOMER; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000535; 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_0000242275. 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; 71367 MW; 324571B4402CBB2A CRC64; MTTPKKTAKI SGNEARELSD LSEDIGIRFK YQNSERVYLQ GSRDDIRVPL REIRQDDTYT AQGTEANPPI PVYDTSGAYG DPAAHIDLKQ GLPHIRTAWL DERGDTEILP KLSSEYGIER AHDPKTAHLR FNQITRPRRA KAGRNVTQLH YARQGIITPE MEFAAIRERM KLDELFRRPE YAKLLKQHTG QSFGANIPTR PDQITPEFVR QEIAAGRAII PANINHPELE PMIIGRNFRV KINGNLGNSA VTSSLTEEVE KMVWSLRWGA DTIMDLSTGA HIHETREWII RNAPVPIGTV PIYQTLEKTG 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 THIE_NEIG1 Reviewed; 205 AA. AC Q5F5C2; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 71. 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=NGO2007; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90615.1; -; Genomic_DNA. DR RefSeq; WP_010355818.1; NC_002946.2. DR RefSeq; YP_209027.1; NC_002946.2. DR ProteinModelPortal; Q5F5C2; -. DR EnsemblBacteria; AAW90615; AAW90615; NGO_2007. DR GeneID; 3282617; -. DR KEGG; ngo:NGO2007; -. DR PATRIC; 20337795; VBINeiGon24812_2421. DR HOGENOM; HOG000155781; -. DR KO; K00788; -. DR OMA; HGNELKR; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NGON242231:GI2G-1908-MONOMER; -. DR UniPathway; UPA00060; UER00141. DR Proteomes; UP000000535; 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_0000157028. 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; 21839 MW; 0716637E2F6CD2A9 CRC64; MTFPPLKSLL KFYAVVPTAD WVGRMVKAGA DTVQLRCKTL HGNELKREIA RCVAACQGSR TQLFINDHWR EAIEAGAYGV HLGQEDMDTA DLAAIAAAGL RLGLSTHSVA ELDRALFVHP GYIASGAIFQ TTTKQMPTAP QGLDKLREYV EQARGTPVVA IGGIDLNNAR AVLATGVSSL AAVRAVTEAA NPEAVVKAFQ ALWDG // ID TILS_NEIG1 Reviewed; 426 AA. AC Q5F8F6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; GN OrderedLocusNames=NGO0820; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89531.1; -; Genomic_DNA. DR RefSeq; WP_010951131.1; NC_002946.2. DR RefSeq; YP_207943.1; NC_002946.2. DR ProteinModelPortal; Q5F8F6; -. DR PRIDE; Q5F8F6; -. DR EnsemblBacteria; AAW89531; AAW89531; NGO_0820. DR GeneID; 3282219; -. DR KEGG; ngo:NGO0820; -. DR PATRIC; 20334794; VBINeiGon24812_0967. DR HOGENOM; HOG000220745; -. DR KO; K04075; -. DR OMA; DAFEQCL; -. DR OrthoDB; EOG6NKR0V; -. DR BioCyc; NGON242231:GI2G-773-MONOMER; -. DR Proteomes; UP000000535; 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; 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 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_1000065619. FT NP_BIND 19 24 ATP. {ECO:0000255|HAMAP-Rule:MF_01161}. SQ SEQUENCE 426 AA; 47476 MW; 881ABE9393C9EA18 CRC64; MKDCFPQGLN GKKTAVALSG GLDSVVLLHL LVCAGKRAGF VPEALHIHHG LSPRADDWAD FCRNYCDMLG VGLETVKVCV EKNGLGIEAA ARQKRYAEFA EKGFDVLALA HHRDDQIETF MLAVARGGGL RALAAMPAVR PLGENGIIWR PLLPFSRQDI WDYARKHGLP NIEDESNTDT AYLRNRFRHR ILPELSAQIP HFGRHVLNNV RALQEDLALL EEVVVQDCRW VCGAGYFDTA RWLTFSPRRK THILRNFLKE NGIPVPNQNA LADIARVLTE AKTGRWNLQG FELHHYAGRL FVFASEQLAK PAFLKDGTIS GNLKKILTEH RFVLKRHPFG LPEAMLEQDG ILRTVAASDT LAVGGIHKNV KKILQGKRVL PFLRPIWPLV ADSGNRPLAL ANCCADFQIS VSDGILPVHP DFPILF // ID TRMB_NEIG1 Reviewed; 238 AA. AC Q5F929; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO0575; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89308.1; -; Genomic_DNA. DR RefSeq; WP_003688973.1; NC_002946.2. DR RefSeq; YP_207720.1; NC_002946.2. DR ProteinModelPortal; Q5F929; -. DR EnsemblBacteria; AAW89308; AAW89308; NGO_0575. DR GeneID; 3282905; -. DR KEGG; ngo:NGO0575; -. DR PATRIC; 20334218; VBINeiGon24812_0681. DR HOGENOM; HOG000073968; -. DR KO; K03439; -. DR OMA; IKLGHGV; -. DR OrthoDB; EOG6K6VBC; -. DR BioCyc; NGON242231:GI2G-548-MONOMER; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000000535; 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_0000229177. 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; 26962 MW; B72C8B617A7DE6B2 CRC64; MTDTPENQTP NDLPAGHSRS IRSFVLRQSH MTAAQQRAID TLWDSFGIDY QATPADLDAR FGSSRPKILE IGFGMGMASA EIARRLPETD FLAIDVHGPG VGNLLKLINE NHLENIRVMR HDAVEVVENM LQDGSLDGIH IFFPDPWHKK RHHKRRLIQA PFIAKLLPKL KTGGYIHLAT DWEEYAQQML EVLSSFDNLQ NTAADYAPTP DYRPETKFEA RGKRLGHGVW DLVFKRIG // ID TRMD_NEIG1 Reviewed; 249 AA. AC Q5FA59; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605}; DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605}; GN Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605}; GN OrderedLocusNames=NGO0172; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA CC = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}. CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family. CC {ECO:0000255|HAMAP-Rule:MF_00605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88928.1; -; Genomic_DNA. DR RefSeq; WP_003687474.1; NC_002946.2. DR RefSeq; YP_207340.1; NC_002946.2. DR ProteinModelPortal; Q5FA59; -. DR SMR; Q5FA59; 1-246. DR EnsemblBacteria; AAW88928; AAW88928; NGO_0172. DR GeneID; 3281334; -. DR KEGG; ngo:NGO0172; -. DR PATRIC; 20333267; VBINeiGon24812_0216. DR HOGENOM; HOG000016242; -. DR KO; K00554; -. DR OMA; YKGVDQR; -. DR OrthoDB; EOG6J48RZ; -. DR BioCyc; NGON242231:GI2G-158-MONOMER; -. DR Proteomes; UP000000535; 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_0000060419. FT REGION 133 138 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00605}. FT BINDING 113 113 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00605}. SQ SEQUENCE 249 AA; 27828 MW; FFE004C4D63D3B92 CRC64; MLIQAVTIFP EMFDSITRYG VTGRANRQGI WQFEAVNPRK FADNRLGYID DRPFGGGPGM IMMAPPLHAA IEHAKAQSSQ TAKVIYLSPQ GKPLTHQKAA ELAELTHLIL LCGRYEGIDE RLLQSSVDEE ISIGDFVVSG GELPAMMLMD AVLRLVPGIL GDIQSAEQDS FSSGILDCPH YTKPLEFQGM AVPEVLRSGN HGLIAEWRLE QSLRRTLERR PDLLEKRVLI PKESRLLNKI LQEQREIQS // ID TRUA_NEIG1 Reviewed; 265 AA. AC Q5F5V8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. 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=NGO1811; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90429.1; -; Genomic_DNA. DR RefSeq; WP_010951355.1; NC_002946.2. DR RefSeq; YP_208841.1; NC_002946.2. DR ProteinModelPortal; Q5F5V8; -. DR EnsemblBacteria; AAW90429; AAW90429; NGO_1811. DR GeneID; 3282256; -. DR KEGG; ngo:NGO1811; -. DR PATRIC; 20337278; VBINeiGon24812_2174. DR HOGENOM; HOG000248672; -. DR KO; K06173; -. DR OMA; PYPLEIN; -. DR OrthoDB; EOG6Z9B4R; -. DR BioCyc; NGON242231:GI2G-1709-MONOMER; -. DR Proteomes; UP000000535; 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_0000057418. 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; 28806 MW; 4A69B5CE60B97A48 CRC64; MDTAQKQRWA ITLSYDGSRF YGWQKQAGGV PTVQAALETA LARIAGESVA TTVAGRTDTG VHATAQVVHF DTAAVRPAQA WIRGVNAHLP EGIAVLHARQ VAPGFHARFD ASGRHYRYLL ESAPVRSPLL KNRAGWTHLE LDIGPMRRAA ALLVGEQDFS SFRAAGCQAK SPVKTIYRAD LTQSAGLVRL DLHGNAFLHH MVRNIMGALV YVGSGRLSVE GFAALIQERS RLKAPPTFMP DGLYLTGVDY PGAYGIVRPQ IPEWL // ID TRMA_NEIG1 Reviewed; 362 AA. AC Q5F757; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. 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=NGO1330; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89980.1; -; Genomic_DNA. DR RefSeq; WP_003691661.1; NC_002946.2. DR RefSeq; YP_208392.1; NC_002946.2. DR ProteinModelPortal; Q5F757; -. DR SMR; Q5F757; 1-360. DR EnsemblBacteria; AAW89980; AAW89980; NGO_1330. DR GeneID; 3282042; -. DR KEGG; ngo:NGO1330; -. DR PATRIC; 20336029; VBINeiGon24812_1564. DR HOGENOM; HOG000218626; -. DR KO; K00557; -. DR OMA; IKMLEWA; -. DR OrthoDB; EOG6V4GKM; -. DR BioCyc; NGON242231:GI2G-1244-MONOMER; -. DR Proteomes; UP000000535; 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_0000281447. 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; 41306 MW; 85149EB33E17E1E4 CRC64; MNDYTQQLQG KKDYLKTLFA GLDVPEWEVY ESPDKHYRMR AEFRIWHEGG EMFYAMFEKG QKASGASLIR CDRFDAASEA VNCLMPELIA VAAQSAELRN HWYAVEFLST LSGEMLVTMI YHKRLDDEWM KAAQALQQQL DISVIGRSRG QKIVLKQDYV TETLRVGDRD FHYRQIEGSF TQPNAAVCRK MLEWACRAAE GLGGDLLELY CGNGNFTLPL SRYFRQVLAT EISKTSVSAA QWNIEANWIG NIKIARLSAE EFTEAYTGKR EFTRLKESGI VLTDYAFSTI FVDPPRAGID EETLKLVSQF DNIIYISCNP ETLRANLDTL TETHTVGRAA LFDQFPFTHH IESGVLLKKK IL // ID TSAD_NEIG1 Reviewed; 354 AA. AC Q5FAC2; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO0104; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88865.1; -; Genomic_DNA. DR RefSeq; WP_003687363.1; NC_002946.2. DR RefSeq; YP_207277.1; NC_002946.2. DR ProteinModelPortal; Q5FAC2; -. DR EnsemblBacteria; AAW88865; AAW88865; NGO_0104. DR GeneID; 3282444; -. DR KEGG; ngo:NGO0104; -. DR PATRIC; 20333107; VBINeiGon24812_0137. DR HOGENOM; HOG000109568; -. DR KO; K01409; -. DR OMA; RDHVKRM; -. DR OrthoDB; EOG6K402S; -. DR BioCyc; NGON242231:GI2G-94-MONOMER; -. DR Proteomes; UP000000535; 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_0000303447. 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; 37683 MW; 3A03CE09ED0C889C CRC64; MLVLGIESSC DETGVALYDT ERGLRSHCLH TQMAMHAEYG GVVPELASRD HIRRLVPLTE GCLAQAGASY GDIDAVAFTQ GPGLGGALLA GSSYANALAL ALDKPVIPVH HLEGHLLSPL LAEEKPDFPF VALLVSGGHT QIMAVRGIGD YELLGESVDD AAGEAFDKTA KLLGLPYPGG AKLSELAESG RPEAFVFPRP MIHSDDLQMS FSGLKTAVLT AVEKVREANG SETIPEQTRN NICRAFQDAV VEVLEAKVKK ALLQTGFRTV VVAGGVGANR KLRETFGNMT VQIPTPKGKP KHPSEKVSVF FPPMAYCTDN GAMIAFAGAM HLGKGREVGA FNVRPRWSLS EIVK // ID TRPA_NEIG1 Reviewed; 261 AA. AC Q5F9Y6; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. 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=NGO0248; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89001.1; -; Genomic_DNA. DR RefSeq; WP_003694852.1; NC_002946.2. DR RefSeq; YP_207413.1; NC_002946.2. DR ProteinModelPortal; Q5F9Y6; -. DR EnsemblBacteria; AAW89001; AAW89001; NGO_0248. DR GeneID; 3281525; -. DR KEGG; ngo:NGO0248; -. DR PATRIC; 20333451; VBINeiGon24812_0306. DR HOGENOM; HOG000223815; -. DR KO; K01695; -. DR OMA; PVFICPP; -. DR OrthoDB; EOG6RVG0K; -. DR BioCyc; NGON242231:GI2G-233-MONOMER; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000535; 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_0000098813. 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; 27992 MW; B4CED35B34FF3EC3 CRC64; MSRIRQAFAA LDGGKALIPY IAVGDPDIRT TLALMHGMVA SGADILELGV PFSDPMADGP VIQRAAERAL ANGISLRDVL DVVRKFRETD TQTPVVLMGY LNPIHKMGYR EFAQEAAKAG VDGVLTVDSP IETIDSLYRE LKDNEVDCIF LIAPTTTEDR IKTIAELAGG FVYYVSLKGV TGAASLDTDE VSRKIEYLRQ YIDIPIGVGF GISNAESARK IGRVAAAIIV GSRIVKEIEN NAGNEAAAVG ALVKELKDAV R // ID TRPB_NEIG1 Reviewed; 400 AA. AC Q5F9W3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. 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=NGO0274; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89024.1; -; Genomic_DNA. DR RefSeq; WP_003687637.1; NC_002946.2. DR RefSeq; YP_207436.1; NC_002946.2. DR ProteinModelPortal; Q5F9W3; -. DR SMR; Q5F9W3; 12-397. DR EnsemblBacteria; AAW89024; AAW89024; NGO_0274. DR GeneID; 3281611; -. DR KEGG; ngo:NGO0274; -. DR PATRIC; 20333519; VBINeiGon24812_0340. DR HOGENOM; HOG000161710; -. DR KO; K01696; -. DR OMA; IPEMLYP; -. DR OrthoDB; EOG6GFGH7; -. DR BioCyc; NGON242231:GI2G-256-MONOMER; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000535; 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_1000018360. FT MOD_RES 92 92 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00133}. SQ SEQUENCE 400 AA; 43459 MW; C31E408696C60AE7 CRC64; MKNYHAPDEK GFFGEHGGLY VSETLIPALK ELEQAYNEAK NDPEFWAEFR RDLKHYVGRP SPVYHAARLS EHLGGAQIWL KREDLNHTGA HKVNNTIGQA LLARRMGKKR VIAETGAGQH GVASATVAAR FGMTCDVYMG ADDIQRQMPN VFRMKLLGAN VIGVDSGSRT LKDAMNEAMR EWVARVDDTF YIIGTAAGPA PYPEMVRDFQ CVIGNEAKAQ MQEATGRQPD VAVACVGGGS NAIGLFYPYI EEENVRLVGV EAGGLGVDTP DHAAPITSGA PIGVLHGFRS YLMQDENGQV LGTHSVSAGL DYPGIGPEHS HLHDIKRVEY TVAKDDEALE AFDLLCRFEG IIPALESSHA VAWAVKNAPK MGKDQVILVN LSGRGDKDIN TVAKLKGIEL // ID TRPC_NEIG1 Reviewed; 260 AA. AC Q5F645; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. 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=NGO1721; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90342.1; -; Genomic_DNA. DR RefSeq; WP_003694229.1; NC_002946.2. DR RefSeq; YP_208754.1; NC_002946.2. DR ProteinModelPortal; Q5F645; -. DR EnsemblBacteria; AAW90342; AAW90342; NGO_1721. DR GeneID; 3281235; -. DR KEGG; ngo:NGO1721; -. DR PATRIC; 20337034; VBINeiGon24812_2057. DR HOGENOM; HOG000230463; -. DR KO; K01609; -. DR OMA; MIDPYQI; -. DR OrthoDB; EOG6WT8JX; -. DR BioCyc; NGON242231:GI2G-1617-MONOMER; -. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000000535; 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_1000018508. SQ SEQUENCE 260 AA; 28622 MW; 097107AE32AD93AB CRC64; MTDILNKILA TKAQEVAAQK AAVNAEHIRA LAAEAAPVRS FIDSIRGKHR LNLPAVIAEI KKASPSKGLI RPDFRPAEIA RAYENAGAAC LSVLTDEPYF QGSPEYLKQA REAVLLPVLR KDFIIDEYQV YQARAWGADA VLLIAAALEQ GQLERFEALA HELGMTVLLE LHDETELEKC RNLTTPLWGV NNRNLRTFEV SLDQTLSLLP ALEGKTVVTE SGITGKADVE FMRARGVHTF LIGETFMRAD DIGAEVGKLF // ID TRPE_NEIG1 Reviewed; 491 AA. AC Q5F8B4; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 73. DE RecName: Full=Anthranilate synthase component 1; DE Short=AS; DE Short=ASI; DE EC=4.1.3.27; GN Name=trpE; OrderedLocusNames=NGO0872; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10417653; DOI=10.1046/j.1365-2958.1999.01514.x; RA Zhu P., Morelli G., Achtman M.; RT "The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, RT deletions, insertion elements and DNA islands."; RL Mol. Microbiol. 33:635-650(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AJ242839; CAB45014.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89573.1; -; Genomic_DNA. DR RefSeq; WP_010360232.1; NC_002946.2. DR RefSeq; YP_207985.1; NC_002946.2. DR ProteinModelPortal; Q5F8B4; -. DR EnsemblBacteria; AAW89573; AAW89573; NGO_0872. DR GeneID; 3281838; -. DR KEGG; ngo:NGO0872; -. DR PATRIC; 20334917; VBINeiGon24812_1028. DR HOGENOM; HOG000025142; -. DR KO; K01657; -. DR OMA; MYFYNFG; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NGON242231:GI2G-815-MONOMER; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000535; 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_0000154101. 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; 54748 MW; A810F7B2304FE47F CRC64; MISKQEYQAQ AAQGYNRIPL VQELLADLDT PLSLYLKLAN RPYTYLLESV VGGERFGRYS FIGLPCSHYL KAGGKHVDVY QNGEIVEQYD GNPLPFIEAF HNRFKTPEIP SLPRFTGGLV GYFGYETVYN FEHFAHRLKN TAKANPLGTP DILLMLSQEL AVIDNLSGKI HLIVYADPSQ PDSYERARER LEDIRTQLRQ SCAIPLSLGS KQTQAVSEFG EEPFKACVDK IKDYIFAGDC MQVVPSQRMS MEFTDNPLAL YRALRTLNPS PYLFYYDFGD FHIVGSSPEI LVRRERDDVI VRPIAGTRLR GKTPAEDLAN EQDLLSDAKE IAEHVMLIDL GRNDVGRISK TGEVKVTDKM VIEKYSHVMH IVSNVEGCLK EGVTNMDILA ATFPAGTLSG APKVRAMEII EEIEPEKRGI YGGAVGVWGF NNDMDLAIAI RTAVIKNNTL FIQSGAGVVA DSDPTSEWQE TQNKARAVVR AAQMVQEGLD K // ID TTCA_NEIG1 Reviewed; 319 AA. AC Q5F956; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. 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=NGO0547; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; AE004969; AAW89281.1; -; Genomic_DNA. DR RefSeq; WP_003692918.1; NC_002946.2. DR RefSeq; YP_207693.1; NC_002946.2. DR ProteinModelPortal; Q5F956; -. DR DNASU; 3282109; -. DR EnsemblBacteria; AAW89281; AAW89281; NGO_0547. DR GeneID; 3282109; -. DR KEGG; ngo:NGO0547; -. DR PATRIC; 20334146; VBINeiGon24812_0645. DR HOGENOM; HOG000013323; -. DR KO; K14058; -. DR OMA; IVQENTY; -. DR OrthoDB; EOG60KN2F; -. DR BioCyc; NGON242231:GI2G-521-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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_0000348771. 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; 35969 MW; 3E4032CE727A36C2 CRC64; MSKKTKQELE NNKLSKRLRH AVGDTINDFN MIEPGDKIMV CLSGGKDSYA LLDILRRLQA SAPIDFELVA VNLDQKQPGF PEEVLPTYLE SIGVPYKIVE EDTYSTVKRV LDEGKTTCSL CSRLRRGILY RTAKELGCTK IALGHHRDDI LATMFLNMFY GGKLKAMPPK LVSDNGEHIV IRPLAYVKEK DLIKYAELKQ FPIIPCNLCG SQPNLQRQVI GDMLRDWDKR FPGRIESMFS ALQNVVPSHL ADTELFDFAG LERGQNLKHG GDLAFDSEKM PERFSDGSEE DESEIKIEPQ KAERKVINIL ANKPKTCGP // ID TRPF_NEIG1 Reviewed; 208 AA. AC Q5F9X5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. 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=NGO0261; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89012.1; -; Genomic_DNA. DR RefSeq; WP_003687611.1; NC_002946.2. DR RefSeq; YP_207424.1; NC_002946.2. DR ProteinModelPortal; Q5F9X5; -. DR EnsemblBacteria; AAW89012; AAW89012; NGO_0261. DR GeneID; 3281084; -. DR KEGG; ngo:NGO0261; -. DR PATRIC; 20333489; VBINeiGon24812_0325. DR HOGENOM; HOG000161598; -. DR KO; K01817; -. DR OMA; FVNASRC; -. DR OrthoDB; EOG6N94DF; -. DR BioCyc; NGON242231:GI2G-244-MONOMER; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000535; 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_1000018613. SQ SEQUENCE 208 AA; 22531 MW; 99DF5E512DE00664 CRC64; MRKIRTKICG ITTPEDALYA AHAGADALGL VFYPQSPRAI DIIKAQKIAA ALPPFVSVVA LFVNESAQNI RRILAEVPIH IIQFHGDEDD AFCRQFDRPY IKAIRVQTAS DIRNAATRFP NAQALLFDAY HPSEYGGTGH RFDWTLLAEY SGKPWVLAGG LTPENVGEAV RITGAEAVDV SGGVEASKGK KDPAKVAAFI ATANRLSR // ID TRPD_NEIG1 Reviewed; 342 AA. AC Q5F7H5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. 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=NGO1203; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89862.1; -; Genomic_DNA. DR RefSeq; WP_010358628.1; NC_002946.2. DR RefSeq; YP_208274.1; NC_002946.2. DR ProteinModelPortal; Q5F7H5; -. DR EnsemblBacteria; AAW89862; AAW89862; NGO_1203. DR GeneID; 3281967; -. DR KEGG; ngo:NGO1203; -. DR PATRIC; 20335705; VBINeiGon24812_1411. DR HOGENOM; HOG000230451; -. DR KO; K00766; -. DR OMA; MIVLNAG; -. DR OrthoDB; EOG67DPT8; -. DR BioCyc; NGON242231:GI2G-1114-MONOMER; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000535; 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 1 342 Anthranilate phosphoribosyltransferase. FT /FTId=PRO_0000227170. 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 342 AA; 36389 MW; 3C9198972DE48ABD CRC64; MITPQQAIER LISNNELFYD EMTDLMRQMM SGKVPPEQIA AILTGLRIKV ETVSEITAAA AVMCEFASKV PLEDADGLVD IVGTGGDGAK TFNISTTSMF VAAAAGAKVA KHGGRSVSSS SGAADVMEQM GANLNLTPEQ IAQSIRQTGI GFMFAPNHHS AMRHVAPVRR SLGFRSIFNI LGPLTNPAGA PNQLLGVFHT DLCGILSRVL QQLGSKHVLV VCGEGGLDEI TLTGKTRVAE LKDGKISEYD IRPEDFGIET RRNLDEIKVA NTQESLLKMN EVLDGKEGAA RDIVLLNTAA ALYAGNIAAS LSDGISAARE GIDSGRAKAK KEEFVGFTRQ FA // ID TRUB_NEIG1 Reviewed; 306 AA. AC Q5F8W8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 69. 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=NGO0642; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89369.1; -; Genomic_DNA. DR RefSeq; WP_003697163.1; NC_002946.2. DR RefSeq; YP_207781.1; NC_002946.2. DR ProteinModelPortal; Q5F8W8; -. DR EnsemblBacteria; AAW89369; AAW89369; NGO_0642. DR GeneID; 3281788; -. DR KEGG; ngo:NGO0642; -. DR PATRIC; 20334368; VBINeiGon24812_0756. DR HOGENOM; HOG000231223; -. DR KO; K03177; -. DR OMA; YELQFIR; -. DR OrthoDB; EOG6358D3; -. DR BioCyc; NGON242231:GI2G-609-MONOMER; -. DR Proteomes; UP000000535; 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 1 306 tRNA pseudouridine synthase B. FT /FTId=PRO_0000121873. FT ACT_SITE 47 47 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01080}. SQ SEQUENCE 306 AA; 33387 MW; DAED8625518BDC30 CRC64; MTNKPAKRPV NGVLLLDKPE GLSSNTALQK ARRLFHAEKA GHTGVLDPLA TGLLPVCFGE AAKFAQYLLD ADKAYTATLK LGEASSTGDA EGEIIAAARA DISLAEFQTA CQALTGNIRQ VPPMFSALKH EGKPLYEYAR KGIVIERKPR DITVYSIDIA EFDAPKAVIS VRCSKGTYIR TLSEGIAKHI GTFAHLTALR RTETAGFTIA QSHTLEALAN LNETERDGLL LPCDVLVSHF PQTVLNDYAV HMLQCGQRPR FEEDLPSDTP VRVYTENGRF VGLAEYQKEI CRMKALRLMN TAASSA // ID TYSY_NEIG1 Reviewed; 264 AA. AC Q5F732; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. 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=NGO1357; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90005.1; -; Genomic_DNA. DR RefSeq; WP_003691712.1; NC_002946.2. DR RefSeq; YP_208417.1; NC_002946.2. DR ProteinModelPortal; Q5F732; -. DR SMR; Q5F732; 1-264. DR EnsemblBacteria; AAW90005; AAW90005; NGO_1357. DR GeneID; 3282062; -. DR KEGG; ngo:NGO1357; -. DR PATRIC; 20336099; VBINeiGon24812_1598. DR HOGENOM; HOG000257899; -. DR KO; K00560; -. DR OMA; IVYELLW; -. DR OrthoDB; EOG6K6V53; -. DR BioCyc; NGON242231:GI2G-1270-MONOMER; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000535; 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_1000000637. FT ACT_SITE 146 146 {ECO:0000255|HAMAP-Rule:MF_00008}. SQ SEQUENCE 264 AA; 30248 MW; 52A71581DD479781 CRC64; MKAYLDLMRH VLDNGTDKSD RTGTGTRSVF GYQMRFDLGK GFPLLTTKKL HLRSIIHELL WFLKGDTNIK YLKDNNVSIW DEWADENGDL GPVYGYQWRS WPAPDGRHID QIANVVEQIK KNPDSRRLIV SAWNPALVDE MALPPCHALF QFYVADGKLS CQLYQRSADI FLGVPFNIAS YALLTMMMAQ VCGLEAGEFV HTFGDAHLYR NHFEQAALQL EREPRALPVM KINPEVKDLF AFKFEDFELE GYDPHPHIKA VVSV // ID TSAC_NEIG1 Reviewed; 189 AA. AC Q5F5I5; DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 16-MAR-2016, entry version 61. 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=NGO1940; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW90552.1; 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; AE004969; AAW90552.1; ALT_INIT; Genomic_DNA. DR EnsemblBacteria; AAW90552; AAW90552; NGO_1940. DR PATRIC; 20337623; VBINeiGon24812_2338. DR HOGENOM; HOG000076163; -. DR OrthoDB; EOG6C5RT4; -. DR BioCyc; NGON242231:GI2G-1842-MONOMER; -. DR Proteomes; UP000000535; 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_0000352937. FT DOMAIN 9 189 YrdC-like. {ECO:0000255|HAMAP- FT Rule:MF_01852}. SQ SEQUENCE 189 AA; 20989 MW; D60370671B0CDB31 CRC64; MLFSRIIAAS AQRKLSVYLK KGGLVAYPTE SCYGLGCLPT LAKALGKLAH LKKRPQHKGM IVIGNQLEQL QPLLQMPSEN IQTMLRNEWP APKTFLLLAK SGVLPALRGK RRSKLAVRVP DHTGARRLCQ ALGMPLVSTS CNRAGKRACR TEREVRRQFG RDVWIVGGRI GRQKSPSQII DGETGKRLR // ID UBIE_NEIG1 Reviewed; 245 AA. AC Q5F9R9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. 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=NGO0321; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89068.1; -; Genomic_DNA. DR RefSeq; WP_003687710.1; NC_002946.2. DR RefSeq; YP_207480.1; NC_002946.2. DR ProteinModelPortal; Q5F9R9; -. DR EnsemblBacteria; AAW89068; AAW89068; NGO_0321. DR GeneID; 3281747; -. DR KEGG; ngo:NGO0321; -. DR PATRIC; 20333629; VBINeiGon24812_0392. DR HOGENOM; HOG000249463; -. DR KO; K03183; -. DR OMA; GGLHRAW; -. DR OrthoDB; EOG6M6JSB; -. DR BioCyc; NGON242231:GI2G-303-MONOMER; -. DR UniPathway; UPA00079; UER00169. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; 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_1000056265. 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; 27401 MW; 2E4F749704875865 CRC64; MGGQKTHFGF STVNEDEKAG KVAEVFHSVA KNYDIMNDVM SAGLHRVWKH FTIHTAHLKK GDKVLDIAGG TGDLSRGWAK RVGKEGEVWL TDINSSMLTV GRDRLLNEGM ILPVSLADAE KLPFPDNYFN LVSVAFGLRN MTYKDAALKE MYRVLKPGGT LLVLEFSKIY KPLEGAYDFY SFKLLPVMGR LIAKDADSYQ YLAESIRMHP DQETLKQMML DAGFDSVDYH NMSAGIVALH KGVKF // ID UBIA_NEIG1 Reviewed; 296 AA. AC Q5F9S8; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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=NGO0312; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89059.1; -; Genomic_DNA. DR RefSeq; WP_010951027.1; NC_002946.2. DR RefSeq; YP_207471.1; NC_002946.2. DR EnsemblBacteria; AAW89059; AAW89059; NGO_0312. DR GeneID; 3281708; -. DR KEGG; ngo:NGO0312; -. DR PATRIC; 20333605; VBINeiGon24812_0382. DR HOGENOM; HOG000003696; -. DR KO; K03179; -. DR OMA; KSTAIYF; -. DR OrthoDB; EOG680X3B; -. DR BioCyc; NGON242231:GI2G-292-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; 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_0000262808. 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; 33223 MW; 553677D34D258C12 CRC64; MNLKSPLFLR LSDRLDVYIR LMRADKPIGT LLLLWPTYWA LWLASDGIPD LAVLAAFTIG TFLMRSAGCV INDFADRDFD GAVERTKNRP FAQGRVKKKE ALLLTAFLCL LAALCLIPLN HLTWLMSLPA LFLALTYPFT KRFFPIPQFY LGFAFSFGIP MAFAAVGNSV PVEAWILFAA NVLWTLAYDT VYAMADKEDD LKIGIKTSAV TFGRYDIAAV MLCHGGFTLL MAVLGAVIGA AWAYWTAIPI VLLLQYRQYA AIKSRVRQIC FETFLANNRI GWVWFAAIFA HTFFAK // ID UBID_NEIG1 Reviewed; 492 AA. AC Q5F742; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 76. 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=NGO1345; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89995.1; -; Genomic_DNA. DR RefSeq; WP_003691687.1; NC_002946.2. DR RefSeq; YP_208407.1; NC_002946.2. DR ProteinModelPortal; Q5F742; -. DR SMR; Q5F742; 3-492. DR EnsemblBacteria; AAW89995; AAW89995; NGO_1345. DR GeneID; 3282543; -. DR KEGG; ngo:NGO1345; -. DR PATRIC; 20336063; VBINeiGon24812_1581. DR HOGENOM; HOG000227663; -. DR KO; K03182; -. DR OMA; DFQEWCQ; -. DR OrthoDB; EOG6QZMM7; -. DR BioCyc; NGON242231:GI2G-1259-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; 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_0000267673. 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; 55308 MW; EE842DF79910CD8C CRC64; MKYKDLRDFI AMLEQQGKLK RVAHPVSPHL EMTEIADRVL RAEGPALLFE NPVKPDGTRY DYPVLANLFG TPERVAMGMG ADSVSKLREI GQTLAYLKEP EPPKGIKDAF SKLPLLKDIW SMAPNVVKNA PCQEIVWEGE DVDLYQLPIQ HCWPEDVAPL VTWGLTVTRG PHKKRQNLGI YRQQLIGKNK LVMRWLSHRG GALDYQEFRK LNPDTPYPVA VVLGCDPSTI LGAVTPVPDT LSEYQFAGLL RGSRTELVKC IGSDLQVPAR AEIVLEGVIH PNETALEGPY GDHTGYYNEQ GHFPVFTVER ITMRENPIYH STYTGKPPDE PAVLGVALNE VFVPLLQKQF SEITDFYLPP EGCSYRMAVV SMKKQYAGHA KRVMTGCWSF LRQFMYTKFI IVVDDDVNVR DWKEVIWAVT TRMDPVRDTV LVENTPIDYL DFASPVSGLG GKMGLDATSK WPGETDREWG RVIKKDPAVT VKIDGIWGKL GL // ID UNG_NEIG1 Reviewed; 219 AA. AC Q5F8I7; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. 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=NGO0786; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89500.1; -; Genomic_DNA. DR RefSeq; WP_003688628.1; NC_002946.2. DR RefSeq; YP_207912.1; NC_002946.2. DR ProteinModelPortal; Q5F8I7; -. DR SMR; Q5F8I7; 3-217. DR EnsemblBacteria; AAW89500; AAW89500; NGO_0786. DR GeneID; 3281984; -. DR KEGG; ngo:NGO0786; -. DR PATRIC; 20334720; VBINeiGon24812_0932. DR HOGENOM; HOG000229528; -. DR KO; K03648; -. DR OMA; IALIPKN; -. DR OrthoDB; EOG6MSS63; -. DR BioCyc; NGON242231:GI2G-740-MONOMER; -. DR Proteomes; UP000000535; 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_1000009920. FT ACT_SITE 61 61 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00148}. SQ SEQUENCE 219 AA; 24688 MW; 8B55F4010567E3E2 CRC64; MDTWHDALGG EKQQPYFQEI LNAVRQERLS GQIIYPPEAD VFNAFRLTAF DRVKVVILGQ DPYHGVGQAH GLAFSVRQGV RIPPSLLNIY KELETDIEGF SIPAHGCLTA WAEQGILLLN TVLTVRAGQA HSHALLGWER FTDTVIRQLA THRKHLVFML WGGYAQQKGR LIDSQNHLIL TAPHPSPLSA YRGFFGCRHF SQANSYLSQH GIEPINWKL // ID UPPP_NEIG1 Reviewed; 273 AA. AC Q5F6K4; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. 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}; GN OrderedLocusNames=NGO1547; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90183.1; -; Genomic_DNA. DR RefSeq; WP_003689465.1; NC_002946.2. DR RefSeq; YP_208595.1; NC_002946.2. DR EnsemblBacteria; AAW90183; AAW90183; NGO_1547. DR GeneID; 3281468; -. DR KEGG; ngo:NGO1547; -. DR PATRIC; 20336596; VBINeiGon24812_1844. DR HOGENOM; HOG000218356; -. DR KO; K06153; -. DR OMA; KVFDIAI; -. DR OrthoDB; EOG6QP13M; -. DR BioCyc; NGON242231:GI2G-1451-MONOMER; -. DR Proteomes; UP000000535; 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_0000151167. 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}. SQ SEQUENCE 273 AA; 30401 MW; 192242AC3FF60C4D CRC64; MDFLIVLKAL MMGLVEGFTE FLPISSTGHL IVFGNLIGFH SNHKVFEIAI QLGAVLAVVF EYRQRFSNVL HGVGKDRKAN RFVLNLAIAF IPAAVMGLLF DKQIKEYLFN PLSVAVMLVL GGFFILWVEK RQSRAEPKIA DVDALRPIDA LMIGVAQVFA LVPGTSRSGS TVMGGMLWGI ERKTATEFSF FLAVPMMVAA TAYDVLKHYR FFTLHDVGLI LIGFIAAFVS GLVAVKALLK FVSKKNYIPF AYYRIVFGIV IIILWLSGWI SWE // ID UVRB_NEIG1 Reviewed; 675 AA. AC Q5F931; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. 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=NGO0573; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89306.1; -; Genomic_DNA. DR RefSeq; WP_010951086.1; NC_002946.2. DR RefSeq; YP_207718.1; NC_002946.2. DR ProteinModelPortal; Q5F931; -. DR SMR; Q5F931; 9-601. DR EnsemblBacteria; AAW89306; AAW89306; NGO_0573. DR GeneID; 3282242; -. DR KEGG; ngo:NGO0573; -. DR PATRIC; 20334212; VBINeiGon24812_0678. DR HOGENOM; HOG000073580; -. DR KO; K03702; -. DR OMA; QEYVDRM; -. DR OrthoDB; EOG6B360R; -. DR BioCyc; NGON242231:GI2G-546-MONOMER; -. DR Proteomes; UP000000535; 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_0000227332. 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. SQ SEQUENCE 675 AA; 76908 MW; 172657531AB929C7 CRC64; MEVIRYPNSP FKLHQPFPPA GDQPTAIAGL IEGLSDGLAY QTLLGVTGSG KTYTMANVIA QSGRPAIIMA HNKTLAAQLY AEMREFFPEN AVEYFVSYYD YYQPEAYVPS RDLFIEKDSA INEHIEQMRL SATKNLMTRD DVIIVATVSA IYGIGDPTEY QQMVLSVKEG DTIEQRDIIA TLVSMQYERG DLDFKRGSFR VRGDVIDVYP AESSENALRI SLFDDEIDRL DMFDPLSGSL HQRVGRYTVF PSSHYVTPRD TVLRACESIK EELRERIEFF AREQRPVEQQ RIEQRTRFDL EMLYEMGFCK GIENYSRHFS GKKEGEPPPT LMDYLPDNAI MFIDESHVTV TQIGGMYKGD ASRKQNLVDY GFRLPSARDN RPLKFHEFEK VMPQTVFVSA TPAKYEEEHA GQVVEQVVRP TGLVDPQTII RPVATQVDDL MSEINDRIQK GERVLVTTLT KRMAEQLTDY YSELGIKVRY LHSDIDTVER VEIIRDLRLG LFDVLVGINL LREGLDIPEV SLVAILDADK EGFLRSHRSL IQTIGRAARN VNGVAILYAD KITDSMKAAV DETERRREKQ IKFNEEHGIV PQQIKKQVKD IIDGVYHEED SGKGRRQGKN KVKVGEIHNE EDAIKEIAKL EKAMQQAARD LQFEEAAVLR DRISNIKENL LFGAE // ID UVRC_NEIG1 Reviewed; 617 AA. AC Q5F928; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 09-DEC-2015, entry version 72. 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=NGO0578; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW89309.1; 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; AE004969; AAW89309.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_207721.1; NC_002946.2. DR ProteinModelPortal; Q5F928; -. DR SMR; Q5F928; 563-617. DR EnsemblBacteria; AAW89309; AAW89309; NGO_0578. DR GeneID; 3282904; -. DR KEGG; ngo:NGO0578; -. DR PATRIC; 20334222; VBINeiGon24812_0683. DR HOGENOM; HOG000279961; -. DR KO; K03703; -. DR OrthoDB; EOG6K13R9; -. DR BioCyc; NGON242231:GI2G-549-MONOMER; -. DR Proteomes; UP000000535; 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_0000227449. 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; 69688 MW; AC9A7EEFCB68C6DA CRC64; MNTENRSPEQ FDIPLFLKNL PKLPGVYRFF DEGGNVLYVG KAVNLKRRVS GYFQKNDHSP RIALMVKQVR HIETTITRSE AEALILENNF IKALSPKYNI LFRDDKSYPY LMLSGHQYPQ MAYYRGTLKN PNQYFGPYPN SNAVRDSIQV LQKVFMLRTC EDSVFEHRDR PCLLYQIKRC TAPCVGHISE EDYCDSVRQA ATFLNGKTDE LTRTLQHKMQ TAAANLQFEE AARYRDQIQA LGIIQSNQFI DSKNPNNPND IDLLALAVSD GLVCVHWVSI RGGRHVGDKS FFPDTKNDPE PNGQDYAEAF VAQHYLGKSK PDIIISNFPV PDALKEALEG EHGKQMQFVT KTIGERKVWL KMAEQNAQMA ITQRHLQQSN QQHRIDELAK ILGMNSDGIN RLECFDISHT QGEATIASCV VYDEQNIQPS QYRRYNITTA KPGDDYAAMR EVLTRRYGKI QEAEANGESV KWPDVVLIDG GKGQIGVAVS VWEELGLHIP LVGIAKGPER KAGMEELILP FTGELFRLPP NSPALHLLQT VRDESHRFAI TGHRKKRDKA RVTSSLGDIP GVGSKRRQAL LTRFGGLRGV IAASREDLEK VEGISKALAE TIYNHLH // ID UPP_NEIG1 Reviewed; 208 AA. AC Q5F9P0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 82. 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=NGO0353; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89097.1; -; Genomic_DNA. DR RefSeq; WP_003690802.1; NC_002946.2. DR RefSeq; YP_207509.1; NC_002946.2. DR ProteinModelPortal; Q5F9P0; -. DR SMR; Q5F9P0; 6-208. DR PRIDE; Q5F9P0; -. DR EnsemblBacteria; AAW89097; AAW89097; NGO_0353. DR GeneID; 3281240; -. DR KEGG; ngo:NGO0353; -. DR PATRIC; 20333703; VBINeiGon24812_0429. DR HOGENOM; HOG000262754; -. DR KO; K00761; -. DR OMA; NTHLWIA; -. DR OrthoDB; EOG6HF5WX; -. DR BioCyc; NGON242231:GI2G-332-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000535; 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_1000053748. 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; 22878 MW; B3B629B57821B215 CRC64; MNVNVINHPL VRHKLTLMRE ADCSTYKFRT LTTELARLMA YEASRDFEIE KYLIDGWCGQ IEGDRIKGKT LTVVPILRAG LGMLDGVLDL IPTAKISVVG LQRDEETLKP ISYFEKFVDS MDERPALIID PMLATGGSMV ATIDLLKEKG CRNIKALVLV AAPEGVKAVN DAHPDVTIYT AALDSRLNEN GYIIPGLGDA GDKIFGTR // ID XERC_NEIG1 Reviewed; 305 AA. AC Q5FAI3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808}; GN Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; GN OrderedLocusNames=NGO0035; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88804.1; -; Genomic_DNA. DR RefSeq; WP_003687253.1; NC_002946.2. DR RefSeq; YP_207216.1; NC_002946.2. DR ProteinModelPortal; Q5FAI3; -. DR EnsemblBacteria; AAW88804; AAW88804; NGO_0035. DR GeneID; 3282503; -. DR KEGG; ngo:NGO0035; -. DR PATRIC; 20332900; VBINeiGon24812_0035. DR HOGENOM; HOG000045294; -. DR KO; K03733; -. DR OMA; ERQVSPH; -. DR OrthoDB; EOG6PZXFP; -. DR BioCyc; NGON242231:GI2G-32-MONOMER; -. DR Proteomes; UP000000535; 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 1 305 Tyrosine recombinase XerC. FT /FTId=PRO_1000070019. FT ACT_SITE 155 155 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 179 179 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 246 246 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 249 249 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 272 272 {ECO:0000255|HAMAP-Rule:MF_01808}. FT ACT_SITE 281 281 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01808}. SQ SEQUENCE 305 AA; 34592 MW; C338E5614BA1C240 CRC64; MVLDGFAAYF DAYLENIVRE GKSEHTVAAY RRDLEELFAL LAQMPSEDAG GVPQDLSRRD FTAALRRLSQ RGLDGRTLAR KLSAWRQYCA WLVKRGLMRA DPTADIKPPK QPERVPKALP QEWLNRMLDL PVDGGDPLAV RDHALFELMY GSGLRVSEIH GLNADDVYLD EAWVHVTGKG RKQRQVPLTG KSVEALKNYL PLRQTASDGK ALFTGRNGTR LSQRQIQKRL ESWAAQYGDG RHVSPHMMRH SYAGHLLQAS RDIRAVQELL GHSSLSTTQI YTKLDFDHIA RLYDEAHPRA KRQDE // ID Y1598_NEIG1 Reviewed; 91 AA. AC Q5F6G1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE RecName: Full=UPF0213 protein NGO1598; GN OrderedLocusNames=NGO1598; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90226.1; -; Genomic_DNA. DR RefSeq; WP_003693497.1; NC_002946.2. DR RefSeq; YP_208638.1; NC_002946.2. DR ProteinModelPortal; Q5F6G1; -. DR EnsemblBacteria; AAW90226; AAW90226; NGO_1598. DR GeneID; 3281646; -. DR KEGG; ngo:NGO1598; -. DR PATRIC; 20336732; VBINeiGon24812_1912. DR HOGENOM; HOG000285485; -. DR OMA; VEQWPSK; -. DR OrthoDB; EOG6RC3X0; -. DR BioCyc; NGON242231:GI2G-1494-MONOMER; -. DR Proteomes; UP000000535; 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 NGO1598. FT /FTId=PRO_1000063675. FT DOMAIN 4 83 GIY-YIG. {ECO:0000255|PROSITE- FT ProRule:PRU00977}. SQ SEQUENCE 91 AA; 10072 MW; 2A0F998B08267FC0 CRC64; MNASNWSVYL ILCENSAFYC GISPNPQQRL AIHTAGKGAK YTRVFKPVAM RIVAGGMDKG TALKQEIAVK KLTAAQKRQL WEQAEKMPSE T // ID Y180_NEIG1 Reviewed; 215 AA. AC Q5FA52; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 63. DE RecName: Full=Maf-like protein NGO0180 {ECO:0000255|HAMAP-Rule:MF_00528}; GN OrderedLocusNames=NGO0180; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88935.1; -; Genomic_DNA. DR RefSeq; YP_207347.2; NC_002946.2. DR ProteinModelPortal; Q5FA52; -. DR EnsemblBacteria; AAW88935; AAW88935; NGO_0180. DR GeneID; 3281464; -. DR KEGG; ngo:NGO0180; -. DR PATRIC; 20333287; VBINeiGon24812_0226. DR HOGENOM; HOG000241745; -. DR KO; K06287; -. DR OMA; FGIPCWQ; -. DR OrthoDB; EOG6SV5F0; -. DR BioCyc; NGON242231:GI2G-165-MONOMER; -. DR Proteomes; UP000000535; 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 1 215 Maf-like protein NGO0180. FT /FTId=PRO_0000267348. FT ACT_SITE 46 46 {ECO:0000255|HAMAP-Rule:MF_00528}. SQ SEQUENCE 215 AA; 23317 MW; 7AF54A210A8D5B99 CRC64; MPSEAPPHIK EHTVNTLYLG SGSPRRMEIL TQLGYRVVKL PAGIDETVKA GETPAPYVQR MAEEKNQAAL TLFCETNGAM PDFPLITADT CVFSDGIILG KPRSQAEAIE FLNRLSGKQH TVLTAVCIHY RGKTSSRVQT NRVVFKPLSS EEISAYVQSG EPMEKAGAYA VQGIGGIFIQ SIEGSFSGIM GLPVYETVSM LQDLGYRPPL SALKP // ID Y1297_NEIG1 Reviewed; 451 AA. AC Q5F786; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE RecName: Full=UPF0210 protein NGO1297 {ECO:0000255|HAMAP-Rule:MF_01221}; GN OrderedLocusNames=NGO1297; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89951.1; -; Genomic_DNA. DR RefSeq; WP_003691602.1; NC_002946.2. DR RefSeq; YP_208363.1; NC_002946.2. DR ProteinModelPortal; Q5F786; -. DR SMR; Q5F786; 7-446. DR EnsemblBacteria; AAW89951; AAW89951; NGO_1297. DR GeneID; 3282113; -. DR KEGG; ngo:NGO1297; -. DR PATRIC; 20335941; VBINeiGon24812_1525. DR HOGENOM; HOG000059201; -. DR KO; K09157; -. DR OMA; EAMTSVC; -. DR OrthoDB; EOG64BQ65; -. DR BioCyc; NGON242231:GI2G-1209-MONOMER; -. DR Proteomes; UP000000535; 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 NGO1297. FT /FTId=PRO_1000066770. SQ SEQUENCE 451 AA; 46335 MW; BC9D96B6660A9839 CRC64; MSIQSGEILE TVKMVADQNF DVRTITIGID LHDCISTDID VLNQNIYNKI TTVGKDLVAT AKHLSAKYGV PIVNQRISVT PIAQIAAATK ADSYVSVAQT LDKAAKAIGV SFIGGFSALV QKGMSPSDEV LIRSVPEAMK TTDIVCSSIN IGSTRAGINM DAVKLAGETI KRTAEITPEG FGCAKIVVFC NAVEDNPFMA GAFHGSGEAD AVINVGVSGP GVVKAALENS DAVSLTEVAE VVKKTAFKIT RVGELIGREA SKMLNIPFGI LDLSLAPTPA VGDSVARILE EMGLSVCGTH GTTAALALLN DAVKKGGMMA SSAVGGLSGA FIPVSEDEGM IAAAEAGVLT LDKLEAMTAV CSVGLDMIAV PGDTPAHTIS GIIADEAAIG MINSKTTAVR IIPVTGKTVG DSVEFGGLLG YAPVMPAKEG SCEVFVNRGG RIPAPVQSMK N // ID Y1674_NEIG1 Reviewed; 148 AA. AC Q5F688; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE RecName: Full=UPF0756 membrane protein NGO1674 {ECO:0000255|HAMAP-Rule:MF_01874}; GN OrderedLocusNames=NGO1674; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01874}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01874}. CC -!- SIMILARITY: Belongs to the UPF0756 family. {ECO:0000255|HAMAP- CC Rule:MF_01874}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90299.1; -; Genomic_DNA. DR RefSeq; WP_003689818.1; NC_002946.2. DR RefSeq; YP_208711.1; NC_002946.2. DR EnsemblBacteria; AAW90299; AAW90299; NGO_1674. DR GeneID; 3281245; -. DR KEGG; ngo:NGO1674; -. DR PATRIC; 20336902; VBINeiGon24812_1995. DR HOGENOM; HOG000021336; -. DR OMA; SKGINWG; -. DR OrthoDB; EOG67DPST; -. DR BioCyc; NGON242231:GI2G-1569-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01874; UPF0756; 1. DR InterPro; IPR007382; UPF0756_TM. DR Pfam; PF04284; DUF441; 1. DR ProDom; PD021096; DUF441_TM; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 148 UPF0756 membrane protein NGO1674. FT /FTId=PRO_0000388908. FT TRANSMEM 10 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 50 70 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 85 105 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. FT TRANSMEM 116 136 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01874}. SQ SEQUENCE 148 AA; 15394 MW; DCCCFE63E1E5C420 CRC64; MNFSFVPLFL VTLILLGVVS NNNSITVSAT ILLLMQQTAL VQFVPLVEKH GLNLGIILLT IGVLSPLVSG KAQVPPVAEF LNFKMISAVF IGIFVAWLAG CGVPLMGRQP VLVTGLLIGT VIGVAFMGGI PVGPLIAADI LSFVAGKV // ID Y1987_NEIG1 Reviewed; 115 AA. AC Q5F5E2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=UPF0102 protein NGO1987 {ECO:0000255|HAMAP-Rule:MF_00048}; GN OrderedLocusNames=NGO1987; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90595.1; -; Genomic_DNA. DR RefSeq; WP_003686873.1; NC_002946.2. DR RefSeq; YP_209007.1; NC_002946.2. DR DNASU; 3282637; -. DR EnsemblBacteria; AAW90595; AAW90595; NGO_1987. DR GeneID; 3282637; -. DR KEGG; ngo:NGO1987; -. DR PATRIC; 20337741; VBINeiGon24812_2397. DR HOGENOM; HOG000016278; -. DR KO; K07460; -. DR OMA; LDIVMQD; -. DR OrthoDB; EOG6PP9TH; -. DR BioCyc; NGON242231:GI2G-1885-MONOMER; -. DR Proteomes; UP000000535; 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 NGO1987. FT /FTId=PRO_1000009236. SQ SEQUENCE 115 AA; 12980 MW; F6519A8E7ACE0768 CRC64; MRLNHKQGTA GEDAALAFLQ SQGCTLLARN WHCAYGEIDL IVKNGGMILF VEVKYRKNQR FGGAAYSISP SKLLKLQRSV EYYLQQNRLT NVPCRLDAVL IEGNRPPEWI KNITG // ID Y1291_NEIG1 Reviewed; 242 AA. AC Q5F792; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Probable transcriptional regulatory protein NGO1291 {ECO:0000255|HAMAP-Rule:MF_00693}; GN OrderedLocusNames=NGO1291; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89945.1; -; Genomic_DNA. DR RefSeq; WP_003689207.1; NC_002946.2. DR RefSeq; YP_208357.1; NC_002946.2. DR ProteinModelPortal; Q5F792; -. DR SMR; Q5F792; 3-238. DR EnsemblBacteria; AAW89945; AAW89945; NGO_1291. DR GeneID; 3282078; -. DR KEGG; ngo:NGO1291; -. DR PATRIC; 20335925; VBINeiGon24812_1517. DR HOGENOM; HOG000228371; -. DR OMA; MTRNGGS; -. DR OrthoDB; EOG6HJ29R; -. DR BioCyc; NGON242231:GI2G-1203-MONOMER; -. DR Proteomes; UP000000535; 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 NGO1291. FT /FTId=PRO_0000175854. SQ SEQUENCE 242 AA; 26074 MW; 0F370DE893C8CFD7 CRC64; MAGHSKWANI QHKKARQDAK RGKIFTRLIK EITVAARMGG GDPGANPRLR LALEKAAENN MPKDNVQRAI DKGTGNLEGV EYIELRYEGY GIGGAALMVD CLTDNKTRTV ADVRHAFTKN GGNLGTDGCV AFNFVHQGYL VFEPGVDEDE LMEAALEAGA EDVVTNDDGS IEVITAPNDW AGVKSALEAA GYKSVDGDVT MRAQNETELS GDDAVKMQKL IDALEDLDDV QDVYTSAVLN LD // ID Y2175_NEIG1 Reviewed; 196 AA. AC Q5F4W9; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=Maf-like protein NGO2175 {ECO:0000255|HAMAP-Rule:MF_00528}; GN OrderedLocusNames=NGO2175; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90768.1; -; Genomic_DNA. DR RefSeq; WP_003690470.1; NC_002946.2. DR RefSeq; YP_209180.1; NC_002946.2. DR ProteinModelPortal; Q5F4W9; -. DR EnsemblBacteria; AAW90768; AAW90768; NGO_2175. DR GeneID; 3282750; -. DR KEGG; ngo:NGO2175; -. DR PATRIC; 20338214; VBINeiGon24812_2629. DR HOGENOM; HOG000241744; -. DR OMA; CAGSFKA; -. DR OrthoDB; EOG6SV5F0; -. DR BioCyc; NGON242231:GI2G-2062-MONOMER; -. DR Proteomes; UP000000535; 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 NGO2175. FT /FTId=PRO_0000267349. FT ACT_SITE 36 36 {ECO:0000255|HAMAP-Rule:MF_00528}. SQ SEQUENCE 196 AA; 21678 MW; 66CCB55E0B0A034E CRC64; MGLELPLVLG TSSVFRREQM ERLGIAFQAA SPDFDETPML GESAPQTALR LAEGKARSLT GRFPGALIVG ADQVAWCDGR QWGKPMNLAN AQKMLMHLSG REIEFYSAVV LLNTVTGRMH RHIDKTVVVM RQLDELHILR YLEREPDAVY CSCAAKSEGL GALLIERIES TDPNALIGLP VFRLVDFLKN EGVDVL // ID Y1946_NEIG1 Reviewed; 280 AA. AC Q5F5H9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE RecName: Full=UPF0276 protein NGO1946 {ECO:0000255|HAMAP-Rule:MF_00697}; GN OrderedLocusNames=NGO1946; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0276 family. {ECO:0000255|HAMAP- CC Rule:MF_00697}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90558.1; -; Genomic_DNA. DR RefSeq; WP_010355671.1; NC_002946.2. DR RefSeq; YP_208970.1; NC_002946.2. DR ProteinModelPortal; Q5F5H9; -. DR SMR; Q5F5H9; 1-274. DR EnsemblBacteria; AAW90558; AAW90558; NGO_1946. DR GeneID; 3282674; -. DR KEGG; ngo:NGO1946; -. DR PATRIC; 20337637; VBINeiGon24812_2345. DR HOGENOM; HOG000281002; -. DR KO; K09930; -. DR OMA; IYSEHLS; -. DR OrthoDB; EOG6X9MK9; -. DR BioCyc; NGON242231:GI2G-1848-MONOMER; -. DR Proteomes; UP000000535; 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 NGO1946. FT /FTId=PRO_1000045471. SQ SEQUENCE 280 AA; 31494 MW; 99170329A35565DC CRC64; MIQHAGLGYR RDLAEDFLSL SENSPICFIE AAPENWLKMG GRARKQFDRV AERLPLALHG LSMSLGGQAP LDTDLIDGIK EMMCRYDCTF FSDHLSYCHD GGHLYDLLPL PFTEEMVHHT ARRIREVQDR LGCRIAVENT SYYLHSPLAE MNEVEFLNAV AREADCGIHL DVNNIYVNAV NHGLLSPEAF LENVDAGRVC YIHIAGHDAE TPELLIDTHG AAVLPTVWDL LELAYTKLPT IPPTLLERDF NFPPFAELEA EVAKIADYQT RAGKEYRRAA // ID Y315_NEIG1 Reviewed; 284 AA. AC Q5F9S5; DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=Nucleotide-binding protein NGO0315 {ECO:0000255|HAMAP-Rule:MF_00636}; GN OrderedLocusNames=NGO0315; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89062.1; -; Genomic_DNA. DR RefSeq; WP_003687703.1; NC_002946.2. DR RefSeq; YP_207474.1; NC_002946.2. DR ProteinModelPortal; Q5F9S5; -. DR EnsemblBacteria; AAW89062; AAW89062; NGO_0315. DR GeneID; 3281722; -. DR KEGG; ngo:NGO0315; -. DR PATRIC; 20333611; VBINeiGon24812_0385. DR HOGENOM; HOG000244885; -. DR KO; K06958; -. DR OMA; VSFGYKY; -. DR OrthoDB; EOG6WHNW8; -. DR BioCyc; NGON242231:GI2G-295-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0315. FT /FTId=PRO_0000107733. 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; 32709 MW; C77D0DD40D367855 CRC64; MKIVLISGLS GSGKSVALRQ MEDLGYFCVD NLPLEMLPSL VSYHIERADE TELAVSVDVR SGIDIAQARE QIAYLRGLGH RVEVLFVEAE EAVLVRRFSE TRRGHPLSNQ DMTLLESLKK EREWLFPLKE IAYCIDTSKM NAQQLRHAVR QWLKVERTGL LVVLESFGFK YGVPNNADFM FDMRSLPNPY YDPELRPYTG MDKPVWDYLD GQPLAQEMVD GIERFVTRWL PRLEDESRSY VTVAIGCTGG QHRSVYIVEK LARRLKGRYE LLIRHRQAQN LSGR // ID Y425_NEIG1 Reviewed; 209 AA. AC O87406; Q5F9G9; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=UPF0070 protein NGO0425; DE AltName: Full=ORF2; GN OrderedLocusNames=NGO0425; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10655208; RA Mehr I.J., Long C.D., Serkin C.D., Seifert H.S.; RT "A homologue of the recombination-dependent growth gene, rdgC, is RT involved in gonococcal pilin antigenic variation."; RL Genetics 154:523-532(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0070 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 TPR repeat. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF058711; AAC63507.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89168.1; -; Genomic_DNA. DR RefSeq; WP_003690875.1; NC_002946.2. DR RefSeq; YP_207580.1; NC_002946.2. DR EnsemblBacteria; AAW89168; AAW89168; NGO_0425. DR GeneID; 3282171; -. DR KEGG; ngo:NGO0425; -. DR PATRIC; 20333863; VBINeiGon24812_0509. DR HOGENOM; HOG000261006; -. DR OMA; KASDEGY; -. DR OrthoDB; EOG6MSS1R; -. DR BioCyc; NGON242231:GI2G-403-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; TPR repeat; KW Transmembrane; Transmembrane helix. FT CHAIN 1 209 UPF0070 protein NGO0425. FT /FTId=PRO_0000214366. FT TRANSMEM 24 42 Helical. {ECO:0000255}. FT REPEAT 161 194 TPR. SQ SEQUENCE 209 AA; 23149 MW; 032AD050FDE577FE CRC64; MAAHLEEQQE LDNFKYFWKT TGKWLFALLI LAALGYLGYT VYQNRAASQN QEAAAVLANI VEKAQNKAPQ SEINAELSKL QQSYPHSISA AQATLMAAAT EFDAQRYDVA EGHLKWVLSN QKDSLIQALA AQRLGVVLLQ QKKYDAALAA LDTPVEADFA PLLMETKGDV YAAQEKSQEA LKNYGQALEK MPQDSVGREL LQMKLDSLK // ID Y244_NEIG1 Reviewed; 60 AA. AC Q5F9Z0; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE RecName: Full=UPF0434 protein NGO0244 {ECO:0000255|HAMAP-Rule:MF_01187}; GN OrderedLocusNames=NGO0244; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88997.1; -; Genomic_DNA. DR RefSeq; WP_002221286.1; NC_002946.2. DR RefSeq; YP_207409.1; NC_002946.2. DR ProteinModelPortal; Q5F9Z0; -. DR SMR; Q5F9Z0; 1-60. DR DNASU; 3281515; -. DR EnsemblBacteria; AAW88997; AAW88997; NGO_0244. DR GeneID; 23782006; -. DR GeneID; 3281515; -. DR KEGG; ngo:NGO0244; -. DR PATRIC; 20333439; VBINeiGon24812_0301. DR HOGENOM; HOG000227338; -. DR KO; K09791; -. DR OMA; ELICHAD; -. DR OrthoDB; EOG6C8N1M; -. DR BioCyc; NGON242231:GI2G-228-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0244. FT /FTId=PRO_0000291115. SQ SEQUENCE 60 AA; 7065 MW; C7E447A4281357A5 CRC64; MEKKFLDILV CPVTKGRLEY HQDKQELWSR QAKLAYPIKD GIPYMLENEA RALSEEELKA // ID Y742_NEIG1 Reviewed; 111 AA. AC Q5F8M8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 63. DE RecName: Full=Nucleoid-associated protein NGO0742 {ECO:0000255|HAMAP-Rule:MF_00274}; GN OrderedLocusNames=NGO0742; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89459.1; -; Genomic_DNA. DR RefSeq; WP_003688693.1; NC_002946.2. DR RefSeq; YP_207871.1; NC_002946.2. DR ProteinModelPortal; Q5F8M8; -. DR SMR; Q5F8M8; 7-100. DR EnsemblBacteria; AAW89459; AAW89459; NGO_0742. DR GeneID; 3281843; -. DR KEGG; ngo:NGO0742; -. DR PATRIC; 20334624; VBINeiGon24812_0884. DR HOGENOM; HOG000293239; -. DR KO; K09747; -. DR OMA; EMGKLTG; -. DR OrthoDB; EOG6DVJWP; -. DR BioCyc; NGON242231:GI2G-699-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0742. FT /FTId=PRO_1000003782. SQ SEQUENCE 111 AA; 11983 MW; 09ECB9D8E9930B1C CRC64; MFGKAGLGGL MKQAQQMQEN MKKAQAKLAE TEIEGEAGNG LVKITMTCAH EVRKIDISPD LIQEAADDKE MLEDLILAAL KSARGKAEET ANKTMGAFTQ DLPPGVGDFF R // ID Y681_NEIG1 Reviewed; 225 AA. AC Q5F8S9; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=UPF0758 protein NGO0681; GN OrderedLocusNames=NGO0681; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89408.1; -; Genomic_DNA. DR RefSeq; WP_003688801.1; NC_002946.2. DR RefSeq; YP_207820.1; NC_002946.2. DR ProteinModelPortal; Q5F8S9; -. DR EnsemblBacteria; AAW89408; AAW89408; NGO_0681. DR GeneID; 3281896; -. DR KEGG; ngo:NGO0681; -. DR PATRIC; 20334460; VBINeiGon24812_0802. DR HOGENOM; HOG000273376; -. DR KO; K03630; -. DR OMA; PHEEFWV; -. DR OrthoDB; EOG6RRKTV; -. DR BioCyc; NGON242231:GI2G-648-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0681. FT /FTId=PRO_0000190710. SQ SEQUENCE 225 AA; 25109 MW; 8D59425DB8626D7C CRC64; MSIKQWPEGE RPREKLLERG AAALSDAELL AILLRVGTRG MSAVDLARYL LQEFGSLGRL MSAEVGKLSA YKGMGTASFT QFAVVREIGR RILEEELQEE ITLSDPDTVA DYLRFHLGQE KVEVSVALLL NRQNQLIAVR ELSRGTVAEN TIYIREIVKL ALDEYADSLI IAHNHPGGSP EPSQEDIMFT RRLAQAMSLV DVSLLDHFIV TSQTVRSFRQ LGLMP // ID YACG_NEIG1 Reviewed; 69 AA. AC Q5F690; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 09-DEC-2015, entry version 68. DE RecName: Full=DNA gyrase inhibitor YacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN Name=yacG {ECO:0000255|HAMAP-Rule:MF_00649}; GN OrderedLocusNames=NGO1672; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW90297.1; 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; AE004969; AAW90297.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003696096.1; NC_002946.2. DR RefSeq; YP_208709.2; NC_002946.2. DR ProteinModelPortal; Q5F690; -. DR EnsemblBacteria; AAW90297; AAW90297; NGO_1672. DR GeneID; 3281270; -. DR KEGG; ngo:NGO1672; -. DR KO; K09862; -. DR OrthoDB; EOG65F8ZX; -. DR BioCyc; NGON242231:GI2G-1566-MONOMER; -. DR Proteomes; UP000000535; 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_0000211708. 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; 7737 MW; 6502317F26D76CFA CRC64; MAESRQTRLQ VKCPTCQTAV VWKPENAFRP FCSQRCKLID LGGWADGKYT VSGQTESLPE ISEPDGAYR // ID YBEY_NEIG1 Reviewed; 171 AA. AC Q5FA84; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 13-APR-2016, entry version 66. 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=NGO0145; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SEQUENCE CAUTION: CC Sequence=AAW88903.1; 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; AE004969; AAW88903.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_003694796.1; NC_002946.2. DR RefSeq; YP_207315.2; NC_002946.2. DR ProteinModelPortal; Q5FA84; -. DR EnsemblBacteria; AAW88903; AAW88903; NGO_0145. DR GeneID; 3281313; -. DR KEGG; ngo:NGO0145; -. DR PATRIC; 20333203; VBINeiGon24812_0184. DR HOGENOM; HOG000132870; -. DR KO; K07042; -. DR OrthoDB; EOG680X6D; -. DR BioCyc; NGON242231:GI2G-133-MONOMER; -. DR Proteomes; UP000000535; 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 1 171 Endoribonuclease YbeY. FT /FTId=PRO_0000284253. 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 171 AA; 19829 MW; 3BB17BEA516718CA CRC64; MKRAKKYPFL TLQRQRFHLN FENASSAAGI PAERDFYRWA WSALKNEYLR ADIGLILLDE EEARAYNRDY RGKDYATNVL SFALNEGEIL PCQVSERLYG DLIICPQVVL KEAAEQGKTP ERHFAHLTIH GTLHLMGYDH IKDDEAEIME AEEIRLMRAA GYPNPYREDG H // ID Y461_NEIG1 Reviewed; 259 AA. AC Q5F9D8; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 53. DE RecName: Full=UPF0246 protein NGO0461 {ECO:0000255|HAMAP-Rule:MF_00652}; GN OrderedLocusNames=NGO0461; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89199.1; -; Genomic_DNA. DR RefSeq; WP_003706583.1; NC_002946.2. DR RefSeq; YP_207611.1; NC_002946.2. DR PRIDE; Q5F9D8; -. DR EnsemblBacteria; AAW89199; AAW89199; NGO_0461. DR GeneID; 3282984; -. DR KEGG; ngo:NGO0461; -. DR PATRIC; 20333956; VBINeiGon24812_0552. DR HOGENOM; HOG000218488; -. DR KO; K09861; -. DR OMA; GLMARYI; -. DR OrthoDB; EOG6423KT; -. DR BioCyc; NGON242231:GI2G-437-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0461. FT /FTId=PRO_0000262035. SQ SEQUENCE 259 AA; 29630 MW; 8008A898A4A93F91 CRC64; MFFVLSPAKN LNEKDPCPVS EFTQPDLLAE SEILMRQLRE LAPQQIAELM HVSDKIALLN AERNAAWHTP FTPENAKQAV FMFNGDVYEG MDANTLNTNQ IQYLQGHVRL LSGLYGLLRP LDLIQPYRLE MGTSFANLRG KNLYEFWGGI ITNLLNDTLA QAGSNTLVNL ASQEYFKSVN TKKLRARLIT PIFKDEKNGK YKIISFYAKR ARGLMVRYAA EHNITDPEML KNFNYEGYAF NDAASNESEW VFMRSEQIK // ID Y791_NEIG1 Reviewed; 91 AA. AC Q5F8I2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE RecName: Full=UPF0250 protein NGO0791 {ECO:0000255|HAMAP-Rule:MF_00659}; GN OrderedLocusNames=NGO0791; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89505.1; -; Genomic_DNA. DR RefSeq; WP_002237935.1; NC_002946.2. DR RefSeq; YP_207917.1; NC_002946.2. DR ProteinModelPortal; Q5F8I2; -. DR EnsemblBacteria; AAW89505; AAW89505; NGO_0791. DR GeneID; 3281959; -. DR KEGG; ngo:NGO0791; -. DR PATRIC; 20334730; VBINeiGon24812_0937. DR HOGENOM; HOG000265101; -. DR KO; K09158; -. DR OMA; KVMGLAK; -. DR OrthoDB; EOG6BGP43; -. DR BioCyc; NGON242231:GI2G-745-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0791. FT /FTId=PRO_1000061876. SQ SEQUENCE 91 AA; 10243 MW; E360DACD6BB66882 CRC64; MTEQENKTSL IEFPCTFPLK VMGAVHPEFE QAVLETVRLH APDTQAHHIT TRPSSKGNYT GATVQVKVEN QEQLDNIYRA LTSHELVKVV L // ID Y569_NEIG1 Reviewed; 182 AA. AC Q5F935; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE RecName: Full=UPF0301 protein NGO0569 {ECO:0000255|HAMAP-Rule:MF_00758}; GN OrderedLocusNames=NGO0569; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89302.1; -; Genomic_DNA. DR RefSeq; WP_003688988.1; NC_002946.2. DR RefSeq; YP_207714.1; NC_002946.2. DR ProteinModelPortal; Q5F935; -. DR EnsemblBacteria; AAW89302; AAW89302; NGO_0569. DR GeneID; 3282197; -. DR KEGG; ngo:NGO0569; -. DR PATRIC; 20334200; VBINeiGon24812_0672. DR HOGENOM; HOG000281193; -. DR KO; K07735; -. DR OMA; IYICAHS; -. DR OrthoDB; EOG6RVFX5; -. DR BioCyc; NGON242231:GI2G-542-MONOMER; -. DR Proteomes; UP000000535; 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 NGO0569. FT /FTId=PRO_0000258844. SQ SEQUENCE 182 AA; 19824 MW; 37C1EFA2F8D166D9 CRC64; MNLSNHFLVA MPDMEDAFFS QSVVYICKHD EDGALGIAIN KPSPITMDMI FSATGKNIPM RMQHDSVMMG GPVQVERGYV VHTPIGNWQS SIGVSDGIAL TSSRDVLENI SREGAVDKAL ISIGYSSWSK GQLERELADN AWLTVPADEH ILFDIPYEHR YAAAFAKLGI DPLALFSGAG HA // ID YIDC_NEIG1 Reviewed; 545 AA. AC Q5F4W6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. 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=NGO2178; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90771.1; -; Genomic_DNA. DR RefSeq; WP_003687191.1; NC_002946.2. DR RefSeq; YP_209183.1; NC_002946.2. DR ProteinModelPortal; Q5F4W6; -. DR EnsemblBacteria; AAW90771; AAW90771; NGO_2178. DR GeneID; 3282747; -. DR KEGG; ngo:NGO2178; -. DR PATRIC; 20338218; VBINeiGon24812_2631. DR HOGENOM; HOG000101822; -. DR KO; K03217; -. DR OMA; ELRHTPF; -. DR OrthoDB; EOG6X6RF2; -. DR BioCyc; NGON242231:GI2G-2065-MONOMER; -. DR Proteomes; UP000000535; 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_1000070124. 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; 60541 MW; A04830BB0B9D46BA CRC64; MDFKRLTAFF AIALVIMIGW EKMFPTPKPV PAPQQAAQKQ AATASAEAAL APATPITVTT DTVQAVIDEK SGDLRRLTLL KYKATGDENK PFVLFGDGKE YTYVAQSELL DAQGNNILKG IGFSAPKKQY TLNGDTVEVR LSAPETNGLK IDKVYTFTKD SYLVNVRFDI ANGSGQTANL SADYRIVRDH SEPEGQGYFT HSYVGPVVYT PEGNFQKVSF SDLDDDAKSG KSEAEYIRKT PTGWLGMIEH HFMSTWILQP KGGQSVCAAG DCRIDIKRRS DKLYSASVSV PLAAIQAGAK AETAVNLYAG PQTTSVIANI ADNLQLAKDY GKVHWFASPL FWLLNQLHNI IGNWGWAIVV LTIIVKAVLY PLTNASYRSM AKMRAAAPKL QTIKEKYGDD RMAQQQAMMQ LYKDEKINPL GGCLPMLLQI PVFIGLYWAL FASVELRQAP WLGWITDLSR ADPYYILPII MAATMFAQTY LNPPPTDPMQ AKMMKIMPLV FSVMFFFFPA GLVLYWVVNN LLTIAQQWHI NRSIEKQRAQ GEVVS // ID YCIB_NEIG1 Reviewed; 176 AA. AC Q5F6A1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=Probable intracellular septation protein A {ECO:0000255|HAMAP-Rule:MF_00189}; GN OrderedLocusNames=NGO1659; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90286.1; -; Genomic_DNA. DR RefSeq; WP_010359130.1; NC_002946.2. DR RefSeq; YP_208698.1; NC_002946.2. DR EnsemblBacteria; AAW90286; AAW90286; NGO_1659. DR GeneID; 3281261; -. DR KEGG; ngo:NGO1659; -. DR PATRIC; 20336864; VBINeiGon24812_1977. DR HOGENOM; HOG000062588; -. DR KO; K06190; -. DR OMA; FWVNFKV; -. DR OrthoDB; EOG6JHRJS; -. DR BioCyc; NGON242231:GI2G-1555-MONOMER; -. DR Proteomes; UP000000535; 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_1000021031. 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; 19922 MW; 5770A90BC082906B CRC64; MKFVSDLLSV ILFFATYTVT KNMIAAAAVA LVAGVVQAAF LYWKHKRLDT MQWVGLVLIV VFGGATIVLG DSRFIMWKPT VLFWCGALFL LGSHLAGKNG LKASIGREIQ LPDAVWGKLT YMWVGFLIFM GIANWFVFTR FEAQWVNYKM FGSTALMLFF FIIQGIYLST YLKKED // ID YIDD_NEIG1 Reviewed; 73 AA. AC Q5F4W4; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE RecName: Full=Putative membrane protein insertion efficiency factor {ECO:0000255|HAMAP-Rule:MF_00386}; GN OrderedLocusNames=NGO2180; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90773.1; -; Genomic_DNA. DR RefSeq; WP_003690475.1; NC_002946.2. DR RefSeq; YP_209185.1; NC_002946.2. DR EnsemblBacteria; AAW90773; AAW90773; NGO_2180. DR GeneID; 3282745; -. DR KEGG; ngo:NGO2180; -. DR PATRIC; 20338222; VBINeiGon24812_2633. DR HOGENOM; HOG000231600; -. DR KO; K08998; -. DR OMA; PFSKGGV; -. DR OrthoDB; EOG61ZTN6; -. DR BioCyc; NGON242231:GI2G-2067-MONOMER; -. DR Proteomes; UP000000535; 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_0000253129. SQ SEQUENCE 73 AA; 8293 MW; 387B1EEC45DBD6CF CRC64; MNFLLSKLLL GLIRFYQYCI SPLIPPRCRY TPTCSQYAVE AVKKYGAFKG LRLAIKRIAR CHPFGGHGHD PVP // ID YQGF_NEIG1 Reviewed; 151 AA. AC Q5F936; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 73. 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=NGO0568; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89301.1; -; Genomic_DNA. DR RefSeq; WP_003706124.1; NC_002946.2. DR RefSeq; YP_207713.1; NC_002946.2. DR ProteinModelPortal; Q5F936; -. DR EnsemblBacteria; AAW89301; AAW89301; NGO_0568. DR GeneID; 3282493; -. DR KEGG; ngo:NGO0568; -. DR PATRIC; 20334198; VBINeiGon24812_0671. DR HOGENOM; HOG000016954; -. DR KO; K07447; -. DR OMA; LYEEWQP; -. DR OrthoDB; EOG6N94FV; -. DR BioCyc; NGON242231:GI2G-541-MONOMER; -. DR Proteomes; UP000000535; 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_0000172102. SQ SEQUENCE 151 AA; 16427 MW; A1B42067CE77BD8B CRC64; MHKIPKGTAL AFDFGEARIG VAQGDAELGL SHPLATVTGG SNDEKFAAIA KLVQEWQPRY FVVGLPVHAD GTEHEMTHLS RKFGRRLNGR FNLPVYWVDE RLSSVCAESL LSEAQVLGKK RKSVLDQVAA QAILHGFLEG GPAECFNGRE G // ID A0A0H4ISK7_NEIG1 Unreviewed; 47 AA. AC A0A0H4ISK7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Polyamine ABC transporter ATP-binding protein {ECO:0000313|EMBL:AKO63604.1}; GN ORFNames=NGO_01035 {ECO:0000313|EMBL:AKO63604.1}, GN NGO_01040 {ECO:0000313|EMBL:AKO63605.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63604.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AKO63604.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63604.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63604.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63605.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63604; AKO63604; NGO_01035. DR EnsemblBacteria; AKO63605; AKO63605; NGO_01040. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AKO63604.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000313|EMBL:AKO63604.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 47 AA; 5615 MW; 83D611885A0164DD CRC64; MNLNKLKNKL FRRPGQRAVI AVPYMPPTWD ETVYISWPEN QPTPLFR // ID A0A0H4IS00_NEIG1 Unreviewed; 59 AA. AC A0A0H4IS00; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Phage protein {ECO:0000313|EMBL:AKO63701.1}; GN ORFNames=NGO_06135 {ECO:0000313|EMBL:AKO63694.1}, GN NGO_06695 {ECO:0000313|EMBL:AKO63701.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63701.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63701.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63701.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63694.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63701.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63694; AKO63694; NGO_06135. DR EnsemblBacteria; AKO63701; AKO63701; NGO_06695. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6200 MW; F6DA0D62A9CB4C50 CRC64; MGDKQGMTKA VAGVMTDAPA DGRKPATASN LPPPYLTGGV QKPKRRAGFR KSSNVTKRT // ID A0A0H4IVF7_NEIG1 Unreviewed; 162 AA. AC A0A0H4IVF7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63725.1}; GN ORFNames=NGO_06995 {ECO:0000313|EMBL:AKO63710.1}, GN NGO_07675 {ECO:0000313|EMBL:AKO63725.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63725.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AKO63725.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63725.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63710.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63725.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63710; AKO63710; NGO_06995. DR EnsemblBacteria; AKO63725; AKO63725; NGO_07675. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 162 AA; 18386 MW; 975307F7A8BBE362 CRC64; MTRPAGFSDC QRVCPDETGF DRRLFRPYAR SLKGQMAKAR ISGKRYRRLS LVSAQADNRP IAPVVCQNTV AGVFFEARFQ QCLLPALAQK SVIISDNARF RRMGALRGTA EKLGHKVLPP APYSPEPNPI EKVWANIKRY LRTVLSDYAR FDDALLSYFD FN // ID A0A0H4ISY6_NEIG1 Unreviewed; 68 AA. AC A0A0H4ISY6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63709.1}; GN ORFNames=NGO_06895 {ECO:0000313|EMBL:AKO63709.1}, GN NGO_09035 {ECO:0000313|EMBL:AKO63764.1}, GN NGO_10220 {ECO:0000313|EMBL:AKO63786.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63709.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63709.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63709.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63709.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63764.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63786.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63709; AKO63709; NGO_06895. DR EnsemblBacteria; AKO63764; AKO63764; NGO_09035. DR EnsemblBacteria; AKO63786; AKO63786; NGO_10220. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 68 AA; 7812 MW; C89807CA912691CF CRC64; MTNFPKKIPL KVLTVFPCGR IVRFFAAAEA ADELKSIARN VGNIERYLRQ AEGILYNFAT LFNKTDYR // ID A0A0H4J5Z1_NEIG1 Unreviewed; 37 AA. AC A0A0H4J5Z1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Polyprotein {ECO:0000313|EMBL:AKO63787.1}; GN ORFNames=NGO_00270 {ECO:0000313|EMBL:AKO63584.1}, GN NGO_10265 {ECO:0000313|EMBL:AKO63787.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63787.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63787.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63787.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63584.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63787.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63584; AKO63584; NGO_00270. DR EnsemblBacteria; AKO63787; AKO63787; NGO_10265. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 37 AA; 3887 MW; 0C6DC60DF94F5403 CRC64; MPPPPEKRKK MPSEDLSDGI CGKTGRAGGS EEDFAPA // ID A0A0H4J5U4_NEIG1 Unreviewed; 99 AA. AC A0A0H4J5U4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63727.1}; GN ORFNames=NGO_07715 {ECO:0000313|EMBL:AKO63727.1}, GN NGO_08235 {ECO:0000313|EMBL:AKO63742.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63727.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AKO63727.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63727.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63727.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63742.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63727; AKO63727; NGO_07715. DR EnsemblBacteria; AKO63742; AKO63742; NGO_08235. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 99 AA; 11498 MW; 644AA4E3587E1DEC CRC64; MQADLAYAYE HITRDYPEAT GAKKGTTIST VSDYFKNIRT RSVHPRLALG YDFGGWRVFS APAVAAGLHQ SLQYYRSRHC RRFRQIHQFR RITPIPQKP // ID A0A0H4IWE3_NEIG1 Unreviewed; 149 AA. AC A0A0H4IWE3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63743.1}; GN ORFNames=NGO_06310 {ECO:0000313|EMBL:AKO63698.1}, GN NGO_08295 {ECO:0000313|EMBL:AKO63743.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63743.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AKO63743.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63743.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63698.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63743.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63698; AKO63698; NGO_06310. DR EnsemblBacteria; AKO63743; AKO63743; NGO_08295. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 51 113 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 149 AA; 16982 MW; 4D599EAEE0C015F4 CRC64; MSTFFRQTAQ AMTAKHIGRF PLSELDQVID WQPIEQYLIR QKTRYLRDRR GRPAHPLSSM FKAVLPGQWH SLSDPELEHS LITRIGFNLF CRFDGPGIPG CSTLCRYRKF RYARAAYFGL LKVGAQSHLK AMCLNLLKAA NRLSAPAAA // ID Q5F7B3_NEIG1 Unreviewed; 506 AA. AC Q5F7B3; Q5F7K4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 49. DE SubName: Full=TspB {ECO:0000313|EMBL:AAW89924.2}; GN ORFNames=NGO_1167 {ECO:0000313|EMBL:AAW89833.2}, GN NGO_1265 {ECO:0000313|EMBL:AAW89924.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89924.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89924.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89924.2}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89833.2; -; Genomic_DNA. DR EMBL; AE004969; AAW89924.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89833; AAW89833; NGO_1167. DR EnsemblBacteria; AAW89924; AAW89924; NGO_1265. DR PATRIC; 20335540; VBINeiGon24812_1335. DR PATRIC; 20335607; VBINeiGon24812_1367. DR HOGENOM; HOG000218809; -. DR OMA; YEYANCL; -. DR OrthoDB; EOG62NX16; -. DR BioCyc; NGON242231:GI2G-1053-MONOMER; -. DR BioCyc; NGON242231:GI2G-1080-MONOMER; -. DR BioCyc; NGON242231:GI2G-1182-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 483 503 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 506 AA; 55907 MW; EC03C753BA309E3A CRC64; MYSFEANANA VKISETLSVD TGQGAKVHKF VPKSSNIYSS DLTKAVDLTH IPTGAKARIN AKITASVSRA GVLSGVGKLV RQGAKFGTRA VPYVGTALLA HDVYETFKED IQARGCRYDP ETDKFVKGYE YANCLWYEDE RRINRTYGCY GVDSSIMRLM PDRSRFPEVK QLMESQMYRL ARPFWNWRKE ELNKLSSLDW NNFVLNRCTF DWNGGGCAVN KGDDFRAGAS FSLGRNPKYK EEMDAKKPEE ILSLKVDADP DKYIEATGYP GYSEKVEVAP GTKVNMGPVT DRNGNPVQVA ATFGRDAQGN TTADVQVIPR PDLTPASAEA PHAQPLPEVS PAENPANNPD PDENPGTRPN PEPDPDLNPD ANPDTDGQPG TSPDSPAVPD RPNGRHRKER KEGEDGGLSC DYFPEILACQ EMGKPSDRMF HDISIPQVTD DKTWSSHNFL PSNGVCPQPK TFHVFGRQYR ASYEPLCVFA EKIRFAVLLA FIIMSAFVVF GSLGGE // ID Q5F549_NEIG1 Unreviewed; 217 AA. AC Q5F549; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90688.1}; GN ORFNames=NGO_0628 {ECO:0000313|EMBL:AAW89356.1}, GN NGO_2087 {ECO:0000313|EMBL:AAW90688.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90688.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW90688.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90688.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89356.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90688.1; -; Genomic_DNA. DR RefSeq; WP_010951093.1; NC_002946.2. DR RefSeq; YP_207768.1; NC_002946.2. DR RefSeq; YP_209100.1; NC_002946.2. DR EnsemblBacteria; AAW89356; AAW89356; NGO_0628. DR EnsemblBacteria; AAW90688; AAW90688; NGO_2087. DR GeneID; 3282830; -. DR GeneID; 3282892; -. DR KEGG; ngo:NGO0628; -. DR KEGG; ngo:NGO2087; -. DR PATRIC; 20334340; VBINeiGon24812_0742. DR HOGENOM; HOG000218644; -. DR OMA; LKRNGWV; -. DR BioCyc; NGON242231:GI2G-1982-MONOMER; -. DR BioCyc; NGON242231:GI2G-596-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24016 MW; ACC0037EDC8B6280 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV ANHRLALAAD GVFEGPAGPG GSYFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADNA EPETLPPAVK KKIMPDGIVY ADSPGSRGKL DAGGFTRCRI NRSKEFADRR NHINGIGDFW NQAKRALRKY NGIDRKPFPP FLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F5M0_NEIG1 Unreviewed; 97 AA. AC Q5F5M0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=DNA-binding competence protein 2 {ECO:0000313|EMBL:AAW89957.1}; DE SubName: Full=DNA-binding competence protein 4 {ECO:0000313|EMBL:AAW90517.1}; GN ORFNames=NGO_1304 {ECO:0000313|EMBL:AAW89957.1}, GN NGO_1902 {ECO:0000313|EMBL:AAW90517.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90517.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW90517.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90517.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89957.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90517.1; -; Genomic_DNA. DR RefSeq; WP_010951237.1; NC_002946.2. DR RefSeq; YP_208369.1; NC_002946.2. DR RefSeq; YP_208929.1; NC_002946.2. DR EnsemblBacteria; AAW89957; AAW89957; NGO_1304. DR EnsemblBacteria; AAW90517; AAW90517; NGO_1902. DR GeneID; 3282102; -. DR GeneID; 3282296; -. DR KEGG; ngo:NGO1304; -. DR KEGG; ngo:NGO1902; -. DR PATRIC; 20335959; VBINeiGon24812_1534. DR HOGENOM; HOG000257817; -. DR OMA; MQRDIFN; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; NGON242231:GI2G-1215-MONOMER; -. DR BioCyc; NGON242231:GI2G-1801-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR InterPro; IPR004509; Competence_ComEA_HhH. DR InterPro; IPR010994; RuvA_2-like. DR SUPFAM; SSF47781; SSF47781; 1. DR TIGRFAMs; TIGR00426; TIGR00426; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000313|EMBL:AAW90517.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 97 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006744782. SQ SEQUENCE 97 AA; 10067 MW; A8C9B060FA64284B CRC64; MKKMFVLFCM LFSCAFSLAA VNINAASQQE LEALPGIGPA KAIAEYRAQN GAFKSVDDLI KVKGIGPAVL AKLKDQASVG APAPKGPAKP VLPAVKK // ID Q5F663_NEIG1 Unreviewed; 320 AA. AC Q5F663; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 55. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90324.1}; GN ORFNames=NGO_1200 {ECO:0000313|EMBL:AAW89860.1}, GN NGO_1703 {ECO:0000313|EMBL:AAW90324.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90324.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW90324.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90324.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89860.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90324.1; -; Genomic_DNA. DR RefSeq; WP_010951214.1; NC_002946.2. DR RefSeq; YP_208272.1; NC_002946.2. DR RefSeq; YP_208736.1; NC_002946.2. DR EnsemblBacteria; AAW89860; AAW89860; NGO_1200. DR EnsemblBacteria; AAW90324; AAW90324; NGO_1703. DR GeneID; 3281830; -. DR GeneID; 3282553; -. DR KEGG; ngo:NGO1200; -. DR KEGG; ngo:NGO1703; -. DR PATRIC; 20335699; VBINeiGon24812_1408. DR HOGENOM; HOG000130878; -. DR OMA; CINADNT; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NGON242231:GI2G-1112-MONOMER; -. DR BioCyc; NGON242231:GI2G-1599-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 152 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 320 AA; 36382 MW; DEEE4813664437D3 CRC64; MRNTVGLDIS KLTFDATAMV GKTEHSAKFD NDSKGLDQFS DRLKSLGYQN LHICMEATGS YYEEVADYFA QYYSVYVVNP LKISKYAESR FKRTKTDKQD AKLIAQYCRS AQESELVKRQ KPTDEQYRLS RMTAAYAQIK SECAAMKNRH HAAKDEEAAK AYAEIIKAMN EQLEVLKEKI KEQTEKPNCK EGVKRLETIP AIGRMTAAVL FHHLTSSKFE TSNKFAAFAG LSPQQKESGT SVRGKGKLTK FGNRKLRAVL FMPAMVAYRI RAFPDFIKRL EEKKKPKKVI IAALMRKLAV IAYHVHKKGG DYDPSRYKSA // ID Q5F8T7_NEIG1 Unreviewed; 217 AA. AC Q5F8T7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 54. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89400.1}; GN ORFNames=NGO_0559 {ECO:0000313|EMBL:AAW89293.1}, GN NGO_0673 {ECO:0000313|EMBL:AAW89400.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89400.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89400.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89400.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89293.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89400.1; -; Genomic_DNA. DR RefSeq; WP_010951083.1; NC_002946.2. DR RefSeq; YP_207705.1; NC_002946.2. DR RefSeq; YP_207812.1; NC_002946.2. DR DNASU; 3282463; -. DR EnsemblBacteria; AAW89293; AAW89293; NGO_0559. DR EnsemblBacteria; AAW89400; AAW89400; NGO_0673. DR GeneID; 3282049; -. DR GeneID; 3282463; -. DR KEGG; ngo:NGO0559; -. DR KEGG; ngo:NGO0673; -. DR PATRIC; 20334174; VBINeiGon24812_0659. DR HOGENOM; HOG000218644; -. DR OMA; FFALEIT; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-533-MONOMER; -. DR BioCyc; NGON242231:GI2G-640-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 23984 MW; 5877A7F55DD402C0 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV ANHRLALAAD EVFEGPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADDA EPETLLPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRLN FGTPSRQLKI LRDRCGI // ID A0A0H4IW84_NEIG1 Unreviewed; 338 AA. AC A0A0H4IW84; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Replication initiation factor {ECO:0000313|EMBL:AKO63693.1}; GN ORFNames=NGO_06130 {ECO:0000313|EMBL:AKO63693.1}, GN NGO_06690 {ECO:0000313|EMBL:AKO63700.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63693.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63693.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63693.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63700.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63693; AKO63693; NGO_06130. DR EnsemblBacteria; AKO63700; AKO63700; NGO_06690. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Initiation factor {ECO:0000313|EMBL:AKO63693.1}; KW Protein biosynthesis {ECO:0000313|EMBL:AKO63693.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 338 AA; 39065 MW; 9857E3B062BF7150 CRC64; MFDDDDFIRA ASAKMEEIFG FGIIEKAKHS GGRFYEGCWL MGTENAQYGR VHYGGQRETM LVELTAVGCN AANIGWESRL FDFLTNAIRP KITRVDIAKD FFNGEYSPNQ AREDRNKGLF TCHHVKPKGE CLGSDWEEED EAKMTSGKTY GIGSRESSKY VRIYEKGKQL GDKTSTWTRF EIEFKAKDIV IPFEVLQTPG EYFGGAYPIC ERFTGSANRI EAVKSKIMID FDTYIERLKK QIGRGINASK AVFPDKSKQE LFEVLEPKHD FLPKKLSFEN YDCSEAKLTP LHEIPSVLKF DQYGMWMDRY IQRQKRGEEQ RYLEKMYDKY ANLPISWA // ID Q5F880_NEIG1 Unreviewed; 273 AA. AC Q5F880; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Integrase {ECO:0000313|EMBL:AAW89607.1}; GN ORFNames=NGO_0881 {ECO:0000313|EMBL:AAW89581.1}, GN NGO_0909 {ECO:0000313|EMBL:AAW89607.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89607.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89607.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89607.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89581.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89607.1; -; Genomic_DNA. DR RefSeq; WP_003706481.1; NC_002946.2. DR RefSeq; YP_207993.1; NC_002946.2. DR RefSeq; YP_208019.1; NC_002946.2. DR EnsemblBacteria; AAW89581; AAW89581; NGO_0881. DR EnsemblBacteria; AAW89607; AAW89607; NGO_0909. DR GeneID; 3281783; -. DR GeneID; 3282231; -. DR KEGG; ngo:NGO0881; -. DR KEGG; ngo:NGO0909; -. DR PATRIC; 20334937; VBINeiGon24812_1038. DR HOGENOM; HOG000023133; -. DR OMA; HHGRYGY; -. DR OrthoDB; EOG664CH4; -. DR BioCyc; NGON242231:GI2G-823-MONOMER; -. DR BioCyc; NGON242231:GI2G-849-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR025948; HTH-like_dom. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13276; HTH_21; 1. DR Pfam; PF13333; rve_2; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 108 270 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 273 AA; 31294 MW; D3195FF6946BDDD4 CRC64; MPSVELLLGI VGLPRSTFYY QLAVQSAEGK YADLKRHIHD IYQRYKGRYG YRRIAAAIRH AGIPVNHKKV SRLMAKTGLK AVIRRRKYRS FKGEVGKVAP NILQRCFHSE KPNEKWVTDV TKFDVGGEKI YLSPIMDLFN GEIVSYRIQT RPTFDLAGEI LKGAPEKPGP SEKPMLHSDQ GWQYQMFFYQ KQLKGNGLVQ SLSRKGNCLD NAAMESFFGT LKSECFHTCK YDSVTESEAA LHEYIRYYNN DRIKLKLKGL SPVQYRIQSL KAA // ID A0A0H4IVY6_NEIG1 Unreviewed; 149 AA. AC A0A0H4IVY6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63588.1}; GN ORFNames=NGO_00385 {ECO:0000313|EMBL:AKO63588.1}, GN NGO_01000 {ECO:0000313|EMBL:AKO63603.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63588.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AKO63588.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63588.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63588.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63603.1; -; Genomic_DNA. DR RefSeq; WP_003705389.1; NC_002946.2. DR RefSeq; YP_009179205.1; NC_002946.2. DR EnsemblBacteria; AKO63588; AKO63588; NGO_00385. DR EnsemblBacteria; AKO63603; AKO63603; NGO_01000. DR GeneID; 26142990; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 51 113 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 149 AA; 17054 MW; BD5B9CAEE0C01679 CRC64; MSTFFRQTAQ AMTAKHIGRF PLSELDQVID WQPIEQYLIR QKTRYLRDRR GRPAHPLSSM FKAVLPGQWH SLSDPELEHS LITRIGFNLF CRFDEPGIPG CSTLCRYRKF RYARAAYFGL LKVGAQSHLK AMCLNLLKAA NRLSAPAAA // ID A0A0H4ISX1_NEIG1 Unreviewed; 119 AA. AC A0A0H4ISX1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63699.1}; GN ORFNames=NGO_05940 {ECO:0000313|EMBL:AKO63689.1}, GN NGO_06090 {ECO:0000313|EMBL:AKO63692.1}, GN NGO_06650 {ECO:0000313|EMBL:AKO63699.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63699.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63699.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63699.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63689.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63692.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63699.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63689; AKO63689; NGO_05940. DR EnsemblBacteria; AKO63692; AKO63692; NGO_06090. DR EnsemblBacteria; AKO63699; AKO63699; NGO_06650. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 14254 MW; FB98BB025FD84F89 CRC64; MIHKPRYIKI VDENGDFTRV LRLHKFPDTS KVFYFEPMFW LKDGRVARKD SLFEVDYIYG ADGCGFLPSN LTEFRKYCRK KHQKFKDDEV LVNRYAVDFL GAKEPPYDDR HVTSVKYFV // ID Q5F6B0_NEIG1 Unreviewed; 114 AA. AC Q5F6B0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW90277.1}; GN ORFNames=NGO_0519 {ECO:0000313|EMBL:AAW89257.1}, GN NGO_1650 {ECO:0000313|EMBL:AAW90277.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90277.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW90277.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90277.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89257.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90277.1; -; Genomic_DNA. DR RefSeq; WP_003695464.1; NC_002946.2. DR RefSeq; YP_207669.1; NC_002946.2. DR RefSeq; YP_208689.1; NC_002946.2. DR EnsemblBacteria; AAW89257; AAW89257; NGO_0519. DR EnsemblBacteria; AAW90277; AAW90277; NGO_1650. DR GeneID; 3281352; -. DR GeneID; 3282929; -. DR KEGG; ngo:NGO0519; -. DR KEGG; ngo:NGO1650; -. DR PATRIC; 20334080; VBINeiGon24812_0612. DR HOGENOM; HOG000071310; -. DR OMA; IAVCWAY; -. DR OrthoDB; EOG62K258; -. DR BioCyc; NGON242231:GI2G-1546-MONOMER; -. DR BioCyc; NGON242231:GI2G-497-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 114 AA; 12664 MW; 6C6AEA132FDD1F89 CRC64; MIGALLKNWK PLLILSAIAF FAVSWQLDRA AQYRRGYGAA VSEVSERLKA AAVEHAEHAR KSSAAYQAQK AAREEKERVR YVQTLKIIEK PVYRNACFDA DGVRELNAAV DDGG // ID A0A0H4IS55_NEIG1 Unreviewed; 232 AA. AC A0A0H4IS55; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 7. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63741.1}; GN ORFNames=NGO_04980 {ECO:0000313|EMBL:AKO63672.1}, GN NGO_08230 {ECO:0000313|EMBL:AKO63741.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63741.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKO63741.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AKO63741.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63672.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63741.1; -; Genomic_DNA. DR RefSeq; WP_030003512.1; NC_002946.2. DR RefSeq; YP_008914851.1; NC_002946.2. DR RefSeq; YP_008914857.1; NC_002946.2. DR EnsemblBacteria; AKO63672; AKO63672; NGO_04980. DR EnsemblBacteria; AKO63741; AKO63741; NGO_08230. DR GeneID; 19592996; -. DR GeneID; 19592998; -. DR KEGG; ngo:NGO0950a; -. DR KEGG; ngo:NGO1553a; -. DR Proteomes; UP000000535; 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; -; 2. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 49 232 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 232 AA; 26193 MW; DA7CE89924891C0E CRC64; MQADLAYAAE RITHDYPEPT GAKKDKKIST VSDYFRNIRT HSVHPRVSVG YDFGSWRIAA DYARYRKWNN SKYSVNIKRV KENNGSGKKL TQDLKTENQE NGTFHAVSSL GLSAVYDFDT GSRFKPYAGV RVSYGHVRHS IDSTKKTTDV ITAPPTTSDG APTTYNANPQ TQNPYHQSDS IRRVGLGVIA GVGFDITPNL TLDTGYRYHN WGRLENTRFK THEASLGMRY RF // ID Q5F7R2_NEIG1 Unreviewed; 164 AA. AC Q5F7R2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89775.1}; GN ORFNames=NGO_0487 {ECO:0000313|EMBL:AAW89225.1}, GN NGO_1108 {ECO:0000313|EMBL:AAW89775.1}, GN NGO_1638 {ECO:0000313|EMBL:AAW90266.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89775.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89775.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89225.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89775.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90266.1; -; Genomic_DNA. DR RefSeq; WP_003693463.1; NC_002946.2. DR RefSeq; YP_207637.1; NC_002946.2. DR RefSeq; YP_208187.1; NC_002946.2. DR RefSeq; YP_208678.1; NC_002946.2. DR EnsemblBacteria; AAW89225; AAW89225; NGO_0487. DR EnsemblBacteria; AAW89775; AAW89775; NGO_1108. DR EnsemblBacteria; AAW90266; AAW90266; NGO_1638. DR GeneID; 3281361; -. DR GeneID; 3282499; -. DR GeneID; 3282960; -. DR KEGG; ngo:NGO0487; -. DR KEGG; ngo:NGO1108; -. DR KEGG; ngo:NGO1638; -. DR HOGENOM; HOG000071229; -. DR OMA; MTVRNTQ; -. DR OrthoDB; EOG61GGGZ; -. DR BioCyc; NGON242231:GI2G-1020-MONOMER; -. DR BioCyc; NGON242231:GI2G-1535-MONOMER; -. DR BioCyc; NGON242231:GI2G-465-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR021739; DUF3310. DR Pfam; PF11753; DUF3310; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 164 AA; 18338 MW; 549C39B77D2570A2 CRC64; MTVRNTQTET VRTEAAPQQG GNTNPGYYKN RAFECVGFAQ YLNFNLGNAF KYIWRHKEKG GREDLEKALR YLERQRAGAP KFKKLKHRRY EKMYAGLKDC GFDGGTEAAL LAVISAAYYI RDGEDNFAWA AACVEDLLEK MPPEAGRAPH PESPMPPETA GGGI // ID Q5F9Y2_NEIG1 Unreviewed; 162 AA. AC Q5F9Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89005.2}; GN ORFNames=NGO_00195 {ECO:0000313|EMBL:AKO63582.1}, GN NGO_0253 {ECO:0000313|EMBL:AAW89005.2}, GN NGO_03975 {ECO:0000313|EMBL:AKO63655.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89005.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89005.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89005.2}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89005.2; -; Genomic_DNA. DR EMBL; AE004969; AKO63582.1; -; Genomic_DNA. DR EMBL; AE004969; AKO63655.1; -; Genomic_DNA. DR RefSeq; WP_025462866.1; NC_002946.2. DR RefSeq; YP_009179204.1; NC_002946.2. DR EnsemblBacteria; AAW89005; AAW89005; NGO_0253. DR EnsemblBacteria; AKO63582; AKO63582; NGO_00195. DR EnsemblBacteria; AKO63655; AKO63655; NGO_03975. DR GeneID; 26142987; -. DR PATRIC; 20333461; VBINeiGon24812_0311. DR HOGENOM; HOG000228640; -. DR OMA; PNECANY; -. DR OrthoDB; EOG657JDZ; -. DR BioCyc; NGON242231:GI2G-237-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 162 AA; 18328 MW; BA66737B36C204EB CRC64; MTRPAGFSDC QRVCPDETGF DRRLFRPYAR SLKGQMAKAR ISGKRYRRLS LVSAQVGNRP IAPMVCQNTV AGVFFEARFQ QCLLPALAQK SVIISDNARF RRMGALRGTA EKLGHKVLPP APCSPEPNPI EKVWANIKRY LRTVLSDYAR FDDALLSYFD FN // ID Q5FAF4_NEIG1 Unreviewed; 227 AA. AC Q5FAF4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 59. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AAW88833.2}; GN ORFNames=NGO_0070 {ECO:0000313|EMBL:AAW88833.2}, GN NGO_11100 {ECO:0000313|EMBL:AKO63806.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88833.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW88833.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW88833.2}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88833.2; -; Genomic_DNA. DR EMBL; AE004969; AKO63806.1; -; Genomic_DNA. DR RefSeq; WP_030003519.1; NC_002946.2. DR RefSeq; YP_008914860.1; NC_002946.2. DR EnsemblBacteria; AAW88833; AAW88833; NGO_0070. DR EnsemblBacteria; AKO63806; AKO63806; NGO_11100. DR GeneID; 19592994; -. DR KEGG; ngo:NGO2060a; -. DR PATRIC; 20333008; VBINeiGon24812_0088. DR HOGENOM; HOG000218831; -. DR OMA; YNQGSTQ; -. DR OrthoDB; EOG68M4G6; -. DR BioCyc; NGON242231:GI2G-62-MONOMER; -. DR Proteomes; UP000000535; 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; -; 2. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 227 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 227 AA; 25693 MW; 31DA362AC402AEFF CRC64; MQADLAYAAE RITHDYPEPT APGKNKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWNDN KYSVDIKELE NKNQNKRDLK TENQENGSFH AVSSLGLSAV YDFKLNDKFK PYIGARVAYG HVRHSIDSTK KITGTLTAYP SDADAAVTVY PDGHPQKNTY QKSNSSRRLG FGAMAGVGID VAPGLTLDAG YRYHNWGRLE NTRFKTHEAS LGMRYRF // ID Q5F7B6_NEIG1 Unreviewed; 320 AA. AC Q5F7B6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89921.1}; GN ORFNames=NGO_1164 {ECO:0000313|EMBL:AAW89830.1}, GN NGO_1262 {ECO:0000313|EMBL:AAW89921.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89921.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89921.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89921.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89830.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89921.1; -; Genomic_DNA. DR RefSeq; WP_010951206.1; NC_002946.2. DR RefSeq; YP_208242.1; NC_002946.2. DR RefSeq; YP_208333.1; NC_002946.2. DR EnsemblBacteria; AAW89830; AAW89830; NGO_1164. DR EnsemblBacteria; AAW89921; AAW89921; NGO_1262. DR GeneID; 3281824; -. DR GeneID; 3281859; -. DR KEGG; ngo:NGO1164; -. DR KEGG; ngo:NGO1262; -. DR PATRIC; 20335599; VBINeiGon24812_1363. DR HOGENOM; HOG000130878; -. DR OMA; VEEDMEQ; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NGON242231:GI2G-1077-MONOMER; -. DR BioCyc; NGON242231:GI2G-1179-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 152 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 320 AA; 36381 MW; 05FF5F0EDE09B722 CRC64; MRNTVGLDIS KLTFDATAMV GKTEHSAKFD NDSKGLDQFS DRLKSLGYQN LHICMEATGS YYEEVADYFA QYYSVYVVNP LKISKYAESR FKRTKTDKQD AKLIAQYCRS AKESELVKRQ KPTDEQYRLS RMTAAYAQIK SECAAMKNRH HAAKDEEAAK AYAQIIKAMN EQLEVLKEKI KEQTEKPNCK EGVKRLETIP AIGRMTAAVL FHHLTSSKFE TSNKFAAFAG LSPQQKESGT SVRGKGKLTK FGNRKLRAVL FMPAMVAYRI RAFPDFIKRL EEKKKPKKVI IAALMRKLAV IAYHVHKKGG DYDPSRYKSA // ID Q5F7Q7_NEIG1 Unreviewed; 62 AA. AC Q5F7Q7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89780.1}; GN ORFNames=NGO_0481 {ECO:0000313|EMBL:AAW89219.1}, GN NGO_1113 {ECO:0000313|EMBL:AAW89780.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89780.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89780.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89780.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89219.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89780.1; -; Genomic_DNA. DR RefSeq; WP_010951056.1; NC_002946.2. DR RefSeq; YP_207631.1; NC_002946.2. DR RefSeq; YP_208192.1; NC_002946.2. DR EnsemblBacteria; AAW89219; AAW89219; NGO_0481. DR EnsemblBacteria; AAW89780; AAW89780; NGO_1113. DR GeneID; 3282517; -. DR GeneID; 3282969; -. DR KEGG; ngo:NGO0481; -. DR KEGG; ngo:NGO1113; -. DR PATRIC; 20333998; VBINeiGon24812_0571. DR HOGENOM; HOG000071225; -. DR OMA; PNTDDEY; -. DR BioCyc; NGON242231:GI2G-1025-MONOMER; -. DR BioCyc; NGON242231:GI2G-459-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 6779 MW; 8119C847393B1C51 CRC64; MPSDLSFILA KELIRSGSIR LSGSTAKGQA GELAVFIRTL RQKPEESEPN TDDEYLIGLL SK // ID Q5F7P5_NEIG1 Unreviewed; 53 AA. AC Q5F7P5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89792.1}; GN ORFNames=NGO_0470 {ECO:0000313|EMBL:AAW89208.1}, GN NGO_1125 {ECO:0000313|EMBL:AAW89792.1}, GN NGO_1621 {ECO:0000313|EMBL:AAW90249.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89792.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89792.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89208.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89792.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90249.1; -; Genomic_DNA. DR RefSeq; WP_003693867.1; NC_002946.2. DR RefSeq; YP_207620.1; NC_002946.2. DR RefSeq; YP_208204.1; NC_002946.2. DR RefSeq; YP_208661.1; NC_002946.2. DR EnsemblBacteria; AAW89208; AAW89208; NGO_0470. DR EnsemblBacteria; AAW89792; AAW89792; NGO_1125. DR EnsemblBacteria; AAW90249; AAW90249; NGO_1621. DR GeneID; 3281429; -. DR GeneID; 3282147; -. DR GeneID; 3282976; -. DR KEGG; ngo:NGO0470; -. DR KEGG; ngo:NGO1125; -. DR KEGG; ngo:NGO1621; -. DR HOGENOM; HOG000071219; -. DR OMA; HIKSIIR; -. DR OrthoDB; EOG60PHMX; -. DR BioCyc; NGON242231:GI2G-1037-MONOMER; -. DR BioCyc; NGON242231:GI2G-1518-MONOMER; -. DR BioCyc; NGON242231:GI2G-448-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 6024 MW; 0A8A3D2EE230D595 CRC64; MSFHPETAYN GGGETEPYGP SPEEIKYRQS PETAETRRMT EKQAEGHIKS IIR // ID Q5F7P3_NEIG1 Unreviewed; 60 AA. AC Q5F7P3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89794.1}; GN ORFNames=NGO_0468 {ECO:0000313|EMBL:AAW89206.1}, GN NGO_1127 {ECO:0000313|EMBL:AAW89794.1}, GN NGO_1619 {ECO:0000313|EMBL:AAW90247.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89794.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89794.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89794.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89206.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89794.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90247.1; -; Genomic_DNA. DR RefSeq; WP_003691535.1; NC_002946.2. DR RefSeq; YP_207618.1; NC_002946.2. DR RefSeq; YP_208206.1; NC_002946.2. DR RefSeq; YP_208659.1; NC_002946.2. DR EnsemblBacteria; AAW89206; AAW89206; NGO_0468. DR EnsemblBacteria; AAW89794; AAW89794; NGO_1127. DR EnsemblBacteria; AAW90247; AAW90247; NGO_1619. DR GeneID; 3281309; -. DR GeneID; 3282431; -. DR GeneID; 3282979; -. DR KEGG; ngo:NGO0468; -. DR KEGG; ngo:NGO1127; -. DR KEGG; ngo:NGO1619; -. DR HOGENOM; HOG000071217; -. DR OMA; YINITIG; -. DR OrthoDB; EOG6RJVFK; -. DR BioCyc; NGON242231:GI2G-1039-MONOMER; -. DR BioCyc; NGON242231:GI2G-1516-MONOMER; -. DR BioCyc; NGON242231:GI2G-446-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 60 AA; 6325 MW; 6C70F8F325C7F023 CRC64; MANIDLTQWD GKTIGAAANP EQGYINITIG SDDLFINIEQ AYAIHAALGE AVAEYEGGAQ // ID Q5F7B0_NEIG1 Unreviewed; 94 AA. AC Q5F7B0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89927.1}; GN ORFNames=NGO_1168 {ECO:0000313|EMBL:AAW89834.1}, GN NGO_1268 {ECO:0000313|EMBL:AAW89927.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89927.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89927.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89927.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89834.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89927.1; -; Genomic_DNA. DR RefSeq; WP_003705965.1; NC_002946.2. DR RefSeq; YP_208246.1; NC_002946.2. DR RefSeq; YP_208339.1; NC_002946.2. DR EnsemblBacteria; AAW89834; AAW89834; NGO_1168. DR EnsemblBacteria; AAW89927; AAW89927; NGO_1268. DR GeneID; 3281949; -. DR GeneID; 3282067; -. DR KEGG; ngo:NGO1168; -. DR KEGG; ngo:NGO1268; -. DR PATRIC; 20335617; VBINeiGon24812_1372. DR HOGENOM; HOG000218812; -. DR OrthoDB; EOG6X112N; -. DR BioCyc; NGON242231:GI2G-1081-MONOMER; -. DR BioCyc; NGON242231:GI2G-1185-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 72 89 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 94 AA; 10010 MW; BF14DD034739D29D CRC64; MFGGRLKNSP SITAKHFLKE NIMKFINTCR KYGAKLAVVT AAPLALAAQA NAALPETAKN ALEAAKADGM EAGWIVVGVF AALFVFSIVK RVMK // ID Q5F7Q6_NEIG1 Unreviewed; 51 AA. AC Q5F7Q6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89781.1}; GN ORFNames=NGO_0480 {ECO:0000313|EMBL:AAW89218.1}, GN NGO_1114 {ECO:0000313|EMBL:AAW89781.1}, GN NGO_1631 {ECO:0000313|EMBL:AAW90259.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89781.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89781.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89781.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89218.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89781.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90259.1; -; Genomic_DNA. DR RefSeq; WP_003689578.1; NC_002946.2. DR RefSeq; YP_207630.1; NC_002946.2. DR RefSeq; YP_208193.1; NC_002946.2. DR RefSeq; YP_208671.1; NC_002946.2. DR EnsemblBacteria; AAW89218; AAW89218; NGO_0480. DR EnsemblBacteria; AAW89781; AAW89781; NGO_1114. DR EnsemblBacteria; AAW90259; AAW90259; NGO_1631. DR GeneID; 3281150; -. DR GeneID; 3281853; -. DR GeneID; 3282966; -. DR KEGG; ngo:NGO0480; -. DR KEGG; ngo:NGO1114; -. DR KEGG; ngo:NGO1631; -. DR HOGENOM; HOG000071224; -. DR OMA; CDEVYKI; -. DR OrthoDB; EOG6G7RD0; -. DR BioCyc; NGON242231:GI2G-1026-MONOMER; -. DR BioCyc; NGON242231:GI2G-1528-MONOMER; -. DR BioCyc; NGON242231:GI2G-458-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 51 AA; 5802 MW; 41FF3EC30C548A75 CRC64; MKKQDRNRLS KKDRRLIKKA MLKAAAKGCD EVYKIAPGLK DGFELLGKQP D // ID Q5F7A8_NEIG1 Unreviewed; 96 AA. AC Q5F7A8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 48. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89929.2}; GN ORFNames=NGO_1170 {ECO:0000313|EMBL:AAW89836.2}, GN NGO_1270 {ECO:0000313|EMBL:AAW89929.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89929.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89929.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89929.2}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89836.2; -; Genomic_DNA. DR EMBL; AE004969; AAW89929.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89836; AAW89836; NGO_1170. DR EnsemblBacteria; AAW89929; AAW89929; NGO_1270. DR PATRIC; 20335621; VBINeiGon24812_1374. DR HOGENOM; HOG000218819; -. DR OMA; YKHLPFP; -. DR OrthoDB; EOG6JDWGV; -. DR BioCyc; NGON242231:GI2G-1083-MONOMER; -. DR BioCyc; NGON242231:GI2G-1187-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 10483 MW; 54E75B84F9AB3A5F CRC64; MNIQLQGHIV GVKKFNGQIE GKSFDYCRLI VATPLDSSQG NALGSSTTEY DFGGSANFEQ FRNAQFPIEA NLNVEIVTTG KTQKLKVIGF QLVKKG // ID Q5F7P7_NEIG1 Unreviewed; 110 AA. AC Q5F7P7; Q5F6D6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 39. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89790.1}; GN ORFNames=NGO_1123 {ECO:0000313|EMBL:AAW89790.1}, GN NGO_1623 {ECO:0000313|EMBL:AAW90251.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89790.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89790.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89790.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89790.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90251.2; -; Genomic_DNA. DR RefSeq; WP_003696914.1; NC_002946.2. DR RefSeq; YP_208202.1; NC_002946.2. DR EnsemblBacteria; AAW89790; AAW89790; NGO_1123. DR EnsemblBacteria; AAW90251; AAW90251; NGO_1623. DR GeneID; 3282254; -. DR KEGG; ngo:NGO1123; -. DR PATRIC; 20335500; VBINeiGon24812_1316. DR PATRIC; 20336786; VBINeiGon24812_1938. DR HOGENOM; HOG000137689; -. DR OMA; GMERYYA; -. DR BioCyc; NGON242231:GI2G-1035-MONOMER; -. DR BioCyc; NGON242231:GI2G-1520-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 12743 MW; 7E7258C9762CD9B4 CRC64; MKYYGTAAYG SPDWGMERYY AREDMRQALD GWEAENRILH ESGLIEIAKK SAREFVRDAD GEPYTQEDWE TYLTEDASRI GKDTEAAMNY AIDEREWFAL AENIGRLANS // ID Q5F7K6_NEIG1 Unreviewed; 361 AA. AC Q5F7K6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89831.1}; GN ORFNames=NGO_1138 {ECO:0000313|EMBL:AAW89805.1}, GN NGO_1165 {ECO:0000313|EMBL:AAW89831.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89831.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89831.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89831.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89805.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89831.1; -; Genomic_DNA. DR RefSeq; WP_010951199.1; NC_002946.2. DR RefSeq; YP_208217.1; NC_002946.2. DR RefSeq; YP_208243.1; NC_002946.2. DR EnsemblBacteria; AAW89805; AAW89805; NGO_1138. DR EnsemblBacteria; AAW89831; AAW89831; NGO_1165. DR GeneID; 3281958; -. DR GeneID; 3282234; -. DR KEGG; ngo:NGO1138; -. DR KEGG; ngo:NGO1165; -. DR PATRIC; 20335536; VBINeiGon24812_1333. DR HOGENOM; HOG000218807; -. DR OMA; SVVECRG; -. DR OrthoDB; EOG6QP0WW; -. DR BioCyc; NGON242231:GI2G-1051-MONOMER; -. DR BioCyc; NGON242231:GI2G-1078-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 361 AA; 40802 MW; 99D25D6BA78C53B4 CRC64; MIYLFTGNMG AGKTPRVVSM ILNNEDGLFK MELEDGTEAD RPLYFCHIDG LDKRKFNARE LAEGQIMSAP LRDVIPEGAV LIVGEAHYTY PVRAAGRPVP PYIQELTELR HHGHTVILMT RHPSQLDIFV RNLVSKHVHL ERKAIGMKQY YWYKCVTSLD NPAGVSGVEA ANWKPPKEAF KYYKSASRHQ KFKKKVPWAV WALIAVVGFV GWKSYGMFQV YSKATDSRIE QEAQKESVVQ TMTEQTASSE TAPFEHFDNL KPEDFVPTLP EKPESKPIYN TVRQVKTFEQ IAGCIDGGKS DCTCYSNQGT PLKEITKIMC KEYVKNGLPF NPYKDERQRT EQAAQSAKAD KPQVLVMGGK S // ID Q5F7B1_NEIG1 Unreviewed; 92 AA. AC Q5F7B1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89926.1}; GN ORFNames=NGO_1142 {ECO:0000313|EMBL:AAW89809.1}, GN NGO_1267 {ECO:0000313|EMBL:AAW89926.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89926.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89926.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89926.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89809.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89926.1; -; Genomic_DNA. DR RefSeq; WP_003689168.1; NC_002946.2. DR RefSeq; YP_208221.1; NC_002946.2. DR RefSeq; YP_208338.1; NC_002946.2. DR EnsemblBacteria; AAW89809; AAW89809; NGO_1142. DR EnsemblBacteria; AAW89926; AAW89926; NGO_1267. DR GeneID; 3282066; -. DR GeneID; 3282237; -. DR KEGG; ngo:NGO1142; -. DR KEGG; ngo:NGO1267; -. DR PATRIC; 20335544; VBINeiGon24812_1337. DR HOGENOM; HOG000218811; -. DR OMA; CLEKHRA; -. DR OrthoDB; EOG6Z3KNP; -. DR BioCyc; NGON242231:GI2G-1055-MONOMER; -. DR BioCyc; NGON242231:GI2G-1184-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 92 AA; 10435 MW; 54B0399BEE6679E7 CRC64; MYCQVGNKCL EKHRAENLYF SLVVPRIKEN GQIIRPEYNG SMWKMSDGQP LRLSLAECSP KDNLQSGLET GRIVFGVLAS VYFVSLLKKV LK // ID Q5F7P1_NEIG1 Unreviewed; 71 AA. AC Q5F7P1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89796.1}; GN ORFNames=NGO_0466 {ECO:0000313|EMBL:AAW89204.1}, GN NGO_1129 {ECO:0000313|EMBL:AAW89796.1}, GN NGO_1617 {ECO:0000313|EMBL:AAW90245.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89796.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89796.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89204.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89796.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90245.1; -; Genomic_DNA. DR RefSeq; WP_003691538.1; NC_002946.2. DR RefSeq; YP_207616.1; NC_002946.2. DR RefSeq; YP_208208.1; NC_002946.2. DR RefSeq; YP_208657.1; NC_002946.2. DR EnsemblBacteria; AAW89204; AAW89204; NGO_0466. DR EnsemblBacteria; AAW89796; AAW89796; NGO_1129. DR EnsemblBacteria; AAW90245; AAW90245; NGO_1617. DR GeneID; 3281587; -. DR GeneID; 3281856; -. DR GeneID; 3282974; -. DR KEGG; ngo:NGO0466; -. DR KEGG; ngo:NGO1129; -. DR KEGG; ngo:NGO1617; -. DR OrthoDB; EOG6VF35Z; -. DR BioCyc; NGON242231:GI2G-1041-MONOMER; -. DR BioCyc; NGON242231:GI2G-1514-MONOMER; -. DR BioCyc; NGON242231:GI2G-444-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 8128 MW; 223299804BE21AB5 CRC64; MSYLEDVKNA LRVIDNLCKE ALKEPESLEG YIDEIRDKAD EADTSLEFLK DVINYGISDL KNVIEVFEDC V // ID Q5F7R1_NEIG1 Unreviewed; 94 AA. AC Q5F7R1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89776.1}; GN ORFNames=NGO_0486 {ECO:0000313|EMBL:AAW89224.1}, GN NGO_1109 {ECO:0000313|EMBL:AAW89776.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89776.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89776.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89776.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89224.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89776.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89224; AAW89224; NGO_0486. DR EnsemblBacteria; AAW89776; AAW89776; NGO_1109. DR PATRIC; 20334008; VBINeiGon24812_0576. DR HOGENOM; HOG000071228; -. DR OMA; MRETCFY; -. DR OrthoDB; EOG6J754X; -. DR BioCyc; NGON242231:GI2G-1021-MONOMER; -. DR BioCyc; NGON242231:GI2G-464-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10175 MW; 0F4A4573BAC02986 CRC64; MRETCFYCNH ADFKTNTGTP VRGFAKCAKA RNAEEKATYY PRTNPCAAGA FQTASGAAVA KRTAVLGEYP PRNAPNLSGK AGKTLWEYPS LPEI // ID Q5F7P8_NEIG1 Unreviewed; 91 AA. AC Q5F7P8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89789.1}; GN ORFNames=NGO_0473 {ECO:0000313|EMBL:AAW89211.1}, GN NGO_1122 {ECO:0000313|EMBL:AAW89789.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89789.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89789.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89789.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89211.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89789.1; -; Genomic_DNA. DR RefSeq; WP_003694994.1; NC_002946.2. DR RefSeq; YP_207623.1; NC_002946.2. DR RefSeq; YP_208201.1; NC_002946.2. DR EnsemblBacteria; AAW89211; AAW89211; NGO_0473. DR EnsemblBacteria; AAW89789; AAW89789; NGO_1122. DR GeneID; 3282265; -. DR GeneID; 3282977; -. DR KEGG; ngo:NGO0473; -. DR KEGG; ngo:NGO1122; -. DR PATRIC; 20333984; VBINeiGon24812_0564. DR OMA; VIATFIC; -. DR BioCyc; NGON242231:GI2G-1034-MONOMER; -. DR BioCyc; NGON242231:GI2G-451-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 91 AA; 8342 MW; 75E05F60D876434D CRC64; MSYLDQPLKH GYGNGNGSGN GSGYGNGYGN GYGNGYGGVG GGGSGSGYGN GNGYSNGSGN GDGDGNGNGS GNGSGYGNGY GNGYSNGSGN G // ID Q5F7P9_NEIG1 Unreviewed; 158 AA. AC Q5F7P9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89788.1}; GN ORFNames=NGO_0474 {ECO:0000313|EMBL:AAW89212.1}, GN NGO_1121 {ECO:0000313|EMBL:AAW89788.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89788.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89788.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89788.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89212.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89788.1; -; Genomic_DNA. DR RefSeq; WP_002255718.1; NC_002946.2. DR RefSeq; YP_207624.1; NC_002946.2. DR RefSeq; YP_208200.1; NC_002946.2. DR EnsemblBacteria; AAW89212; AAW89212; NGO_0474. DR EnsemblBacteria; AAW89788; AAW89788; NGO_1121. DR GeneID; 3282407; -. DR GeneID; 3282973; -. DR KEGG; ngo:NGO0474; -. DR KEGG; ngo:NGO1121; -. DR PATRIC; 20333986; VBINeiGon24812_0565. DR HOGENOM; HOG000071220; -. DR OMA; MGAKRAD; -. DR OrthoDB; EOG6QRWH7; -. DR BioCyc; NGON242231:GI2G-1033-MONOMER; -. DR BioCyc; NGON242231:GI2G-452-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 158 AA; 17221 MW; 3F62B09E22113097 CRC64; MEANKFEVKS LSDLIKVFAG IAADFEAAMG VKRADISTEF DEPQHEPQPP VTVAEQKGIN DFAIGKEVII RTYSAGVWFG VLKQKAGNEV ILTKARRMYS WWAKESISLS GVARHGIRQD GSQICGELDS VWLEAIEIIP VTGGAAESIR TALEVAQS // ID Q5F6B6_NEIG1 Unreviewed; 361 AA. AC Q5F6B6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90271.1}; GN ORFNames=NGO_1263 {ECO:0000313|EMBL:AAW89922.1}, GN NGO_1643 {ECO:0000313|EMBL:AAW90271.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90271.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW90271.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90271.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89922.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90271.1; -; Genomic_DNA. DR RefSeq; WP_010951229.1; NC_002946.2. DR RefSeq; YP_208334.1; NC_002946.2. DR RefSeq; YP_208683.1; NC_002946.2. DR EnsemblBacteria; AAW89922; AAW89922; NGO_1263. DR EnsemblBacteria; AAW90271; AAW90271; NGO_1643. DR GeneID; 3281329; -. DR GeneID; 3281840; -. DR KEGG; ngo:NGO1263; -. DR KEGG; ngo:NGO1643; -. DR PATRIC; 20335861; VBINeiGon24812_1485. DR HOGENOM; HOG000218807; -. DR OMA; TAPFEHS; -. DR OrthoDB; EOG6QP0WW; -. DR BioCyc; NGON242231:GI2G-1180-MONOMER; -. DR BioCyc; NGON242231:GI2G-1540-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 361 AA; 40742 MW; 88C35D6BA78C42A5 CRC64; MIYLFTGNMG AGKTPRVVSM ILNNEDGLFK MELEDGTEAD RPLYFCHIDG LDKRKFNARE LAEGQIMSAP LRDVIPEGAV LIVGEAHYTY PVRAAGRPVP PYIQELTELR HHGHTVILMT RHPSQLDIFV RNLVSKHVHL ERKAIGMKQY YWYKCVTSLD NPAGVSGVEA ANWKPPKEAF KYYKSASRHQ KFKKKVPWAV WALIAVVGFV GWKSYGMFQV YSKATDSRIE QEAQKESVVQ TMTEQTASSE TAPFEHSDNL KPEDFVPTLP EKPESKPIYN TVRQVKTFEQ IAGCIDGGKS DCTCYSNQGT PLKEITKIMC KEYVKNGLPF NPYKDERQRT EQAAQSAKAD KPQVLVMGGK S // ID Q5F7A9_NEIG1 Unreviewed; 65 AA. AC Q5F7A9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89928.1}; GN ORFNames=NGO_1169 {ECO:0000313|EMBL:AAW89835.1}, GN NGO_1269 {ECO:0000313|EMBL:AAW89928.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89928.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89928.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89835.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89928.1; -; Genomic_DNA. DR RefSeq; WP_003689600.1; NC_002946.2. DR RefSeq; YP_208247.1; NC_002946.2. DR RefSeq; YP_208340.1; NC_002946.2. DR EnsemblBacteria; AAW89835; AAW89835; NGO_1169. DR EnsemblBacteria; AAW89928; AAW89928; NGO_1269. DR GeneID; 3281939; -. DR GeneID; 3282172; -. DR KEGG; ngo:NGO1169; -. DR KEGG; ngo:NGO1269; -. DR PATRIC; 20335619; VBINeiGon24812_1373. DR HOGENOM; HOG000218902; -. DR OrthoDB; EOG6K405M; -. DR BioCyc; NGON242231:GI2G-1082-MONOMER; -. DR BioCyc; NGON242231:GI2G-1186-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7304 MW; E9B4487BDB049E35 CRC64; MQKVYVVQSV STGDFLYLSP ETGDIGHTKL ITNADYFYDF EEAVNAGLEE IGNQCEFVVF GFLKD // ID Q5F7Q8_NEIG1 Unreviewed; 75 AA. AC Q5F7Q8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89779.1}; GN ORFNames=NGO_0483 {ECO:0000313|EMBL:AAW89221.1}, GN NGO_1112 {ECO:0000313|EMBL:AAW89779.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89779.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|EMBL:AAW89779.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89779.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89221.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89779.1; -; Genomic_DNA. DR RefSeq; WP_003698261.1; NC_002946.2. DR RefSeq; YP_207633.1; NC_002946.2. DR RefSeq; YP_208191.1; NC_002946.2. DR EnsemblBacteria; AAW89221; AAW89221; NGO_0483. DR EnsemblBacteria; AAW89779; AAW89779; NGO_1112. DR GeneID; 3281851; -. DR GeneID; 3282964; -. DR KEGG; ngo:NGO0483; -. DR KEGG; ngo:NGO1112; -. DR PATRIC; 20334000; VBINeiGon24812_0572. DR HOGENOM; HOG000071226; -. DR OrthoDB; EOG679TGV; -. DR BioCyc; NGON242231:GI2G-1024-MONOMER; -. DR BioCyc; NGON242231:GI2G-461-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 75 AA; 8418 MW; 7AA6A88FBB705CDF CRC64; MNQKQTQCKQ IVDYIRNKGC ITSLEAYQNL KVTQLAARIT DLEGRGFVFA KPKYKVGNCK NPVAHYSIAK SGIEP // ID Q5F6E3_NEIG1 Unreviewed; 327 AA. AC Q5F6E3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 49. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW90244.1}; GN ORFNames=NGO_1130 {ECO:0000313|EMBL:AAW89797.1}, GN NGO_1616 {ECO:0000313|EMBL:AAW90244.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90244.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW90244.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW90244.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89797.1; -; Genomic_DNA. DR EMBL; AE004969; AAW90244.1; -; Genomic_DNA. DR RefSeq; WP_010951195.1; NC_002946.2. DR RefSeq; YP_208209.1; NC_002946.2. DR RefSeq; YP_208656.1; NC_002946.2. DR EnsemblBacteria; AAW89797; AAW89797; NGO_1130. DR EnsemblBacteria; AAW90244; AAW90244; NGO_1616. DR GeneID; 3281565; -. DR GeneID; 3282225; -. DR KEGG; ngo:NGO1130; -. DR KEGG; ngo:NGO1616; -. DR PATRIC; 20335518; VBINeiGon24812_1325. DR HOGENOM; HOG000071215; -. DR OMA; KELSAMY; -. DR OrthoDB; EOG6ND0RP; -. DR BioCyc; NGON242231:GI2G-1042-MONOMER; -. DR BioCyc; NGON242231:GI2G-1513-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 327 AA; 36317 MW; C776DF6862BEE97B CRC64; MQTVATKPTA KQMLAAKRAA KESTRQERAV KRAGTVRNVD RNRLSARSKA QKENIARMLS GAKVSEDEAL TCGIMMRLSL QDMRYACNQE LINFAEHIVK QVQRLGLYCN TDDPANGESV LFACREASQA VAQWTKDFDN LSPNQRQLVL RPLSNLFAAY EEFLKDAPAR LIAEVSAYSL AVRVAKKAMA FLELDGGLIS AVGKVVNGAD SRAEARRLKM PYAEFTGRIL HAANLLYDVG IQADKELSAM YGKPLNPVRP RRISDVRRPM MKMLVADKGG ALVRAVKDSE DVIRHCDNGA GFSCFNWTEH FKRTANLISL MHREAAA // ID Q5F7P4_NEIG1 Unreviewed; 228 AA. AC Q5F7P4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89793.1}; GN ORFNames=NGO_0469 {ECO:0000313|EMBL:AAW89207.1}, GN NGO_1126 {ECO:0000313|EMBL:AAW89793.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89793.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAW89793.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FA 1090 {ECO:0000313|EMBL:AAW89793.1}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The Complete Genome Sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89207.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89793.1; -; Genomic_DNA. DR RefSeq; WP_010951053.1; NC_002946.2. DR RefSeq; YP_207619.1; NC_002946.2. DR RefSeq; YP_208205.1; NC_002946.2. DR EnsemblBacteria; AAW89207; AAW89207; NGO_0469. DR EnsemblBacteria; AAW89793; AAW89793; NGO_1126. DR GeneID; 3282194; -. DR GeneID; 3282978; -. DR KEGG; ngo:NGO0469; -. DR KEGG; ngo:NGO1126; -. DR PATRIC; 20333976; VBINeiGon24812_0560. DR HOGENOM; HOG000071218; -. DR OMA; HATCIRI; -. DR OrthoDB; EOG6TBHF7; -. DR BioCyc; NGON242231:GI2G-1038-MONOMER; -. DR BioCyc; NGON242231:GI2G-447-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 228 AA; 25649 MW; D15FB6AC17E00F42 CRC64; MSLILSVKDE SNFKPCPAGS HHATCIRIID LGTQLVEYQN EQKRQHKILV QWEIDPEGDP EMLMPDGRPY LISRRYTASL HSKSQLATDL KSWRGRDFTP EERDNFDLRN ILGKPCLLSI AHQESSDGKT TYANISAISN KMKSYTPKHP DNAVFAFDLS DPDWANYGLL NEKLREQIAK SPEYAEAVNG RQPPAPPQKQ AQAAEGRPEH PQGNAAPAED IEDDIPFN // ID Q5F6F0_NEIG1 Unreviewed; 324 AA. AC Q5F6F0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 68. DE SubName: Full=D-arabinose 5-phosphate isomerase {ECO:0000313|EMBL:AAW90237.2}; GN ORFNames=NGO_1609 {ECO:0000313|EMBL:AAW90237.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90237.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90237.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6F0; -. DR DNASU; 3281540; -. DR EnsemblBacteria; AAW90237; AAW90237; NGO_1609. DR PATRIC; 20336756; VBINeiGon24812_1923. DR HOGENOM; HOG000264729; -. DR OMA; LMACLMR; -. DR OrthoDB; EOG6RFZWS; -. DR BioCyc; NGON242231:GI2G-1506-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000313|EMBL:AAW90237.2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 34149 MW; 942FE4C22509FF9E CRC64; MAENEKYLDW AREVLHTEAE GLREIAAELD ENFVLAADAL LHCKGRVVIT GMGKSGHIGR KMAATMASTG TPAFFVHPAE AAHGDLGMIV DNDVVAAISN SGESDEITAI IPALKRKDIT LVCITARPDS TMARHADIHI TASVSQEACP LGLAPTTSTT AVMALGDALA VVLLRARAFT PDDFALIHPA GSLGKRLLLR VADIMHKGGG LPAVRLGTPL KGAIVSMSEK GLGMLAVTDG QGCLKGVFTD GDLRRLFQEC DNFTGLSIDE VMHTHPKTIS AERLATEALK VMQANHVNGL LVTDADGVLT GALNMHDLLA ARIV // ID Q5F543_NEIG1 Unreviewed; 713 AA. AC Q5F543; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=FetA {ECO:0000313|EMBL:AAW90694.1}; GN ORFNames=NGO_2093 {ECO:0000313|EMBL:AAW90694.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90694.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90694.1; -; Genomic_DNA. DR RefSeq; WP_010951406.1; NC_002946.2. DR RefSeq; YP_209106.1; NC_002946.2. DR ProteinModelPortal; Q5F543; -. DR EnsemblBacteria; AAW90694; AAW90694; NGO_2093. DR GeneID; 3282824; -. DR KEGG; ngo:NGO2093; -. DR PATRIC; 20338021; VBINeiGon24812_2533. DR HOGENOM; HOG000218731; -. DR KO; K16087; -. DR OMA; FRPNDIA; -. DR OrthoDB; EOG6JQGXW; -. DR BioCyc; NGON242231:GI2G-1988-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00444644}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 23 713 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256181. FT DOMAIN 46 144 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 453 712 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 713 AA; 78864 MW; F24D556E983C90FB CRC64; MNAPFFRLSL LSLTLAAGFA HAAENNANVA LDTVTVKGDR QGSKIRTNIV TLQQKDESTA TDMRELLKEE PSIDFGGGNG TSQFLTLRGM GQNSVDIKVD NAYSDSQILY HQGRFIVDPA LVKVVSVQKG AGSASAGIGA TNGAIIAKTV DAQDLLKGLD KNWGVRLNSG FAGNNGVSYG ASVFGKEGNF DGLFSYNRND EKDYEAGKGF RNVNGGKTVP YSALDKRSYL AKIGTTFGDG DHRIVLSHMK DQHRGIRTVR EEFAVGGENS RITIKRQAPA YRETTQSNTN LAYTGKDLGF VEKLDANAYV LEKKRYSADD KDNGYAGNVK GPNHTRIATR GMNFNFDSRL AEQTLLKYGI NYRHQEIKPQ AFLNSQFKIE DKKDATEEDK KKNRENEKIA KAYRLTNPTK TDTGAYIEAI HEIDGFTLTG GLRYDRFKVK THDGKTVSSS SLNPSFGVIW QPREHWSFSA SHNYASRSPR LYDALQTHGK RGIISIADGT KAERARNTEI GFNYNDGTFA ANGSYFRQTI KDALANPQNR HDSVAVREAV NAGYIKNHGY ELGASYRTGG LTAKVGVSRS KPRFYDTHPK KLLSANPEFG AQTGRTWTAS LAYRFKNPNL EIGWRGRYVQ KATGSILAAG QKDRDGKLEN VVRQGFGVND VFANWKPLGK DTLNVNLSVN NVFDKFYYPH SQRWTNTLPG VGRDVRLGVN YKF // ID Q5F5Y9_NEIG1 Unreviewed; 144 AA. AC Q5F5Y9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Fur family transcriptional regulator {ECO:0000313|EMBL:AAW90398.1}; GN ORFNames=NGO_1779 {ECO:0000313|EMBL:AAW90398.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90398.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the Fur family. CC {ECO:0000256|SAAS:SAAS00578401}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90398.1; -; Genomic_DNA. DR RefSeq; WP_010359353.1; NC_002946.2. DR RefSeq; YP_208810.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y9; -. DR EnsemblBacteria; AAW90398; AAW90398; NGO_1779. DR GeneID; 3282476; -. DR KEGG; ngo:NGO1779; -. DR PATRIC; 20337200; VBINeiGon24812_2136. DR HOGENOM; HOG000014144; -. DR KO; K03711; -. DR OMA; DERSDIG; -. DR OrthoDB; EOG6J48SS; -. DR BioCyc; NGON242231:GI2G-1677-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR CollecTF; EXPREG_00000ec0; -. 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 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 {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00469751}; KW Metal-binding {ECO:0000256|SAAS:SAAS00514465}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 144 AA; 16411 MW; 0C615BCABDA7E8B4 CRC64; MEKFSNIAQL KDSGLKVTGP RLKILDLFEK HAEEHLSAED VYRILLEEGV EIGVATIYRV LTQFEQAGIL QRHHFETGKA VYELDKGDHH DHIVCVKCGE VTEFHNPEIE ALQDKIAEEN GYRIVDHALY MYGVCSDCQA KGKR // ID Q5F5D2_NEIG1 Unreviewed; 371 AA. AC Q5F5D2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501}; DE Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501}; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000256|HAMAP-Rule:MF_02121}; GN ORFNames=NGO_1997 {ECO:0000313|EMBL:AAW90605.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90605.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_02121}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP- CC Rule:MF_02121, ECO:0000256|RuleBase:RU004501}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004502}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004502}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP- CC Rule:MF_02121, ECO:0000256|RuleBase:RU004502}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_02121, CC ECO:0000256|RuleBase:RU004041, ECO:0000256|SAAS:SAAS00558004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90605.1; -; Genomic_DNA. DR RefSeq; WP_003696344.1; NC_002946.2. DR RefSeq; YP_209017.1; NC_002946.2. DR ProteinModelPortal; Q5F5D2; -. DR SMR; Q5F5D2; 1-369. DR EnsemblBacteria; AAW90605; AAW90605; NGO_1997. DR GeneID; 3282627; -. DR KEGG; ngo:NGO1997; -. DR PATRIC; 20337763; VBINeiGon24812_2408. DR HOGENOM; HOG000161376; -. DR KO; K00133; -. DR OMA; SCQGGDY; -. DR OrthoDB; EOG67X1PS; -. DR BioCyc; NGON242231:GI2G-1895-MONOMER; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_02121}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02121, ECO:0000256|RuleBase:RU004501}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121, KW ECO:0000256|RuleBase:RU004501, ECO:0000313|EMBL:AAW90605.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}. FT DOMAIN 2 122 Semialdhyde_dh. FT {ECO:0000259|SMART:SM00859}. FT NP_BIND 9 12 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 37 38 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT NP_BIND 165 166 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT ACT_SITE 135 135 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT ACT_SITE 275 275 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_02121, FT ECO:0000256|PIRSR:PIRSR000148-1}. FT BINDING 73 73 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. FT BINDING 102 102 Phosphate. {ECO:0000256|HAMAP- FT Rule:MF_02121}. FT BINDING 162 162 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02121}. FT BINDING 193 193 NADP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_02121}. FT BINDING 241 241 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02121}. FT BINDING 244 244 Phosphate. {ECO:0000256|HAMAP- FT Rule:MF_02121}. FT BINDING 268 268 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02121}. FT BINDING 351 351 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}. SQ SEQUENCE 371 AA; 39837 MW; 5C95937EFA09002A CRC64; MKVGFVGWRG MVGSVLMQRM KEENDFAHIP EAFFFTSSNV GGAAPDFGQA AKTLLDANDV AELAKMDIIV TCQGGDYTKS VFQALRDSGW NGYWIDAASS LRMKDDAIIA LDPVNRNVID NGLKNGVKNY IGGNCTVSLM LMALGGLFQN DLVEWATSMT YQAASGAGAK NMRELISGMG AIHAQVADEL ADPSSAILDI DRKVSDFLRS EDYPKANFGV PLAGSLIPWI DVDLGNGQSK EEWKGGVETN KILGRSGNPT VIDGLCVRIG AMRCHSQAIT LKLKKDLPVS EIEAILAGAN DWVKVVPNEK EAGIRELTPA KVTGTLSVPV GRIRKLGMGG EYISAFTVGD QLLWGAAEPM RRVLRIVLGS L // ID Q5FAF1_NEIG1 Unreviewed; 219 AA. AC Q5FAF1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Phosphatase {ECO:0000313|EMBL:AAW88836.1}; GN ORFNames=NGO_0073 {ECO:0000313|EMBL:AAW88836.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88836.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88836.1; -; Genomic_DNA. DR RefSeq; WP_003687323.1; NC_002946.2. DR RefSeq; YP_207248.1; NC_002946.2. DR ProteinModelPortal; Q5FAF1; -. DR EnsemblBacteria; AAW88836; AAW88836; NGO_0073. DR GeneID; 3282279; -. DR KEGG; ngo:NGO0073; -. DR PATRIC; 20333022; VBINeiGon24812_0095. DR HOGENOM; HOG000248344; -. DR KO; K01091; -. DR OMA; EAYLETF; -. DR OrthoDB; EOG600DR0; -. DR BioCyc; NGON242231:GI2G-65-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 185 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 219 AA; 23196 MW; 81FB67404FE43A8C CRC64; MTPPKLIIFD WDGTLADTTQ PIIDTMRRSF AECGFPPPEA ERVRSLIGYS LPEIIRALLE MPSEAAVADI ARTYSAHYLN PNNRNMTLFP DAPPCLDKLK AQGFRLAVAT GKGRAGLDNA ISQTATGGYW LATACAGEYP SKPSPEMVFG LCGELGLDPK EALVVGDTAH DLHMAANAGA AAVGVATGAH SREQLLGAPH LAVLDGLSEL PGFLARHYA // ID Q5F9E2_NEIG1 Unreviewed; 162 AA. AC Q5F9E2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Type IV pilin {ECO:0000313|EMBL:AAW89195.1}; GN ORFNames=NGO_0456 {ECO:0000313|EMBL:AAW89195.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89195.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89195.1; -; Genomic_DNA. DR RefSeq; WP_003702442.1; NC_002946.2. DR RefSeq; YP_207607.1; NC_002946.2. DR ProteinModelPortal; Q5F9E2; -. DR SMR; Q5F9E2; 39-157. DR EnsemblBacteria; AAW89195; AAW89195; NGO_0456. DR GeneID; 3282988; -. DR KEGG; ngo:NGO0456; -. DR PATRIC; 20333944; VBINeiGon24812_0546. DR HOGENOM; HOG000218897; -. DR KO; K02655; -. DR OMA; YIEKGYQ; -. DR OrthoDB; EOG6FZ4D4; -. DR BioCyc; NGON242231:GI2G-433-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 18083 MW; 2F63C6EEF1362D1C CRC64; MMSNKMEQKG FTLIEMMIVV TILGIISVIA IPSYQSYIEK GYQSQLYTEM VGINNVLKQF ILKNPQDDND TLKSKLKIFV SGYKMNPKIA KKYSVSVRFV DAEKPRAYRL VGVPNAGTGY TLSVWMNSVG DGYKCRDATS AQAYSDTLSA DSGCEAFSNR KK // ID Q5F5E6_NEIG1 Unreviewed; 259 AA. AC Q5F5E6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. 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 ORFNames=NGO_1983 {ECO:0000313|EMBL:AAW90591.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90591.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90591.1; -; Genomic_DNA. DR RefSeq; WP_003686869.1; NC_002946.2. DR RefSeq; YP_209003.1; NC_002946.2. DR ProteinModelPortal; Q5F5E6; -. DR SMR; Q5F5E6; 4-256. DR EnsemblBacteria; AAW90591; AAW90591; NGO_1983. DR GeneID; 3282641; -. DR KEGG; ngo:NGO1983; -. DR PATRIC; 20337733; VBINeiGon24812_2393. DR HOGENOM; HOG000030427; -. DR KO; K01265; -. DR OMA; VIKDEYH; -. DR OrthoDB; EOG6MWNDS; -. DR BioCyc; NGON242231:GI2G-1881-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90591.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAW90591.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:AAW90591.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 28216 MW; B14DDAE77F9F56C8 CRC64; MNGIIIKTPE EIEKMRELGK LVAEALDYIG QFVKPGITTD EIDKLVYDYH VNVQGGYPAP LHYGNPPYPK SCCTSVNHVI CHGIPDDKPL KEGDIINIDL TIKKDGFHGD SSRMFTVGKV SPIAQRLIDV THASMMAGIE AVKPGATLGG VGYACQQVAE NAGYSVVQEF CGHGIGRGFH EAPQVLHYGK KGQGPVLKPG MIFTVEPMIN QGKRHLRILN DGWTVVTKDR SLSAQWEHEV LVTETGYEIL TVSPATGKP // ID Q5F8L9_NEIG1 Unreviewed; 589 AA. AC Q5F8L9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 92. DE SubName: Full=ATPase {ECO:0000313|EMBL:AAW89468.1}; GN ORFNames=NGO_0753 {ECO:0000313|EMBL:AAW89468.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89468.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89468.1; -; Genomic_DNA. DR RefSeq; WP_003699959.1; NC_002946.2. DR RefSeq; YP_207880.1; NC_002946.2. DR ProteinModelPortal; Q5F8L9; -. DR EnsemblBacteria; AAW89468; AAW89468; NGO_0753. DR GeneID; 3282610; -. DR KEGG; ngo:NGO0753; -. DR PATRIC; 20334652; VBINeiGon24812_0898. DR HOGENOM; HOG000218968; -. DR KO; K07673; -. DR OMA; FLQIQLT; -. DR OrthoDB; EOG6JX7HQ; -. DR BioCyc; NGON242231:GI2G-708-MONOMER; -. DR Proteomes; UP000000535; 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; 3.30.450.40; -; 2. 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; 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. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|SAAS:SAAS00577625}; KW Membrane {ECO:0000256|SAAS:SAAS00577774, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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}. SQ SEQUENCE 589 AA; 66676 MW; 19B1E29133156223 CRC64; MILPTRFSDG IPLSLRLKLL TGLWVGLAAL SVVLTLLLSF RLENAASVIE EAGNLKMQAY RLAYMAGEGS PRAQIDNQIA EFEKSLKRIS QSDAIHPLIP SDNPLAYDLI QSMLIIDWQA NILPPLQAYR RPTQIELYRF AGNIELFLQA LENAGEKNTW WLRRFQWVIM LMTLVSSVLM LFWHQIWVIR PLQALREGAE RIGQRHFDIP VPEDGTPEFK QVGRCFNQMA LRLKTLYDDL EGQVAEQTHN LEKQNRNLTL LYRTTRDLHQ SYTPRQAAEE FLNHILPAVG AQSGNICLEN GSDTDISVHT AEHGKKPPLE KYHDETFPIE YQNEKLGMLS LGFSDGTSLT GDDRTLLQTL IRQLGVSLAG AKQEEEKRLL AVLQERNLIA QGLHDSIAQA LTFLNLQVQM LETAFAENKR EEAAENIGFI KTGVQECYED VRELLLNFRT KISNKEFPEA VADLFARFTQ QTGITVETVW ENGSFLPTQD EQLQMIFILQ ESLSNIRKHA RATHVKFTLS EYGGRFTMTI QDNGQGFDTE KIGEPTGSHV GLHIMQERAK RIRAVLEIRS QAQQGTTVSL TGAPKESLP // ID A0A0H4J5X7_NEIG1 Unreviewed; 32 AA. AC A0A0H4J5X7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=EamA-like transporter family protein {ECO:0000313|EMBL:AKO63772.1}; GN ORFNames=NGO_09425 {ECO:0000313|EMBL:AKO63772.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63772.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63772.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63772; AKO63772; NGO_09425. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 32 AA; 3512 MW; 43F570B9D00003D1 CRC64; MAVVFLDERP NTQEWIGLGL VTAGVLTLAL KR // ID Q5F824_NEIG1 Unreviewed; 398 AA. AC Q5F824; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 81. DE RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020}; GN ORFNames=NGO_0977 {ECO:0000313|EMBL:AAW89663.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89663.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020, CC ECO:0000256|SAAS:SAAS00314496}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP- CC Rule:MF_00020, ECO:0000256|RuleBase:RU003835, CC ECO:0000256|SAAS:SAAS00589723}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89663.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F824; -. DR PRIDE; Q5F824; -. DR EnsemblBacteria; AAW89663; AAW89663; NGO_0977. DR PATRIC; 20335152; VBINeiGon24812_1145. DR HOGENOM; HOG000288399; -. DR OMA; IDMANEK; -. DR OrthoDB; EOG69975F; -. DR BioCyc; NGON242231:GI2G-905-MONOMER; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00589711}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00421397}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00589699, KW ECO:0000313|EMBL:AAW89663.2}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00539098}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00539034}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00589711}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00589699, KW ECO:0000313|EMBL:AAW89663.2}. FT NP_BIND 206 210 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT NP_BIND 281 283 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT NP_BIND 329 333 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT METAL 384 384 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00020}. FT SITE 239 239 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00020}. SQ SEQUENCE 398 AA; 42405 MW; 11D00D5073881996 CRC64; MSQKLILVLN CGSSSLKGAV LDNGSGEVLL SCLAEKLNLP DAYITFKVNG EKHKVDLSAH PDHTGAVEAL MEELEAHGLD SRIGAIGHRV VSGGELYNES ILVDDEVIAG IEKCIPLAPL HNPAHLLGLR AAQSIFKGLP NVVVFDTSFH QTMPEVAYKY AVPQELYEKY GLRRYGAHGT SYRFVADETA HFLGKDKKDL RMVIAHLGNG ASITAVANGE SRDTSMGLTP LEGLVMGTRS GDIDPSVFGF LAENANMTIA QITDMLNKKS GLLGISGLSN DCRTIEEEAA KGHKGAKLAL DMFIYRLAKY IGSMAVAAGG LDALVFTGGI GENSDIIRER VIGYLGFLGL NIDQEANLKA RFGNAGVITT ADSKAVAVVI PTNEELMIAH DTARLSGL // ID Q5F9Q0_NEIG1 Unreviewed; 339 AA. AC Q5F9Q0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042}; DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042}; GN ORFNames=NGO_0343 {ECO:0000313|EMBL:AAW89087.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89087.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89087.1; -; Genomic_DNA. DR RefSeq; WP_003706641.1; NC_002946.2. DR RefSeq; YP_207499.1; NC_002946.2. DR ProteinModelPortal; Q5F9Q0; -. DR MEROPS; S26.001; -. DR EnsemblBacteria; AAW89087; AAW89087; NGO_0343. DR GeneID; 3281755; -. DR KEGG; ngo:NGO0343; -. DR PATRIC; 20333683; VBINeiGon24812_0419. DR HOGENOM; HOG000003674; -. DR KO; K03100; -. DR OMA; NTDMFRS; -. DR OrthoDB; EOG6KDKTM; -. DR BioCyc; NGON242231:GI2G-322-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU362042}; KW Membrane {ECO:0000256|RuleBase:RU362042}; KW Protease {ECO:0000256|RuleBase:RU362042}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 37573 MW; 8C8CCAF255DBC949 CRC64; MNTMLMSGAA AALLAGIILY FKSDKKRQEN GEWSSGLEYA YILTAVGVFA ALSLFMSFTA VFLIFVVLCG TAWGVYKYRL KTHPEISESS HFGDYFGSFF PTVLVLFLIR SFIAEPFQIP SSSMRPGLIK GDFILVGKFS YGLRVPVLNN VFIPTGKIER GDVVVFNYPL QPEMTYIKRI VGIPGDIVEY RDKVLTVNGK PASDIPDGTY RYPDDTDPSE IHNTDMFRSG LDGKSFNILK KEGQPAVSLP VLGKYTSDIM SENGYSIDQS GLNHCQYADD GSGFVCKVPE GRYFAMGDNR DNSADSRYWG FVDDKLVVGK AMFILMNFGD FGRAGTAIR // ID Q5F950_NEIG1 Unreviewed; 1206 AA. AC Q5F950; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAW89287.1}; GN ORFNames=NGO_0553 {ECO:0000313|EMBL:AAW89287.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89287.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89287.1; -; Genomic_DNA. DR RefSeq; WP_010951080.1; NC_002946.2. DR RefSeq; YP_207699.1; NC_002946.2. DR ProteinModelPortal; Q5F950; -. DR EnsemblBacteria; AAW89287; AAW89287; NGO_0553. DR GeneID; 3282081; -. DR KEGG; ngo:NGO0553; -. DR PATRIC; 20334158; VBINeiGon24812_0651. DR HOGENOM; HOG000071306; -. DR KO; K16087; -. DR OMA; NRNYIDP; -. DR OrthoDB; EOG6FBWT1; -. DR BioCyc; NGON242231:GI2G-527-MONOMER; -. DR Proteomes; UP000000535; 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; -; 4. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010916; TonB_box_CS. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF07715; Plug; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00444644, KW ECO:0000256|SAAS:SAAS00447760}; KW Receptor {ECO:0000313|EMBL:AAW89287.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357, KW ECO:0000256|SAAS:SAAS00444615}; KW Transmembrane {ECO:0000256|SAAS:SAAS00447760}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00447760}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 1206 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256076. FT DOMAIN 66 167 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 923 1203 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 1206 AA; 136535 MW; E413D309FF968C58 CRC64; MMSGFSPKPK TIILSLAGAF GALAFADTPN NTEQQKELNT IVVHGKRSAD QKGADDVYYK NVSNAYVGKE YLERYRVQSA GDVLKGLNGV YNMNTRTAGG AITPNIRGIT GKGRIPVTID GTEQTIDVWM NNYGVGDRNY LDPALFRSIA VEKSPALTRG VKSGVGGAMS IRTIEPSDII PEGRNWGIEV KTEFSGNTVA QKNDLRQFLG RDYRTLSPIG ATADGVSGMP DVLTGYTGKP SPTALLLDEG IADTKFSGGK SHTNFKDDRQ LMLSAAFKTD ITDGLAAYSH RQKGNYYAGK RGYQSYLNNP IYGADACYDQ YPDKSWREKD ILCKSSASLV PNMAVLFRPG EEIMNSHTDT KILLLKNNWY LPDNQKISLQ YMDNKIGFGE INPLITAWIL GFAEQSLNEP VQQAPGIGTK IDSKTYKIGY EWKPQNNKWI DLQADMWRVK TDSNRHQSGG PVVGVITSDF DYDLWYWCNI RKKPSPNLRG ESCESAMTWN AYGSARTHEE VLRMIEDTPD KIARKLAEYD ENNRAITDRW MGHTGGYYTI TPADKNVLTD QTNQIGKMMN LAELKQKLNQ ERYYIEHPDR IIVPGARQRT DVVRNGFNLS NRLRLSDKLS LTLAADYQRE TLEERTDTAD SNDLMNTFGV LTRMAALGGP QSAKKREWGA NLVFDWKPTS RLNIQAGVRY QNYKGNNIEL ARQRAARNPW YQYGLGSDSY VTGLMMPYYE LADEEDIANQ KRMLQLYDPD RADGQVAEYQ DLNRRFKEKN GYDFDPHDTL VGQDTRFYAK SDGNFVQYAD GNKNTDVLYV LRRKQIIPMN AGKFDPGKVQ ITPEMYRERV NNPQGKSGSY RRYIPGSHIY ITPGSVREEM ERMANENQIP SKEDNNQALE FNSDLNRTAW IRHQFGEADR WRMPQEQRAH SWSPMLAVSY DLADNHRLFA RYARMSRFPS LYELTAATGS GGLYGSETVA EYSLKPEKST NWEVGYNFNF APHFAKLRQG DLRLTYYSNK IKNQIDTSNE DGGMIQYDKA VSKGVELQSR LDSGRFFASF GGTYRLKHMV CDKGIAFKFD YYLQRVPECL EGGFGLSRFF QSLQPKYSLT LDVGTRFFNE KLELGMRAIH HSKAERRNYD KLIADGAGQV YARNGKPYGW HAATLLDAYA RYRIGKHIDL NFSVTNLANR YYLDPMSSTP VPGPGRTITF GIKGRF // ID Q5F5N0_NEIG1 Unreviewed; 404 AA. AC Q5F5N0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=Sodium:glutamate symporter {ECO:0000313|EMBL:AAW90507.1}; GN ORFNames=NGO_1890 {ECO:0000313|EMBL:AAW90507.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90507.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90507.1; -; Genomic_DNA. DR RefSeq; WP_010951365.1; NC_002946.2. DR RefSeq; YP_208919.1; NC_002946.2. DR EnsemblBacteria; AAW90507; AAW90507; NGO_1890. DR GeneID; 3282270; -. DR KEGG; ngo:NGO1890; -. DR PATRIC; 20337480; VBINeiGon24812_2271. DR HOGENOM; HOG000282013; -. DR KO; K03312; -. DR OMA; PTAMVNM; -. DR OrthoDB; EOG6FRCSX; -. DR BioCyc; NGON242231:GI2G-1791-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 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; 43023 MW; 8C57046AD5EBCF74 CRC64; MEWAFNSYYT LIAATLVLLV GKVLVKKIKI LRDFNIPEPV AGGLIAAIIL FALHEAYGVS FKFEKPLQNA FMLIFFTSIG LSADFSRLKA GGLPLVVFTA IVGGFILVQN FVGVGLATAL GLDPLIGLIT GSVSLTGGHG TSGAWGPNFE TQYGLVGATG LGIASVTFGL VFGGLIGGPV ARRLINKMGR KPVENTKQDQ DDNADDVFEQ AKRTRLITAE SAVETLAMFA ACLAFAEIMD GFDKEYLFDL PKFVWCLFGG VVIRNILTAA FKVNMFDRAI DVFGNASLSL FLAMALLNLK LWELTGLAGS VTVILAVQTA VMVLYATFVT YVFMGRDYDA AVLAAGHCGF GLGATPTAVA NMQSVTHTFG ASHKAFLIVP MVGAFFVDLI NAAILTGFVN FFKG // ID A0A0H4IT61_NEIG1 Unreviewed; 53 AA. AC A0A0H4IT61; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Guanylate cyclase {ECO:0000313|EMBL:AKO63759.1}; GN ORFNames=NGO_08950 {ECO:0000313|EMBL:AKO63759.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63759.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63759.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63759; AKO63759; NGO_08950. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 5738 MW; 20B02F4AA1881A88 CRC64; MQNIKSGKRL KIDTVTQSKT GFCPNAGADL PLTAAEQPDR RPSLSVKPPF TPK // ID A0A0H4IV14_NEIG1 Unreviewed; 397 AA. AC A0A0H4IV14; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63630.1}; GN ORFNames=NGO_02965 {ECO:0000313|EMBL:AKO63630.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63630.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63630.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63630; AKO63630; NGO_02965. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. 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; 2.40.170.20; -; 1. DR InterPro; IPR030149; FcuA/FatA. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR PANTHER; PTHR32552:SF14; PTHR32552:SF14; 1. DR Pfam; PF00593; TonB_dep_Rec; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 143 394 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 397 AA; 44409 MW; 9CCCFDF2525C45C0 CRC64; MAANQYHTGT ARLTDQYFRT LSMNLTARGE FETGPVTHNW STAFDRVIRQ RKTINGSGNG NSKIEVKANE NIANQLASFK ADYPNSWANS ANLDANIKVN SLALSDTLGF VDNKYPLTLG GRFQAVEYTD KKKSQSGDAK RFSPMLMAAW VPQPDLVVCG NYMEDLERAD IKTDDSGETT MAKPRVSRQF EIGVRKNWGD FVTTLNAFQI KRPGYWRGNT KKGTDFAAYK AAGGAAGDEQ GMERNRGIEF NAYANLLNKT LRPTFGVMYL QSSVKNYPNA RDMLVNGVQV ANPRVIVKTG VERDTPFAKG LSLNGNVSYF GKSYQDTQKQ YAFPSYTLVD VGARYKTKLG KNTLTVSSSV ENLFNKNYWQ VQRGQFDRSF AVVGLPRTYW LKAELDF // ID A0A0H4IVM3_NEIG1 Unreviewed; 29 AA. AC A0A0H4IVM3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63805.1}; GN ORFNames=NGO_11030 {ECO:0000313|EMBL:AKO63805.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63805.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63805.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63805; AKO63805; NGO_11030. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 29 AA; 3013 MW; DB78E572BE1235D2 CRC64; MLREGIEAAL IVGIVAGFLK QSGHSKTDA // ID A0A0H4J5W0_NEIG1 Unreviewed; 134 AA. AC A0A0H4J5W0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Sugar transporter {ECO:0000313|EMBL:AKO63747.1}; GN ORFNames=NGO_08320 {ECO:0000313|EMBL:AKO63747.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63747.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63747.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63747; AKO63747; NGO_08320. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR InterPro; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sugar transport {ECO:0000313|EMBL:AKO63747.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000313|EMBL:AKO63747.1}. FT TRANSMEM 17 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 127 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 134 AA; 14388 MW; D6B6C3699ABB3795 CRC64; MICSFILAKV PNKYHKAGYF GCLALGALGF FSIFFIYNQY ALILSYILIG IAWAGIITYP LTIVANALSG KHMDTYLGLF NGSVCMPQIV ASLLSFVLFP MLGGHQATMF LVAGAVLLLG AFSVCLIKEI HGGV // ID Q5F7C2_NEIG1 Unreviewed; 217 AA. AC Q5F7C2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 46. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89915.1}; GN ORFNames=NGO_1256 {ECO:0000313|EMBL:AAW89915.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89915.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89915.1; -; Genomic_DNA. DR RefSeq; WP_010951225.1; NC_002946.2. DR RefSeq; YP_208327.1; NC_002946.2. DR EnsemblBacteria; AAW89915; AAW89915; NGO_1256. DR GeneID; 3281786; -. DR KEGG; ngo:NGO1256; -. DR PATRIC; 20335845; VBINeiGon24812_1477. DR HOGENOM; HOG000218644; -. DR KO; K07488; -. DR OMA; IKECEFR; -. DR BioCyc; NGON242231:GI2G-1173-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24091 MW; 75FFAC4A14CE2F34 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFGGPAGPG GSYFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADNA EPETLLPAVK KKIMPDGIVY ADSPGSRGKL DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRFN FGTPSRQLKI LRDWCGI // ID Q5F8Y0_NEIG1 Unreviewed; 916 AA. AC Q5F8Y0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. 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 ORFNames=NGO_0629 {ECO:0000313|EMBL:AAW89357.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89357.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89357.1; -; Genomic_DNA. DR RefSeq; WP_003692988.1; NC_002946.2. DR RefSeq; YP_207769.1; NC_002946.2. DR ProteinModelPortal; Q5F8Y0; -. DR SMR; Q5F8Y0; 38-533. DR EnsemblBacteria; AAW89357; AAW89357; NGO_0629. DR GeneID; 3282891; -. DR KEGG; ngo:NGO0629; -. DR PATRIC; 20334342; VBINeiGon24812_0743. DR HOGENOM; HOG000076278; -. DR KO; K02469; -. DR OMA; ETVDWVP; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; NGON242231:GI2G-597-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 101385 MW; 3704364191D0F844 CRC64; MTDATIRHDH KFALETLPVS LEDEMRKSYL DYAMSVIVGR ALPDVRDGLK PVHRRVLYAM HELKNNWNAA YKKSARIVGD VIGKYHPHGD SAVYDTIVRM AQNFAMRYVL IDGQGNFGSV DGLAAAAMRY TEIRMAKISH EMLADIEEET VNFGPNYDGS EHEPLVLPTR FPTLLVNGSS GIAVGMATNI PPHNLTDTIN ACLRLLDEPK TEIDELIDII QAPDFPTGAT IYGLGGVREG YKTGRGRVVI RGKTHIEPIG KNGEREAIVI DEIPYQVNKA KLVEKIGDLV REKTLEGISE LRDESDKSGM RVVIELKRNE NAEVVLNQLY KLTPLQDSFG INMVVLVDGQ PRLLNLKQIL SEFLRHRREV VTRRTLFRLK KARHEGHIAE GKAVALSNID EIIKLIKESP NAAEAKEKLL ARPWRSSLVE EMLTRSGLDL EMMRPEGLAA NIGLKKQGYY LSEIQADAIL RMSLRNLTGL DQKEIIESYK 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 DLEDETADNE NTLPSGKNGV RPSGRGSGGL RGMRLPADGK IVSLITFAPE TEESGLQVLT ATANGYGKRT PIADYSRKNK GGQGSIAINT GERNGDLVAA TLVGETDDLM LITSGGVLIR TKVEQIRETG RAAAGVKLIN LDEGETLVSL ERVAEDESEL SGASVISNVT EPEAEN // ID Q5FA63_NEIG1 Unreviewed; 308 AA. AC Q5FA63; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW88924.1}; GN ORFNames=NGO_0168 {ECO:0000313|EMBL:AAW88924.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88924.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88924.1; -; Genomic_DNA. DR RefSeq; WP_010951005.1; NC_002946.2. DR RefSeq; YP_207336.1; NC_002946.2. DR ProteinModelPortal; Q5FA63; -. DR TCDB; 3.A.1.15.10; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAW88924; AAW88924; NGO_0168. DR GeneID; 3281403; -. DR KEGG; ngo:NGO0168; -. DR PATRIC; 20333257; VBINeiGon24812_0211. DR HOGENOM; HOG000180308; -. DR KO; K02077; -. DR OMA; HAWQNVA; -. DR OrthoDB; EOG6B3601; -. DR BioCyc; NGON242231:GI2G-154-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|RuleBase:RU003512}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 308 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256256. SQ SEQUENCE 308 AA; 33728 MW; 0C0EC0A7B5CB4043 CRC64; MKHLKLTLIA ALLATAATAA PLPVVTSFSI LGDVAKQIGG ERVAVQSLVG ANQDTHAYHM TSGDIKKIRS AKLVLLNGLG LEAADIQRAV EQSKVSYAEA TKGIQPLKAE EEGGHHHDHH HDHDHDHEGH HHDHGEYDPH VWNDPVLMSD YAQNVAETLI KADPEGKVYY QQRLGNYQMQ LKKLHSDAQA AFNAVPAAKR KVLTGHDAFS YMGNRYNISF IAPQGVSSEA EPSAKQVAAI IRQIKREGIK AVFTENIKDT RMVDRIAKET GVNVSGKLYS DALGNAPADT YIGMYRHNVK ALTNAMKQ // ID Q5F8B1_NEIG1 Unreviewed; 378 AA. AC Q5F8B1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 86. 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}; GN ORFNames=NGO_0875 {ECO:0000313|EMBL:AAW89576.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89576.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89576.1; -; Genomic_DNA. DR RefSeq; WP_003688516.1; NC_002946.2. DR RefSeq; YP_207988.1; NC_002946.2. DR ProteinModelPortal; Q5F8B1; -. DR EnsemblBacteria; AAW89576; AAW89576; NGO_0875. DR GeneID; 3281845; -. DR KEGG; ngo:NGO0875; -. DR PATRIC; 20334923; VBINeiGon24812_1031. DR HOGENOM; HOG000034029; -. DR KO; K01589; -. DR OMA; DSPCGQV; -. DR OrthoDB; EOG6QZMX7; -. DR BioCyc; NGON242231:GI2G-818-MONOMER; -. DR UniPathway; UPA00074; UER00942. DR Proteomes; UP000000535; 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:UP000000535}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01928, KW ECO:0000256|RuleBase:RU361200}; 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:UP000000535}. 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; 41076 MW; D431D6CE4BFBF11B CRC64; MNTPPILPPA MLGILGGGQL GRMFAVAAKT MGYKVTVLDP DPNAPAAEFA DRHLCAPFDD RAALDELAKC AAVTTEFENV NADAMRSLAK HTNVSPSGDC VSIAQNRIQE KAWIRKAGLQ TAPYQAVCKA EDITEASAQF LPGILKTATL GYDGKGQIRV KTLDELKAAF AEHGGVDCVL EKMVDLRGEI SVIVCRLNDE NVQTFDPAEN IHENGILAYS IVPARLSADV QQQARQTAQR LADELDYVGV LAVEMFVVGD THELLVNETA PRTHNSGHHT IDACAADQFQ QQVRIMCNLP PADTKLLSPC CMANILGDVW QEDGGEPDWL PLQSRPNAHL HLYGKKTAQK GRKMGHFTVL TTDSDTAFQE AKKLHQSL // ID A0A0H4IRU7_NEIG1 Unreviewed; 123 AA. AC A0A0H4IRU7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63646.1}; GN ORFNames=NGO_03830 {ECO:0000313|EMBL:AKO63646.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63646.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63646.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63646; AKO63646; NGO_03830. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 123 AA; 13256 MW; BEB7B21749EE9D9D CRC64; MNSLKTDGVY SLPTAVGSSN LPVENTACHI QVIAGTQPGW CRQLGYPAYT SDVYERYQTS SANDDWSAWK KLNSEGIPAG AIVSFPKAVR NPAGYLKADG TIFAQNTFST FTAPWATQTN CPT // ID A0A0H4IVI7_NEIG1 Unreviewed; 159 AA. AC A0A0H4IVI7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Autotransporter {ECO:0000313|EMBL:AKO63760.1}; GN ORFNames=NGO_08955 {ECO:0000313|EMBL:AKO63760.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63760.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63760.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63760; AKO63760; NGO_08955. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 159 AA; 18279 MW; 134C05EC51F10F5D CRC64; MSFDCFGAFS YQPGSDTRPT NVGDTADFSF SDKPANGVFH YFSSGKTDQK SSEALYDEIN ITGKNYNSGI LAVDNMPVVK KYITDNYRTD LKQAVKKQLQ DLYKTRPEAW EENKKRVREE IIKQFGISED VFNKLQQKMP QKINSLIEEQ VLTPYILRP // ID A0A0H4IW16_NEIG1 Unreviewed; 126 AA. AC A0A0H4IW16; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Crossover junction endodeoxyribonuclease RusA {ECO:0000313|EMBL:AKO63623.1}; GN ORFNames=NGO_02610 {ECO:0000313|EMBL:AKO63623.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63623.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63623.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63623; AKO63623; NGO_02610. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1330.70; -; 1. DR InterPro; IPR008822; Endonuclease_RusA-like. DR Pfam; PF05866; RusA; 1. DR SUPFAM; SSF103084; SSF103084; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 126 AA; 13769 MW; 5D8ED12677D75389 CRC64; MRVIRLILPY PVSANRYWRI WRNRAVRSAE AAAYKETVRR IAQGAGAMPS EGFVAVRLRL IPKANKDGGA NKTVIDLDNA LKVALDALQG VAYHNDRQVR RIAAEYGGEP VAGGGLAVEV GELDEK // ID A0A0H4J5X4_NEIG1 Unreviewed; 185 AA. AC A0A0H4J5X4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Transporter {ECO:0000313|EMBL:AKO63767.1}; GN ORFNames=NGO_09360 {ECO:0000313|EMBL:AKO63767.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63767.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63767.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63767; AKO63767; NGO_09360. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 76 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 126 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 11 185 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 185 AA; 19182 MW; FFB21348D744DFFC CRC64; MTHTASKTPK LWAVIAAAAF ILLITIGMRM TLGLFVQPVV NTTELNIAQF SLIITVFQLM WGVLQPLSGA LADRFGAFRV LSGGALLLVC ACLIASNIPT YWGLMIAVGL LLAFGTGSGG FSIIMGQVAA QVPTHKRGLA SGLVNAGGSA GQFLFAPLVQ GLKDSSSCPK SAGRVHFTFG AQSPC // ID A0A0H4ITC4_NEIG1 Unreviewed; 67 AA. AC A0A0H4ITC4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63824.1}; GN ORFNames=NGO_11680 {ECO:0000313|EMBL:AKO63824.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63824.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63824.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63824; AKO63824; NGO_11680. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7606 MW; 80C26CE6BC059933 CRC64; MPSEAAWAFR RHFLHLKQRI GNPAPPVHGN PHLKTICMPN HTPIPVSVIC TLPVLGNHRF FAYNSRI // ID Q5F546_NEIG1 Unreviewed; 324 AA. AC Q5F546; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Iron ABC transporter permease {ECO:0000313|EMBL:AAW90691.1}; GN ORFNames=NGO_2090 {ECO:0000313|EMBL:AAW90691.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90691.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90691.1; -; Genomic_DNA. DR RefSeq; WP_010951403.1; NC_002946.2. DR RefSeq; YP_209103.1; NC_002946.2. DR ProteinModelPortal; Q5F546; -. DR EnsemblBacteria; AAW90691; AAW90691; NGO_2090. DR GeneID; 3282827; -. DR KEGG; ngo:NGO2090; -. DR PATRIC; 20338013; VBINeiGon24812_2529. DR HOGENOM; HOG000099129; -. DR KO; K02015; -. DR OMA; FMTLNVK; -. DR OrthoDB; EOG6WMJ1X; -. DR BioCyc; NGON242231:GI2G-1985-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00417415, KW ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 19 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 138 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 204 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; 35258 MW; 59A98DA5A5D1532E CRC64; MPSEKNIGFM AGSSRPLRVA FALLLVSCIL FMTLNVKGDW DFVLHLRLTK LAALLMVAYA VGVSTQLFQT LTNNPILTPS ILGFDSLYVF LQTLLVFTFG GVGYTSLPLT GKFGFELVVM MGGSLLLFYT LIRQGGRDLP HMILIGVIFG ILFRSLSSLL SRMIDPEEFT AAQANMFAGF NTVRSELLGI GALVLLVSAA VVWHERYRSD VHLLGRDQAV NLGISYTRNT LWILLWIAAL VATATAVVGP VSFFGLLAAS LANHFSPSVR HSVRLPMTVC VGGILLVGGQ TVFEHFLGMK AVLSVVVEFA GGLVFLYLVL KHKK // ID A0A0H4IS51_NEIG1 Unreviewed; 83 AA. AC A0A0H4IS51; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63736.1}; GN ORFNames=NGO_08040 {ECO:0000313|EMBL:AKO63736.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63736.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63736.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63736; AKO63736; NGO_08040. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 83 AA; 8929 MW; C5BC10742FD1751E CRC64; MGVGRSVFQT ASLGKAYAVF PSVIPTQAGI HICSHAGSDK NQETEYRLRI PACVGMTAVR LFGFMVILNQ MPSETADSNV RPT // ID Q5F8F1_NEIG1 Unreviewed; 253 AA. AC Q5F8F1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 60. DE SubName: Full=Ankyrin {ECO:0000313|EMBL:AAW89536.2}; GN ORFNames=NGO_0826 {ECO:0000313|EMBL:AAW89536.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89536.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89536.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8F1; -. DR EnsemblBacteria; AAW89536; AAW89536; NGO_0826. DR PATRIC; 20334810; VBINeiGon24812_0975. DR HOGENOM; HOG000220744; -. DR OMA; EHMWIND; -. DR OrthoDB; EOG6GXTRB; -. DR BioCyc; NGON242231:GI2G-778-MONOMER; -. DR Proteomes; UP000000535; 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; PF13606; Ank_3; 1. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 196 253 ANK_REP_REGION. FT {ECO:0000259|PROSITE:PS50297}. SQ SEQUENCE 253 AA; 29068 MW; 66D39BEDE8E41740 CRC64; MMGDSVIYYV EQADEPVNRA GERARKTFKY FWRELFWERR RIISALDFAM VKVPFFQDGE DGEICEHMWI DDIYFDGLYI YGVLNNEPGG LTNVEQGESV CVPVGDISDW MFVCNGIPYG GFTVQAMRGQ MTEEERTEHD TAWGIDFGDP GQVLPVYEEK EHPENLEEHP MCRNCIDDFR QQLSQNPDFL HEQDEDGYTP LHHEAMAGNA LMVQAMLEYG ANPASKTSEG YTALDFARLT GWQNVADLLE PRH // ID Q5F9H2_NEIG1 Unreviewed; 129 AA. AC Q5F9H2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 50. DE SubName: Full=MORN repeat family protein {ECO:0000313|EMBL:AAW89165.1}; GN ORFNames=NGO_0422 {ECO:0000313|EMBL:AAW89165.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89165.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89165.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F9H2; -. DR EnsemblBacteria; AAW89165; AAW89165; NGO_0422. DR PATRIC; 20333857; VBINeiGon24812_0506. DR HOGENOM; HOG000218875; -. DR OMA; YEMRTRH; -. DR OrthoDB; EOG6CVVDC; -. DR BioCyc; NGON242231:GI2G-400-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003409; MORN. DR Pfam; PF02493; MORN; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 129 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256632. SQ SEQUENCE 129 AA; 14204 MW; CCAF856563FC6B5C CRC64; MLKHLAFLLP AMMFALPAQT AVLSPYQETG CTYEGGIGKD GLPSGKGIWR CRDGRGYTGS FKNGKFDGQG VYTVAAGREV FLEPFNSDST KFRNMALSGT FKQGLAHGRF AASQNGETLF YYEMRTRHD // ID A0A0H4ISZ3_NEIG1 Unreviewed; 76 AA. AC A0A0H4ISZ3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63714.1}; GN ORFNames=NGO_07315 {ECO:0000313|EMBL:AKO63714.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63714.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63714.1; -; Genomic_DNA. DR RefSeq; WP_002259831.1; NC_002946.2. DR RefSeq; YP_009115484.1; NC_002946.2. DR EnsemblBacteria; AKO63714; AKO63714; NGO_07315. DR GeneID; 22847892; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 76 AA; 8857 MW; 9DADCB7A6A3A60FE CRC64; METLDERIKN LGKSLEDRID ANLIDATLEY ITFSERLLAF ETLCDYIEDF NIQLTEKESQ EISFINKEFG IESTSD // ID A0A0H4IT81_NEIG1 Unreviewed; 235 AA. AC A0A0H4IT81; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63779.1}; GN ORFNames=NGO_09965 {ECO:0000313|EMBL:AKO63779.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63779.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63779.1; -; Genomic_DNA. DR RefSeq; WP_030003518.1; NC_002946.2. DR RefSeq; YP_008914859.1; NC_002946.2. DR EnsemblBacteria; AKO63779; AKO63779; NGO_09965. DR GeneID; 19592990; -. DR KEGG; ngo:NGO1861a; -. DR Proteomes; UP000000535; 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; -; 3. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 50 235 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 235 AA; 26707 MW; 64FBF3067CD1BEC0 CRC64; MQADLAYAYE HITRDYPDAA GANQGKKIST VSDYFKNIRT RSVHPRLAFG YDFGGWRIAA DYARYRKWHN NKYSVNIKEL GRNDNSASDS KHLNIKTQKT EHQENGTFHA VSSLGLSTVY DFRANDKFKP YIGVRVAYGH VRHQVHSMEK ETTTVTTYPS DGSAKTSVPS EMPPKPAYHE NRSSRRLGFG AMAGVGIDVA PGLTLDAGYR YHYWGRLENT RFKTHEASLG VRYRF // ID A0A0H4IV03_NEIG1 Unreviewed; 74 AA. AC A0A0H4IV03; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63615.1}; GN ORFNames=NGO_01650 {ECO:0000313|EMBL:AKO63615.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63615.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63615.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63615; AKO63615; NGO_01650. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 73 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 74 AA; 8525 MW; BC89A24DA338B91E CRC64; MSVWDIWDRM VEIYHKYKKP CLVLAVDFVM GMVFIEPNEE PCIGRCYAPM PESPDFANAV AMAVAMICIV FIYD // ID A0A0H4IWD4_NEIG1 Unreviewed; 237 AA. AC A0A0H4IWD4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63728.1}; GN ORFNames=NGO_07725 {ECO:0000313|EMBL:AKO63728.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63728.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63728.1; -; Genomic_DNA. DR RefSeq; WP_030003516.1; NC_002946.2. DR RefSeq; YP_008914855.1; NC_002946.2. DR EnsemblBacteria; AKO63728; AKO63728; NGO_07725. DR GeneID; 19593004; -. DR KEGG; ngo:NGO1463a; -. DR Proteomes; UP000000535; 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; -; 3. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 237 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 237 AA; 27198 MW; 708F4C892B75B956 CRC64; MQADLAYAYE HITRDYPDAA GANKGKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWHNN KYSVNIKELE RKNNKTFGGN QLNIKYQKTE HQENGTFHAV SSLGLSTVYD FRVNDKFKPY IGVRVGYGHV RHGIDSTKKT KNTLTAYHSA GTKPTYYDDI DSGKNQKNTY RQNRSSRRLG FGAMAGVGID VAPGLTLDAG YRYHYWGRLE NTRFKTHEAS LGVRYRF // ID A0A0H4IWE0_NEIG1 Unreviewed; 106 AA. AC A0A0H4IWE0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Membrane fusogenic activity family protein {ECO:0000313|EMBL:AKO63738.1}; GN ORFNames=NGO_08205 {ECO:0000313|EMBL:AKO63738.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63738.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63738.1; -; Genomic_DNA. DR RefSeq; WP_030003521.1; NC_002946.2. DR RefSeq; YP_208599.2; NC_002946.2. DR EnsemblBacteria; AKO63738; AKO63738; NGO_08205. DR GeneID; 3281321; -. DR KEGG; ngo:NGO1551; -. DR KO; K09806; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 81 104 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 106 AA; 11587 MW; 119680C0E04D539F CRC64; MFGKQLFEEV GSKISETIAN SPAKDVEKNI KAMLGGAFNR MDLVTREEFD IQQQVLIKTR TKLAALEARL AKLEAAQNPQ RAALEAAEAA AEEAVAEIRQ QTEAGE // ID Q5FAK7_NEIG1 Unreviewed; 436 AA. AC Q5FAK7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01105}; DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01105}; DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01105}; GN Name=argA {ECO:0000256|HAMAP-Rule:MF_01105}; GN ORFNames=NGO_0027 {ECO:0000313|EMBL:AAW88796.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88796.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:2R8V, ECO:0000213|PDB:2R98, ECO:0000213|PDB:3B8G} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH COENZYME A. RX PubMed=18184660; DOI=10.1074/jbc.M707678200; RA Shi D., Sagar V., Jin Z., Yu X., Caldovic L., Morizono H., RA Allewell N.M., Tuchman M.; RT "The crystal structure of N-acetyl-L-glutamate synthase from Neisseria RT gonorrhoeae provides insights into mechanisms of catalysis and RT regulation."; RL J. Biol. Chem. 283:7176-7184(2008). RN [3] {ECO:0000213|PDB:3D2M, ECO:0000213|PDB:3D2P} RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH COENZYME A. RX PubMed=19095660; DOI=10.1074/jbc.M805348200; RA Min L., Jin Z., Caldovic L., Morizono H., Allewell N.M., Tuchman M., RA Shi D.; RT "Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase RT by L-arginine."; RL J. Biol. Chem. 284:4873-4880(2009). CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. {ECO:0000256|HAMAP-Rule:MF_01105, CC ECO:0000256|SAAS:SAAS00064071}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 1/4. {ECO:0000256|HAMAP- CC Rule:MF_01105, ECO:0000256|SAAS:SAAS00064059}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}. CC -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme CC ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), CC ArgA fulfills an anaplerotic role. {ECO:0000256|HAMAP- CC Rule:MF_01105}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01105, CC ECO:0000256|SAAS:SAAS00561278}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000256|HAMAP-Rule:MF_01105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88796.1; -; Genomic_DNA. DR RefSeq; WP_010950974.1; NC_002946.2. DR RefSeq; YP_207208.1; NC_002946.2. DR PDB; 2R8V; X-ray; 2.50 A; A=1-436. DR PDB; 2R98; X-ray; 2.40 A; A=1-436. DR PDB; 3B8G; X-ray; 2.60 A; A=1-436. DR PDB; 3D2M; X-ray; 2.21 A; A=1-436. DR PDB; 3D2P; X-ray; 2.56 A; A/B=1-436. DR PDBsum; 2R8V; -. DR PDBsum; 2R98; -. DR PDBsum; 3B8G; -. DR PDBsum; 3D2M; -. DR PDBsum; 3D2P; -. DR ProteinModelPortal; Q5FAK7; -. DR SMR; Q5FAK7; 5-436. DR EnsemblBacteria; AAW88796; AAW88796; NGO_0027. DR GeneID; 3283070; -. DR KEGG; ngo:NGO0027; -. DR PATRIC; 20332884; VBINeiGon24812_0027. DR HOGENOM; HOG000262225; -. DR KO; K14682; -. DR OMA; KQALYNY; -. DR OrthoDB; EOG6T1WVF; -. DR BioCyc; NGON242231:GI2G-24-MONOMER; -. DR BRENDA; 2.3.1.1; 3590. DR UniPathway; UPA00068; UER00106. DR EvolutionaryTrace; Q5FAK7; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2R8V, ECO:0000213|PDB:2R98, KW ECO:0000213|PDB:3B8G, ECO:0000213|PDB:3D2M}; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01105, KW ECO:0000256|SAAS:SAAS00448251}; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105, KW ECO:0000256|SAAS:SAAS00448257}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01105, KW ECO:0000256|SAAS:SAAS00448257}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01105}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01105, KW ECO:0000256|SAAS:SAAS00448251}. FT DOMAIN 287 436 N-acetyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01105, FT ECO:0000259|PROSITE:PS51186}. FT REGION 151 152 Coenzyme A 1 binding. FT {ECO:0000213|PDB:3D2M}. FT REGION 357 359 Coenzyme A 1 binding. FT {ECO:0000213|PDB:3D2M}. FT REGION 357 359 Coenzyme A 2 binding. FT {ECO:0000213|PDB:3B8G}. FT REGION 364 370 Coenzyme A 1 binding. FT {ECO:0000213|PDB:3D2M}. FT REGION 364 370 Coenzyme A 3 binding. FT {ECO:0000213|PDB:3D2P}. FT REGION 365 370 Coenzyme A 2 binding. FT {ECO:0000213|PDB:3B8G}. FT REGION 392 398 Coenzyme A 1 binding. FT {ECO:0000213|PDB:3D2M}. FT REGION 394 398 Coenzyme A 2 binding. FT {ECO:0000213|PDB:3B8G}. FT BINDING 134 134 Coenzyme A 1. {ECO:0000213|PDB:3D2M}. FT BINDING 152 152 Coenzyme A 2. {ECO:0000213|PDB:3B8G}. FT BINDING 357 357 Coenzyme A 3; via carbonyl oxygen. FT {ECO:0000213|PDB:3D2P}. FT BINDING 394 394 Coenzyme A 3; via carbonyl oxygen. FT {ECO:0000213|PDB:3D2P}. FT BINDING 398 398 Coenzyme A 3. {ECO:0000213|PDB:3D2P}. SQ SEQUENCE 436 AA; 47003 MW; 6019B9B2B4FC8A0C CRC64; MNAPDSFVAH FREAAPYIRQ MRGTTLVAGI DGRLLEGGTL NKLAADIGLL SQLGIRLVLI HGAYHFLDRL AAAQGRTPHY CRGLRVTDET SLGQAQQFAG TVRSRFEAAL CGSVSGFARA PSVPLVSGNF LTARPIGVID GTDMEYAGVI RKTDTAALRF QLDAGNIVWM PPLGHSYGGK TFNLDMVQAA ASVAVSLQAE KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAASETRR LISSAVAALE GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI AALIRPLEEQ GVLLHRSREY LENHISEFSI LEHDGDLYGC AALKTFAEAD CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA ERGFQTASED ELPETRRKDY RSNGRNPHIL VRRLHR // ID A0A0H4IW62_NEIG1 Unreviewed; 72 AA. AC A0A0H4IW62; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:AKO63668.1}; GN ORFNames=NGO_04890 {ECO:0000313|EMBL:AKO63668.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63668.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63668.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63668; AKO63668; NGO_04890. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 59 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 72 AA; 8615 MW; 29752105F7C1389E CRC64; MIGRLFRIFF FFALAALIIN RLFSRRQKRV LREVAEISAW VLLGAAAATL FWYLFMLYFK HIPDSYRRKN AV // ID A0A0H4IW79_NEIG1 Unreviewed; 196 AA. AC A0A0H4IW79; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63688.1}; GN ORFNames=NGO_05770 {ECO:0000313|EMBL:AKO63688.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63688.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63688.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63688; AKO63688; NGO_05770. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1330.70; -; 1. DR InterPro; IPR008822; Endonuclease_RusA-like. DR Pfam; PF05866; RusA; 1. DR SUPFAM; SSF103084; SSF103084; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 196 AA; 21326 MW; 4BFCA0D0DA13BD17 CRC64; MQNLPQQGSP AKARGGGSRR DDGGKAARIH PRRARRLPDI GRRPVDATGR GMRVTRLILP YPVSANRYWR IWRNRAVRSA EAAAYKETVR RIAQGAGAMP SEGAVAVYVR LIPKANKDGG ANKTVIDLDN ALKVTLDALQ GVAYHNDRQV RRIAAEYGGE PVTGGGLAVE VGELEMEQTD AADEGWDFIG QEGWDV // ID Q5F837_NEIG1 Unreviewed; 284 AA. AC Q5F837; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE RecName: Full=Segregation and condensation protein A {ECO:0000256|SAAS:SAAS00093938}; GN ORFNames=NGO_0961 {ECO:0000313|EMBL:AAW89650.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89650.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89650.1; -; Genomic_DNA. DR RefSeq; WP_003696990.1; NC_002946.2. DR RefSeq; YP_208062.1; NC_002946.2. DR EnsemblBacteria; AAW89650; AAW89650; NGO_0961. DR GeneID; 3282601; -. DR KEGG; ngo:NGO0961; -. DR PATRIC; 20335112; VBINeiGon24812_1125. DR HOGENOM; HOG000242825; -. DR KO; K05896; -. DR OMA; RKQNFNI; -. DR OrthoDB; EOG6CZQPX; -. DR BioCyc; NGON242231:GI2G-892-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00464526}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 284 AA; 31735 MW; B7AB81C67CB58C6A CRC64; MPPIPALSAP SEHTVAWVFG QPVTDLPQDL FIPPDALKVV LGSFQGPLDL LLYLIRKQNI DVLDIPMVEI TGQYLHYIAQ MEAYQFDLAA EYLLMAAMLI EIKSRLLLPR TEAVEDEEAD PRAELVRRLL AYEQMKLAAQ GLDALPRAGR DFAWAYLPLE IAAETKLPEV YIADLMQAWL GILSRAKHTR SHEVIQETLS VRAQMTAILR RLNEHGICRF HALFNPEQGA AYVIVNFIAL LELAKEGLVG IVQEDGFGEI RISLNHEGAH SDGIFGTRGG RDVF // ID Q5FAD9_NEIG1 Unreviewed; 354 AA. AC Q5FAD9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=Glycosyl transferase family 1 {ECO:0000313|EMBL:AAW88848.1}; GN ORFNames=NGO_0087 {ECO:0000313|EMBL:AAW88848.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88848.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88848.1; -; Genomic_DNA. DR RefSeq; WP_003704929.1; NC_002946.2. DR RefSeq; YP_207260.1; NC_002946.2. DR ProteinModelPortal; Q5FAD9; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW88848; AAW88848; NGO_0087. DR GeneID; 3282283; -. DR KEGG; ngo:NGO0087; -. DR PATRIC; 20333061; VBINeiGon24812_0114. DR HOGENOM; HOG000137696; -. DR OMA; MDNLKAQ; -. DR OrthoDB; EOG6D2KR6; -. DR BioCyc; NGON242231:GI2G-77-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88848.1}. FT DOMAIN 173 330 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 354 AA; 38955 MW; 55464788049F77F6 CRC64; MKIILTTSMS GLGGTETATV RLGRLLKRHG HDIILASSDG PFVGEAQASG IRWQPVDFYR GGLAGYLKST FAYARMLRRE QPDIIDCQMA RVVPACALAA KIVSPKTKII CHSHGLDAAT YPKTAKLFDK LGAYIIGNCK HEREKLIRHG FPAGRIAYAY NTPPEFHFRK TEKECAVLGT LSRLDTVRAV HLMLDILKKM VGRNIPVRLN MAGIGEEMDN LKAQAKRLGI EDKVTFLGGV RDLTGYFKEV DILVNTPHCV GDHGAGVGNN ILEAGLYDTP VVTYNMAGIS EMVITGQTGY CIPFGDDEAF IEAVDTLIKH PELRSQMGKA LHKHVETLCS DDEIYRTTMA AYEM // ID Q5F7D2_NEIG1 Unreviewed; 350 AA. AC Q5F7D2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW89905.1}; GN ORFNames=NGO_1246 {ECO:0000313|EMBL:AAW89905.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89905.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89905.1; -; Genomic_DNA. DR RefSeq; WP_010951223.1; NC_002946.2. DR RefSeq; YP_208317.1; NC_002946.2. DR ProteinModelPortal; Q5F7D2; -. DR DNASU; 3282608; -. DR EnsemblBacteria; AAW89905; AAW89905; NGO_1246. DR GeneID; 3282608; -. DR KEGG; ngo:NGO1246; -. DR PATRIC; 20335811; VBINeiGon24812_1465. DR HOGENOM; HOG000281079; -. DR KO; K04774; -. DR OMA; WYGEDAL; -. DR OrthoDB; EOG6P5ZHQ; -. DR BioCyc; NGON242231:GI2G-1158-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 160 Peptidase_S49_N. FT {ECO:0000259|Pfam:PF08496}. FT DOMAIN 163 312 Peptidase_S49. FT {ECO:0000259|Pfam:PF01343}. FT COILED 63 93 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 350 AA; 39474 MW; D404F0E9A4092453 CRC64; MWKEILLNYG IFLLELLTVF GAIALIVLAI VQSKKQSESG SVVLTDFSEN YKKQRQSFET FFLSEEETKH QEKKEKKKEK AEAKAEKKRL KEGGEKSAET QKSRLFVLDF DGDLYAHAVE SLRHEITAVL LIAKPEDEVL LRLESPGGVV HGYGLAASQL RRLRERNIPL TVAVDKVAAS GGYMMACVAD KIVSAPFAVI GSVGVVAEVP NIHRLLKKHD IDVDVMTAGE FKRTVTFMGE NTEKGKQKFR QELEETHQLF KQFVSENRPG LDIEKIATGE HWFGRQALAL NLIDEISTSD DLLLKAFENK QVIEVKYQEK RSLIQRIGLQ AEASVEKLFA KLVNRRADVM // ID Q5F9G1_NEIG1 Unreviewed; 213 AA. AC Q5F9G1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 55. DE SubName: Full=Alpha/beta hydrolase {ECO:0000313|EMBL:AAW89176.1}; GN ORFNames=NGO_0434 {ECO:0000313|EMBL:AAW89176.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89176.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89176.1; -; Genomic_DNA. DR RefSeq; WP_003706615.1; NC_002946.2. DR RefSeq; YP_207588.1; NC_002946.2. DR ProteinModelPortal; Q5F9G1; -. DR ESTHER; neig1-q5f9g1; Atu1826-like. DR EnsemblBacteria; AAW89176; AAW89176; NGO_0434. DR GeneID; 3282098; -. DR KEGG; ngo:NGO0434; -. DR PATRIC; 20333883; VBINeiGon24812_0519. DR HOGENOM; HOG000265112; -. DR KO; K07018; -. DR OMA; KVAECGH; -. DR OrthoDB; EOG6XDH0P; -. DR BioCyc; NGON242231:GI2G-411-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89176.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 213 AA; 22755 MW; CC19C60BDB7D4451 CRC64; MLKPETIHIP GPAGILETIH IPSEQVPARG VAVINHPNPL QGGTNTNKVI QTAAKALSKL GFHCYLPNLR GVGGSEGTHD YGRGETQDCL AVIDYARAQH PEAPEFALSG FSFGGYVATF AAQVSIPDLL LLIGAAVCHY TDRPEPSAVP NVAKTLMIHG AEDEVVEIEK ALKWAEPQDL PVITIAGSTH FFHGKLIVLR DTILRFAPVC LNG // ID Q5F6V2_NEIG1 Unreviewed; 1161 AA. AC Q5F6V2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894}; GN ORFNames=NGO_1443 {ECO:0000313|EMBL:AAW90085.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90085.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90085.1; -; Genomic_DNA. DR RefSeq; WP_003705759.1; NC_002946.2. DR RefSeq; YP_208497.1; NC_002946.2. DR ProteinModelPortal; Q5F6V2; -. DR EnsemblBacteria; AAW90085; AAW90085; NGO_1443. DR GeneID; 3281743; -. DR KEGG; ngo:NGO1443; -. DR PATRIC; 20336305; VBINeiGon24812_1701. DR HOGENOM; HOG000036391; -. DR KO; K03529; -. DR OMA; AFQTASN; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NGON242231:GI2G-1350-MONOMER; -. DR Proteomes; UP000000535; 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; 1. DR PIRSF; PIRSF005719; SMC; 1. DR SUPFAM; SSF52540; SSF52540; 4. 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:UP000000535}; 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:UP000000535}. FT DOMAIN 3 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 692 879 {ECO:0000256|HAMAP-Rule:MF_01894}. SQ SEQUENCE 1161 AA; 130360 MW; 2AFC9643B35CC0B0 CRC64; MRLTHIKLSG FKSFTDPTTI HVPGQLVAVI GPNGCGKSNV IDAVRWVLGE ASAKQLRGES MQDVIFNGAA TRRPAPRASV ELVFDNSDHS LQGAWGQYAE VSIKRQLTRQ GESTYFINNQ TVRRRDITDL FLGTGVGARG YAVIEQGMIS RIIEARPEEL RAYIEEAAGV SKYKERRKET EGRLKDTREH LQRLGDLQNE LARQVEKLEK QAETAERYKS LTAQLNQQQD LLDYAQWQQS LAAADKATAQ HQSLQAQQDE TAAQVQALNN EVHALQTAEQ SQQQAVHELS NKRGVLREQI ARLEEQIRHR QNLHQRIERD KQAAQAQLQR IRQEQQQIRV QLEENELQVE EKQTELAEWA MQVAEHEERL PELEEVQATL NAAFQTQQDE ANRIRRELAL KQQQLAHAEQ TVAKHEERKG RLKQENQALN LPDEAETAAA QEAAALLQSR QEHYEEQIIA AEEALHAARE AFQTASNRFQ SLKQQHITLQ AQQQALSQIL SQQQEAADFW QATDHAAAPQ LWQHITAPAE WQHALSVILA ERLHARSVPN SFVPPAPLPQ GQAAWLSDGL SGGIKKSLPV QALLNQIQAQ PPFQTALHHW LDGVLCAPDL SYALAHQNDL GTHQIWLTPE GHQVDKVSVL LYAKPAQESL IAQKARLDGI AAELENLAPG LSAAEAAFKQ TEAAVCSSEV QHKNLMQQQQ QHTRQYSQAQ QRTAELLART NQGQIRREHI ERELAQLAEE QTVLQHTSDG LSDDIATLQE AAAELEHQQQ TTAHSRQEQQ GRLKQAQLAL LEANRQYGLA EVAVHKLNQQ KQNYRQQIAR LEQQTLDWQE RRQELALAYE TEFQNDEQHI KLDELTETVH TLDEEYIAVQ EKLAQIQEQG REQYARVQTL QTKLPQLQAA TQTALLQQQE ALINAKRYHQ NLTERAADLD VLEALAKESA KVLNSSIGSL TRQIEALGAV NLAALQELEE ARERDGYYRS QSEDVQAAIA LLEEAIAQID DKTKARFKET FDAVNGKVQT FFPTLFGGGE ATLKMIGDDL LTAGVSIMAR PPGKKNSTIH LLSGGEKALT AMSLVFALFS LNPAPFCLLD EVDAPLDDAN TSRFCKLVKE MSVQTQFLYI SHNRLTMEMA EQLVGVTMQE KGVSRVVAVD IKQALEMAEA V // ID Q5F5Q6_NEIG1 Unreviewed; 189 AA. AC Q5F5Q6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:AAW90481.1}; GN ORFNames=NGO_1860 {ECO:0000313|EMBL:AAW90481.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90481.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90481.1; -; Genomic_DNA. DR RefSeq; WP_003690114.1; NC_002946.2. DR RefSeq; YP_208893.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q6; -. DR EnsemblBacteria; AAW90481; AAW90481; NGO_1860. DR GeneID; 3282354; -. DR KEGG; ngo:NGO1860; -. DR PATRIC; 20337408; VBINeiGon24812_2235. DR HOGENOM; HOG000050676; -. DR OMA; DEEIACE; -. DR OrthoDB; EOG64XXSX; -. DR BioCyc; NGON242231:GI2G-1765-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 189 AA; 20865 MW; 365C2B2E9508FED3 CRC64; MAAGKHTKHS NRVRIIGGQC RGRKLSFASA DGLRPTPDSV REKLFNWLGQ DLTGKTVLDL FGGSGALGME AASRNAKRVV IADNNRQTVQ TLEKNSRELG LGQVQTVCSD GIAYLANLKE KFDVVFLDPP FAWQSWESLF NVLGTRLNDG AYVYIEAGRQ PDKPDWLTGY REGKSGQGTF ELRVFQVAE // ID A0A0H4ISR2_NEIG1 Unreviewed; 47 AA. AC A0A0H4ISR2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Restriction endonuclease subunit M {ECO:0000313|EMBL:AKO63654.1}; GN ORFNames=NGO_03935 {ECO:0000313|EMBL:AKO63654.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63654.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63654.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63654; AKO63654; NGO_03935. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AKO63654.1}; KW Hydrolase {ECO:0000313|EMBL:AKO63654.1}; KW Nuclease {ECO:0000313|EMBL:AKO63654.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 47 AA; 5490 MW; B705D47A4A3B19AF CRC64; MKPAPFYVQY FALAEQNSND PLYQMQKICR HSREGGNPDL SARKFIE // ID A0A0H4IRZ2_NEIG1 Unreviewed; 179 AA. AC A0A0H4IRZ2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Fumarate hydratase {ECO:0000313|EMBL:AKO63691.1}; GN ORFNames=NGO_06025 {ECO:0000313|EMBL:AKO63691.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63691.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63691.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63691; AKO63691; NGO_06025. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro. DR Gene3D; 3.20.130.10; -; 1. DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat. DR Pfam; PF05683; Fumerase_C; 1. DR SUPFAM; SSF117457; SSF117457; 1. DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 163 Fumerase_C. {ECO:0000259|Pfam:PF05683}. SQ SEQUENCE 179 AA; 19208 MW; A076DBA2C2CB9142 CRC64; MASWKTGDVL LLNGKILTGR DAAHKRLVNM LDKGEELPVD FTNRLIYYVG PVDPVGDEVV GPAGPTTATR MDKFTRQMLK QTGLLGMIGK SERGAATCEA IADNKAVYLM AVGGAAYLVA KAIKSSKVLA FPELGMEAVY EFEVKDMPVT VAVDSKGESI HATAPRKWQA KIGIIPVES // ID A0A0H4J5B7_NEIG1 Unreviewed; 45 AA. AC A0A0H4J5B7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AKO63592.1}; GN ORFNames=NGO_00500 {ECO:0000313|EMBL:AKO63592.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63592.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63592.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63592; AKO63592; NGO_00500. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 5262 MW; 64077275458F36DD CRC64; MFRVAVFCGN DEALDCEDLS LPPSFPQKWE SRNEKQQEFI GNDRN // ID Q5F725_NEIG1 Unreviewed; 1067 AA. AC Q5F725; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Acriflavine resistance protein B {ECO:0000313|EMBL:AAW90012.1}; GN ORFNames=NGO_1364 {ECO:0000313|EMBL:AAW90012.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90012.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90012.1; -; Genomic_DNA. DR RefSeq; WP_010951248.1; NC_002946.2. DR RefSeq; YP_208424.1; NC_002946.2. DR ProteinModelPortal; Q5F725; -. DR EnsemblBacteria; AAW90012; AAW90012; NGO_1364. DR GeneID; 3282529; -. DR KEGG; ngo:NGO1364; -. DR PATRIC; 20336113; VBINeiGon24812_1605. DR HOGENOM; HOG000158129; -. DR KO; K18138; -. DR OMA; FFGWFNA; -. DR OrthoDB; EOG683S5M; -. DR BioCyc; NGON242231:GI2G-1277-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 113997 MW; EB9E6283604BE031 CRC64; MAKFFIDRPI FAWVISIFII AAGIFGIKSL PVSQYPSVAA PTITLHAIYP GASAQVMEGS VLSVIERNMN GVEGLDYMST SADSSGSGSV SLTFTPDTDE NLAQVEVQNK LSEVLSTLPA TVQQYGVTVS KARSNFLMIV MLSSDVQSTE EMNDYAQRNV VPELQRIEGV GQVRLFGAQR AMRIWVDPKK LQNYNLSFAD VGSALSAQNI QISAGSIGSL PAVRGQTVTA TVTAQGQLGT AEEFGNVILR ANTDGSNIYL KDVAKVGLGM EDYSSSTRLN GVNTTGMAVM LSNSGNAMAT AKAVKERLAV LEKYFPQGMS WKTPYDTSKF VEISIEKVIH TLIEAMVLVF VVMYLFLQNI RYTLIPTIVV PISLLGGFAF ISYMGMSINV LTMFAMILVI GIVVDDAIVV VENVERIMAG EGLPPKEATK KAMGQISGAV IGITAVLISV FVPLAMFSGA AGNIYKQFAL TMASSIAFSA FLALTLTPAL CATMLKTIPK GHHEEKKGFF GWFNKKFDSW THGYEGRVAK VLRKTFRMMV VYIGLAVVGV FLFMRLPTSF LPTEDQGFVM VSVQLPAGAT KERTDATLAQ VTQLAKSIPE IENIITVSGF SFSGSGQNMA MGFAILKDWN ERTASGSDAV AVAGKLTGMM MGTLKDGFGI SVVPPPILEL GNGSGLSINL QDRNNTGHTA LLAKRNELIQ KMRASGLFDP STVRAGGLED SPQLKIDINR AAAAAQGISF ADIRTALASA LSSSYVSDFP NQGRLQRVMV QADEDARMQP ADILNLTVPN KSGVAVPLST IATVSWENGT EQSVRFNGYP SMKLSASPAT GVSTGQAMAA VQKMVDELGG GYSFEWGGQS REEAKGGSQT LILYGLAVAA VFLVLAALYE SWSIPLAVIL VIPLGLIGAA AGVTGRNLFE GLLGSVPSFA NDIYFQVGFV TVMGLSAKNA ILIIEFAKDL QAQGKSAVEA ALEAARLRFR PIIMTSFAFI LGVVPLYIAA GASSASQRAI GTTVFWGMLV GTLLSVFLVP LFYVVVRKFF KETAHEHEMA VRHASKAGIT GSDDKQY // ID Q5F6Z5_NEIG1 Unreviewed; 217 AA. AC Q5F6Z5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 47. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90042.1}; GN ORFNames=NGO_1394 {ECO:0000313|EMBL:AAW90042.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90042.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90042.1; -; Genomic_DNA. DR RefSeq; WP_010951256.1; NC_002946.2. DR RefSeq; YP_208454.1; NC_002946.2. DR EnsemblBacteria; AAW90042; AAW90042; NGO_1394. DR GeneID; 3281287; -. DR KEGG; ngo:NGO1394; -. DR PATRIC; 20336181; VBINeiGon24812_1639. DR HOGENOM; HOG000218644; -. DR OMA; WEYEDNT; -. DR BioCyc; NGON242231:GI2G-1307-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24105 MW; 8D5CF6B27A7B8B27 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFERPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAEDDA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRLN SGTPPRQLKI LRDRCGI // ID A0A0H4IUY3_NEIG1 Unreviewed; 145 AA. AC A0A0H4IUY3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63590.1}; GN ORFNames=NGO_00400 {ECO:0000313|EMBL:AKO63590.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63590.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63590.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63590; AKO63590; NGO_00400. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR Pfam; PF00593; TonB_dep_Rec; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 144 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 145 AA; 15777 MW; A8667B7A99D6DE76 CRC64; MGKRVMEGVE TEISGAITPK WQIHAGYSYL HSQIKTAANP RDDGIFLLVP KHSANLWTTY QVTPGLTVGG GVNAMSGITS SAGMHAGGYA TFDAMAAYRF TPKLKLQINA DNIFNRHYYA RVGGTNTFNI PGSERSLTAN LRYSF // ID Q5F6H7_NEIG1 Unreviewed; 524 AA. AC Q5F6H7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE RecName: Full=Phosphate transporter {ECO:0000256|RuleBase:RU363058}; GN ORFNames=NGO_1581 {ECO:0000313|EMBL:AAW90210.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90210.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90210.1; -; Genomic_DNA. DR RefSeq; WP_003693510.1; NC_002946.2. DR RefSeq; YP_208622.1; NC_002946.2. DR EnsemblBacteria; AAW90210; AAW90210; NGO_1581. DR GeneID; 3281088; -. DR KEGG; ngo:NGO1581; -. DR PATRIC; 20336690; VBINeiGon24812_1891. DR HOGENOM; HOG000231892; -. DR KO; K03306; -. DR OMA; WINLATW; -. DR OrthoDB; EOG6NWBS7; -. DR BioCyc; NGON242231:GI2G-1478-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363058}; KW Phosphate transport {ECO:0000256|RuleBase:RU363058}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 151 177 Helical. {ECO:0000256|RuleBase:RU363058}. FT TRANSMEM 183 202 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; 56503 MW; 0931F7BEFB8112E1 CRC64; MAQIQMSANV KTINAVFAAM LVGTVGYFIY WGLGYTHYNY AALFIIATMF GVFMAFNIGG NDVANSFGTS VGAGTLTIPQ ALLIAAVFEV SGAVIAGGEV TDTIRKGIVD LKGVDFEPIQ FVFIMMSALL AAALWLLFAS RKGLPVSTTH AIIGGIVGSA LCMAFTHNAD GVALIRWGKL GEIGMSWVLS PVLGGAVSYF LFSRVKKNVL DYNAWAEGTL KGIKQEKKAY KERHRLFFEG LSEAEKVEYA TKMAHDAQIY DEPEFDPQEL QSEYYRGLYA FDNRKNNVDS YKALHSWIPF IASFGTMMIS AMLIFKGLKN LHLGMSNVNS FLTIFMIGAA VWMGTFVFAK SLKRKDLGKS TFQMFSWMQV FTACGFAFSH GANDIANAIG PFAAIMDVLR TNSVAAQSAV PPIAMLTFGI ALIVGLWFVG KEVIKTVGTS LAEMHPASGF TAELSAASVV MGASLMGLPV SSTHILVGAV LGIGLVNRNA NWKLMKPIGL AWVITLPAAA VLSMASYLIL QAVF // ID Q5F575_NEIG1 Unreviewed; 242 AA. AC Q5F575; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Hydrolase {ECO:0000313|EMBL:AAW90662.1}; GN ORFNames=NGO_2055 {ECO:0000313|EMBL:AAW90662.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90662.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90662.1; -; Genomic_DNA. DR RefSeq; WP_003705095.1; NC_002946.2. DR RefSeq; YP_209074.1; NC_002946.2. DR ProteinModelPortal; Q5F575; -. DR DNASU; 3282741; -. DR EnsemblBacteria; AAW90662; AAW90662; NGO_2055. DR GeneID; 3282741; -. DR KEGG; ngo:NGO2055; -. DR PATRIC; 20337911; VBINeiGon24812_2478. DR HOGENOM; HOG000266042; -. DR KO; K07025; -. DR OMA; KSHALPF; -. DR OrthoDB; EOG6Z0Q8F; -. DR BioCyc; NGON242231:GI2G-1956-MONOMER; -. DR Proteomes; UP000000535; 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; TIGR01509; HAD-SF-IA-v3; 1. DR TIGRFAMs; TIGR01993; Pyr-5-nucltdase; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90662.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 9 187 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 242 AA; 27343 MW; A79533A6F06FDD49 CRC64; MQENPTVWLF DLDNTLHDAD AGIFHLINRA MTRYMARRLK LSESAASDLR QDYWHRYGAT LAGLQIHHPE IDIAEFLRES HPIDAILTRL HGMADTENTL CRLNGRKAVF SNGPSFYVRA VAGALGLENC FDALFGTDDF GLLYKPNPQA YLNVCRLLDV PPECCIMVDD SADNLHQAKA LGMKTVRFGA KSHAPPFIDA SVSDMAQLAR YAETLSERRQ NHYNTRTPRK YERMLCVKPS LS // ID A0A0H4IRQ0_NEIG1 Unreviewed; 332 AA. AC A0A0H4IRQ0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63631.1}; GN ORFNames=NGO_03050 {ECO:0000313|EMBL:AKO63631.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63631.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63631.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63631; AKO63631; NGO_03050. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.25.40.10; -; 1. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 332 AA; 36785 MW; D17CF519F34A5636 CRC64; MGKTSAKNNN PHGQYLLAQY CRHGTPPDFE TAHLLYRKAA AQGLPEAHWQ LGLQYRFGQG TKADTAQAVN HLRAAAQQGY IPAYTPLAEL ILPTAPDEAV YRFQQAAQEN DPDAHAALAD IYLQGKYLER NHKLALHHAE AAAAERHPEG LRIPGDICRY GLGIALDTEK ARHYYRQAAE AGSLTAYQKL ISDSALNHPE QYDGIKDSAI RRQQAEQLYQ KPKPCITDYN AHPNTQPRSN CTQKPQNSDT AKPKPIWAVC ITSDRAQPPT TTKPANGLNK PPRKKTVWRS TTSPASITAD TVSNRIKEKA CHCLQEAINN GYGQKNVLQE LL // ID Q5F7G7_NEIG1 Unreviewed; 217 AA. AC Q5F7G7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 48. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89870.1}; GN ORFNames=NGO_1211 {ECO:0000313|EMBL:AAW89870.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89870.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89870.1; -; Genomic_DNA. DR RefSeq; WP_010951217.1; NC_002946.2. DR RefSeq; YP_208282.1; NC_002946.2. DR DNASU; 3281917; -. DR EnsemblBacteria; AAW89870; AAW89870; NGO_1211. DR GeneID; 3281917; -. DR KEGG; ngo:NGO1211; -. DR PATRIC; 20335727; VBINeiGon24812_1422. DR HOGENOM; HOG000218644; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-1122-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24023 MW; 79DDCB2E88FD6BBD CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFEGPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADNA EPETLPPAVK KKIMPDGIVY ADSPGSRGKL DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F9I4_NEIG1 Unreviewed; 67 AA. AC Q5F9I4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 79. DE SubName: Full=Cold-shock protein {ECO:0000313|EMBL:AAW89153.1}; GN ORFNames=NGO_0410 {ECO:0000313|EMBL:AAW89153.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89153.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89153.1; -; Genomic_DNA. DR RefSeq; WP_002217533.1; NC_002946.2. DR RefSeq; YP_207565.1; NC_002946.2. DR ProteinModelPortal; Q5F9I4; -. DR SMR; Q5F9I4; 1-67. DR EnsemblBacteria; AAW89153; AAW89153; NGO_0410. DR GeneID; 25047475; -. DR GeneID; 3282233; -. DR KEGG; ngo:NGO0410; -. DR PATRIC; 20333831; VBINeiGon24812_0493. DR HOGENOM; HOG000070674; -. DR KO; K03704; -. DR OMA; NDKVEFT; -. DR OrthoDB; EOG618R0J; -. DR BioCyc; NGON242231:GI2G-388-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Activator {ECO:0000256|SAAS:SAAS00444396}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00444364}; KW DNA-binding {ECO:0000256|SAAS:SAAS00444440}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F6B8_NEIG1 Unreviewed; 320 AA. AC Q5F6B8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90269.1}; GN ORFNames=NGO_1641 {ECO:0000313|EMBL:AAW90269.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90269.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90269.1; -; Genomic_DNA. DR RefSeq; WP_010951315.1; NC_002946.2. DR RefSeq; YP_208681.1; NC_002946.2. DR EnsemblBacteria; AAW90269; AAW90269; NGO_1641. DR GeneID; 3281314; -. DR KEGG; ngo:NGO1641; -. DR PATRIC; 20336822; VBINeiGon24812_1956. DR HOGENOM; HOG000130878; -. DR OMA; RYNTECK; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NGON242231:GI2G-1538-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 152 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 320 AA; 36409 MW; 625023A19C7516BD CRC64; MRNTVGLDIS KLTFDATAMV GKTEHSAKFD NDSKGLDQFS DRLKSLGYQN LHICMEATGS YYEEVADYFA QYYSVYVVNP LKISKYAESR FKRTKTDKQD ARLIAQYCRS AKESELVKRQ KPTDEQYRLS RMTAAYAQIK SECAAMKNRH HAAKDEEAAK AYAQIIKAMN EQLEVLKEKI KEQTEKPNCK EGVKRLETIP AIGRMTAAVL FHHLTSSKFE TSNKFAAFAG LSPQQKESGT SVRGKGKLTK FGNRKLRAVL FMPAMVAYRI RAFPDFIKRL EEKKKPKKVI IAALMRKLAV IAYHVHKKGG DYDPSRYKSA // ID Q5F571_NEIG1 Unreviewed; 522 AA. AC Q5F571; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Trifunctional thioredoxin/methionine sulfoxide reductase A/B protein {ECO:0000313|EMBL:AAW90666.1}; DE EC=1.8.4.11 {ECO:0000313|EMBL:AAW90666.1}; DE EC=1.8.4.12 {ECO:0000313|EMBL:AAW90666.1}; GN ORFNames=NGO_2059 {ECO:0000313|EMBL:AAW90666.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90666.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC {ECO:0000256|SAAS:SAAS00005618}. CC -!- SIMILARITY: Contains MsrB (methionine-R-sulfoxide reductase) CC domain. {ECO:0000256|SAAS:SAAS00536110}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90666.1; -; Genomic_DNA. DR RefSeq; WP_010951394.1; NC_002946.2. DR RefSeq; YP_209078.1; NC_002946.2. DR ProteinModelPortal; Q5F571; -. DR SMR; Q5F571; 32-182, 196-364, 375-521. DR EnsemblBacteria; AAW90666; AAW90666; NGO_2059. DR GeneID; 3282737; -. DR KEGG; ngo:NGO2059; -. DR PATRIC; 20337919; VBINeiGon24812_2482. DR HOGENOM; HOG000243423; -. DR KO; K12267; -. DR OMA; AQYDITQ; -. DR OrthoDB; EOG6091JX; -. DR BioCyc; NGON242231:GI2G-1960-MONOMER; -. DR Proteomes; UP000000535; 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; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00536034, KW ECO:0000313|EMBL:AAW90666.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 522 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256183. FT DOMAIN 17 174 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 522 AA; 58057 MW; AB1394108B57B318 CRC64; MKHRTFFSLC AKFGCLLALG ACSPKIVDAG TATVPHTLST LKTADNRPAS VYLKKDKPTL IKFWASWCPL CLSELGQAEK WAQDAKFSSA NLITVASPGF LHEKKDGEFQ KWYAGLNYPK LPVVTDNGGT IAQNLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR NPNADLGSLK HSFYKPDTQK KDSAIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTENPSYED VSYRHTGHAE TVKVTYDADK LSLDDILQYY FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL PGKTKAAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SFNMRRTEVR SRAADSHLGH VFPDGPRDKG RLRYCINGAS LKFIPLEQMD AAGYGALKGK VK // ID Q5F510_NEIG1 Unreviewed; 201 AA. AC Q5F510; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Stringent starvation protein A {ECO:0000313|EMBL:AAW90727.1}; GN ORFNames=NGO_2130 {ECO:0000313|EMBL:AAW90727.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90727.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90727.1; -; Genomic_DNA. DR RefSeq; WP_003687122.1; NC_002946.2. DR RefSeq; YP_209139.1; NC_002946.2. DR ProteinModelPortal; Q5F510; -. DR EnsemblBacteria; AAW90727; AAW90727; NGO_2130. DR GeneID; 3282791; -. DR KEGG; ngo:NGO2130; -. DR PATRIC; 20338109; VBINeiGon24812_2577. DR HOGENOM; HOG000255228; -. DR KO; K03599; -. DR OMA; RIVLYEK; -. DR OrthoDB; EOG6MWN8X; -. DR BioCyc; NGON242231:GI2G-2021-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; EB45D7A74F53C5CB CRC64; MMTLYSGITC PFSHRCRFVL YEKGMDFEIK DIDIYNKPED LAVMNPYNQV PVLVERDLVL HESNIINEYI DERFPHPQLM PGDPVMRGRG RLVLYRMEKE LFNHVQVLEN PAAANKEQAK AREAIGNGLT MLSPSFSKSK YILGEDFSMI DVALAPLLWR LDHYDVKLGK SAAPLLKYAE RIFQREAFIE ALTPAEKAMR K // ID A0A0H4IW12_NEIG1 Unreviewed; 208 AA. AC A0A0H4IW12; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Restriction endonuclease EcoprrI subunit S {ECO:0000313|EMBL:AKO63618.1}; GN ORFNames=NGO_02155 {ECO:0000313|EMBL:AKO63618.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63618.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63618.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63618; AKO63618; NGO_02155. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AKO63618.1}; KW Hydrolase {ECO:0000313|EMBL:AKO63618.1}; KW Nuclease {ECO:0000313|EMBL:AKO63618.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 53 182 Methylase_S. {ECO:0000259|Pfam:PF01420}. SQ SEQUENCE 208 AA; 24352 MW; 6BEA9787501817E7 CRC64; MDMQSKAKKL IEMIQTAPVE WKPLGEVLVR TKGTKITAGQ MKEMHKDNAP LKIFAGGKTF ALVDFDDVPD KDIHREPSII VKSRGIIEFE YYDKPFSHKN EMWSYHSVNK HIYIKYVYYF LKTQENYFRN IGSKMQMPQI ATPDTDNYKI PIPSLETQQK IVKILDKFTE LEATLEATLE AELALRKRQY RYYRDLLLDF DNQIGGDS // ID A0A0H4IW51_NEIG1 Unreviewed; 72 AA. AC A0A0H4IW51; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63658.1}; GN ORFNames=NGO_04350 {ECO:0000313|EMBL:AKO63658.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63658.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63658.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63658; AKO63658; NGO_04350. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 72 AA; 7597 MW; 54B6C434E4A01726 CRC64; MSAACPELEG RYLDLVRRAA VSFGFAQGQA NPAGGQEETQ AASDAVSGRS VKKPIKINIE SKVPSSQTSV FR // ID A0A0H4J5N2_NEIG1 Unreviewed; 57 AA. AC A0A0H4J5N2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63697.1}; GN ORFNames=NGO_06300 {ECO:0000313|EMBL:AKO63697.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63697.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63697.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63697; AKO63697; NGO_06300. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 57 AA; 6803 MW; 3D2607F594C9973F CRC64; MLPIIRKKVK PDGIVYTDTF RSYDVLDVSE FSHLRKFNGI PKEHLGLYLK KCQWHLK // ID A0A0H4J610_NEIG1 Unreviewed; 103 AA. AC A0A0H4J610; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=PilS cassette {ECO:0000313|EMBL:AKO63807.1}; GN ORFNames=NGO_11105 {ECO:0000313|EMBL:AKO63807.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63807.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63807.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63807; AKO63807; NGO_11105. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 103 AA; 11255 MW; 5FDE4EAC216E2534 CRC64; MAGRQHFCRR GIPPSDIKGK YVQSVTVANG VVTAEMKSDG VNKEIKGKKL SLWGRRQDGS VKWFCGQPVT RNDAKADDVK ADAANAIETK HLPSTCRDEP TAK // ID Q5F5B9_NEIG1 Unreviewed; 480 AA. AC Q5F5B9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 51. DE SubName: Full=Protease TldD {ECO:0000313|EMBL:AAW90618.1}; GN Name=tldD {ECO:0000313|EMBL:AAW90618.1}; GN ORFNames=NGO_2010 {ECO:0000313|EMBL:AAW90618.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90618.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90618.1; -; Genomic_DNA. DR RefSeq; WP_010951381.1; NC_002946.2. DR RefSeq; YP_209030.1; NC_002946.2. DR ProteinModelPortal; Q5F5B9; -. DR EnsemblBacteria; AAW90618; AAW90618; NGO_2010. DR GeneID; 3281898; -. DR KEGG; ngo:NGO2010; -. DR PATRIC; 20337801; VBINeiGon24812_2424. DR HOGENOM; HOG000224929; -. DR KO; K03568; -. DR OMA; MVGNDLS; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; NGON242231:GI2G-1911-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90618.1}; KW Protease {ECO:0000313|EMBL:AAW90618.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 480 AA; 50699 MW; 8E87C8AA9FB3B97A CRC64; MHPTYSAVQA RLLEANRLSP ELLAKSLCII GAHHVDYADI YCQRTAYESW HLEEGIVKSG SFQIDQGVGV RAVSGDKTAF AYADSLCIDS INRSARAVRA IGAAGGKVSA KMPSETRGKP VCSASDPIAG LDSAAKVALL NKVEAIAKAA DPRIVQVMAG LTCEYDMVYL ARLDGKHAAD IRPMVRLNVT VIAKQGERRE QGGAGGGGRY DLAYFDETLV RQFVDAAVKQ ALTNLESRPA PAGEMTVVLG NGWPGVLLHE AVGHGLEGDF NRKGTSVFSG RIGERVAAKG VTVVDQGDIA GRRGSLNIDD EGNETRRTVL IEDGILVGYM QDETNARLTG TQSTGNGRRQ SYASVPMPRM TNTFMENGSY EPEEIIASID KGIYAVNFGG GQVDITSGKF VFGASEAWWV EGGRLQYPVK GATIIGNGPE VLKHVSMIGN DTALDSGVGV CGKEGQSVPV GVGQPTLRID AGLTVGGSAI // ID Q5F5K0_NEIG1 Unreviewed; 117 AA. AC Q5F5K0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 68. DE RecName: Full=Arsenate reductase {ECO:0000256|RuleBase:RU362029}; DE EC=1.20.4.1 {ECO:0000256|RuleBase:RU362029}; GN ORFNames=NGO_1924 {ECO:0000313|EMBL:AAW90537.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90537.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite + CC glutaredoxin disulfide + H(2)O. {ECO:0000256|RuleBase:RU362029}. CC -!- SIMILARITY: Belongs to the ArsC family. CC {ECO:0000256|RuleBase:RU362029, 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; AE004969; AAW90537.1; -; Genomic_DNA. DR RefSeq; WP_003692077.1; NC_002946.2. DR RefSeq; YP_208949.1; NC_002946.2. DR ProteinModelPortal; Q5F5K0; -. DR EnsemblBacteria; AAW90537; AAW90537; NGO_1924. DR GeneID; 3282850; -. DR KEGG; ngo:NGO1924; -. DR PATRIC; 20337586; VBINeiGon24812_2320. DR HOGENOM; HOG000059717; -. DR KO; K00537; -. DR OMA; MIKIYHN; -. DR OrthoDB; EOG6PP9QC; -. DR BioCyc; NGON242231:GI2G-1827-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC. 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362029}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 117 AA; 12876 MW; 595C5A82E1D863D7 CRC64; MSEIKIFHNP RCSKSRAAVS LLEERGIAAE AVKYLDTPPD LSELKDIFNK LGLESARGMM RVKDDLYKEL GLDNPDLDND ALLRAIADHP ALLERPIVLA NGKAAVGRPL ENIEAVL // ID A0A0H4IV74_NEIG1 Unreviewed; 226 AA. AC A0A0H4IV74; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63680.1}; GN ORFNames=NGO_05420 {ECO:0000313|EMBL:AKO63680.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63680.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63680.1; -; Genomic_DNA. DR RefSeq; WP_030003513.1; NC_002946.2. DR RefSeq; YP_008914852.1; NC_002946.2. DR EnsemblBacteria; AKO63680; AKO63680; NGO_05420. DR GeneID; 19592997; -. DR KEGG; ngo:NGO1040a; -. DR Proteomes; UP000000535; 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; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 49 226 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 226 AA; 25582 MW; CAE0487165BF924C CRC64; MQADLAYAYE HITRDYPDAA GANQGKKIST VSDYFKNIRT HSIHPRVSVG YDFGGWRIAA DYARYRKWND NKYSVDIKEL ENKNQNKRDL KTENQENGSF HAVSSLGLSA VYDFKLNDKF KPYIGARVAY GHVRHSIDST KKTTEFLTAA GQDGGAPTVY NNGSTQDAHQ ESDSIRRVGL GVIAGIGFDI TPKLTLDTGY RYHNWGRLEN TRFKTHEASL GVRYRF // ID Q5F945_NEIG1 Unreviewed; 186 AA. AC Q5F945; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89292.1}; GN ORFNames=NGO_0558 {ECO:0000313|EMBL:AAW89292.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89292.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89292.1; -; Genomic_DNA. DR RefSeq; WP_003691360.1; NC_002946.2. DR RefSeq; YP_207704.1; NC_002946.2. DR ProteinModelPortal; Q5F945; -. DR EnsemblBacteria; AAW89292; AAW89292; NGO_0558. DR GeneID; 3282459; -. DR KEGG; ngo:NGO0558; -. DR PATRIC; 20334170; VBINeiGon24812_0657. DR HOGENOM; HOG000262660; -. DR OMA; GEFNRDE; -. DR OrthoDB; EOG6QCDB3; -. DR BioCyc; NGON242231:GI2G-532-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 186 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256629. FT DOMAIN 20 184 YceI. {ECO:0000259|SMART:SM00867}. SQ SEQUENCE 186 AA; 20261 MW; 2E0C7D8E5D5047DD CRC64; MKKIIFAALA AAAVGTASAT YKVDEYHANV RFAIDHFNTS TNVGGFYGLT GSVEFDQAKR DGKIDITIPV ANLQSGSQPF TGHLKSADIF DAAQYPDIRF VSTKFNFNGK KLVSVDGNLT MRGKTAPVKL KAEKFNCYQS PMAETEVCGG DFSTTIDRTK WGVDYLVNAG MTKNVRIDIQ IEAAKQ // ID Q5F6F9_NEIG1 Unreviewed; 472 AA. AC Q5F6F9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356}; GN ORFNames=NGO_1600 {ECO:0000313|EMBL:AAW90228.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90228.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90228.1; -; Genomic_DNA. DR RefSeq; WP_003697465.1; NC_002946.2. DR RefSeq; YP_208640.1; NC_002946.2. DR ProteinModelPortal; Q5F6F9; -. DR SMR; Q5F6F9; 2-472. DR EnsemblBacteria; AAW90228; AAW90228; NGO_1600. DR GeneID; 3281610; -. DR KEGG; ngo:NGO1600; -. DR PATRIC; 20336738; VBINeiGon24812_1915. DR HOGENOM; HOG000005157; -. DR KO; K01915; -. DR OMA; KVLNQVG; -. DR OrthoDB; EOG6B360N; -. DR BioCyc; NGON242231:GI2G-1496-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Ligase {ECO:0000256|RuleBase:RU004356}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004356}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT MOD_RES 401 401 O-AMP-tyrosine. FT {ECO:0000256|PIRSR:PIRSR604809-50}. SQ SEQUENCE 472 AA; 52004 MW; 6B4CAEAA53E95672 CRC64; MSIKNAVKLI EESEARFVDL RFTDTKGKQH HFTVPARIVL EDPEEWFENG PAFDGSSIGG WKGIEASDMQ LRPDASTAFV DPFYDDVTVV ITCDVIDPAD GQGYDRDPRS IARRAEAYLK SSGIGDTAYF GPEPEFFVFD GVEFETDMHK TRYEITSESG AWASGLHMDG QNTGHRPAVK GGYAPVAPID CGQDLRSAMV NILEGLGIEV 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 A0A0H4IW04_NEIG1 Unreviewed; 80 AA. AC A0A0H4IW04; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63608.1}; GN ORFNames=NGO_01255 {ECO:0000313|EMBL:AKO63608.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63608.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63608.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63608; AKO63608; NGO_01255. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 80 AA; 8862 MW; 9D5B6F9AD27AB919 CRC64; MQTVWKKPQR RGGGICQIVA GAGVRFFVCG VTLGVGHFRR RLCRLKRPAG DAAAFPIDRH ICRPRSGRVL PGRPPICLRL // ID Q5F975_NEIG1 Unreviewed; 329 AA. AC Q5F975; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Integrase {ECO:0000313|EMBL:AAW89262.1}; GN ORFNames=NGO_0524 {ECO:0000313|EMBL:AAW89262.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89262.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000256|SAAS:SAAS00541913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89262.1; -; Genomic_DNA. DR RefSeq; WP_003689040.1; NC_002946.2. DR RefSeq; YP_207674.1; NC_002946.2. DR ProteinModelPortal; Q5F975; -. DR EnsemblBacteria; AAW89262; AAW89262; NGO_0524. DR GeneID; 3282923; -. DR KEGG; ngo:NGO0524; -. DR PATRIC; 20334094; VBINeiGon24812_0619. DR HOGENOM; HOG000255251; -. DR OMA; VIREMAM; -. DR OrthoDB; EOG61ZTF7; -. DR BioCyc; NGON242231:GI2G-502-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 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 Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 164 320 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. SQ SEQUENCE 329 AA; 37516 MW; A665EEEA243DC48C CRC64; MATITQRNGK WRVQIRMKGV SRSATFERAS DAKAWAARIE SQIMDGIQGN APRNTIFADL IRRYLSEVTP SKRGAREESY RIGRALKTPL AKVRLADLRP QDFADWRDQR LQEVSPTSVG RELTTLSAVC EHAMKEWGLL RENPVRKISK PKKSRARTRR PTEQEIADIC AALLYRPNEK PKMAVQRVAV AVLFAIETAM RAGEICGLKW ADVNMRRRIA HLPITKNGDS RDVPLSLRAA ELIEQLRGID DTWVFSLDAK SLDVLFRRAR DNCGIQGLHF HDTRREALTR LSKKVPVEVL AKISGHRDLR ILLNVYYRPD MADIAKMLD // ID A0A0H4IV19_NEIG1 Unreviewed; 164 AA. AC A0A0H4IV19; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Cell filamentation protein Fic {ECO:0000313|EMBL:AKO63635.1}; GN ORFNames=NGO_03335 {ECO:0000313|EMBL:AKO63635.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63635.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63635.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63635; AKO63635; NGO_03335. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 145 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 164 AA; 19446 MW; 95C6A90AD1BCD0B3 CRC64; MQPITGNFDL AHLQTIHREL FGNVYDWAGK IRRVDISKGN TRFANFAFIE NESRKLLEKL KNENYLRVLD KDKFAERAAY YLDELNVLHP FREGNGRTLR LFMTQLAIKN GFQIHWQNIS AEQMIQACIQ AYHADSSLLA RLIIRQFRTI VFFRRLKHQQ TTIF // ID Q5F679_NEIG1 Unreviewed; 384 AA. AC Q5F679; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 61. DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:AAW90308.2}; GN ORFNames=NGO_1683 {ECO:0000313|EMBL:AAW90308.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90308.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90308.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F679; -. DR EnsemblBacteria; AAW90308; AAW90308; NGO_1683. DR PATRIC; 20336924; VBINeiGon24812_2006. DR HOGENOM; HOG000112072; -. DR OMA; MTTANSE; -. DR OrthoDB; EOG6C014B; -. DR BioCyc; NGON242231:GI2G-1578-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 41470 MW; 5B05695174B2FF41 CRC64; METHTDETKL QNTQVKRKRR LTALTLLFAL SAAAAGSAFF LWWQHEEETE DAYVAGRVVQ VTPQKGGTVR KVLHDDTDAV KKGDVLAVLD DDNDVLAYER AKNELVQAVR QNRRQNAATS QAGAQVALRR ADLARAQDDL RRRSALAESG AVSAEELAHA RTAVSQAQAA VKAALAEESS ARAALGGDVS LREQPEVQTA IGRLKDAWLN LRRTQVRAPA DGQVAKRSVQ VGQQVAAGAP LMAVVPLSDV WVDANFKETQ LRHMKIGQPA ELVSDLYGKQ IVYRGRVAGF SAGTGSAFSL IPAQNATGNW IKVVQRVPVR IVLNREDVDR HPLRIGLSMT VKVDTSAAGA PVSKTPGAAL PEMESTDWSE VDRTVDEILG QSAP // ID A0A0H4J5X0_NEIG1 Unreviewed; 98 AA. AC A0A0H4J5X0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63762.1}; GN ORFNames=NGO_08995 {ECO:0000313|EMBL:AKO63762.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63762.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63762.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63762; AKO63762; NGO_08995. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.40.128.100; -; 1. DR InterPro; IPR009876; OM_adhesin_OpcA. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 98 AA; 10944 MW; 6496FFAC124E268D CRC64; MRFKAEYARS KNDADDKRGN AHIANGAIGK MAAVYAGYTY TQPGGESTRF RGGLERVQVK RYLGEKCCGY ACPKSERFTL QADGEIRQNL GEGWFLKL // ID Q5F8V6_NEIG1 Unreviewed; 263 AA. AC Q5F8V6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 79. 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 ORFNames=NGO_0654 {ECO:0000313|EMBL:AAW89381.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89381.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89381.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8V6; -. DR EnsemblBacteria; AAW89381; AAW89381; NGO_0654. DR PATRIC; 20334398; VBINeiGon24812_0771. DR HOGENOM; HOG000238069; -. DR OMA; ITEHKRQ; -. DR OrthoDB; EOG64JFM7; -. DR BioCyc; NGON242231:GI2G-621-MONOMER; -. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. FT DOMAIN 7 226 NAD_synthase. {ECO:0000259|Pfam:PF02540}. SQ SEQUENCE 263 AA; 29230 MW; 7FE07EA9EE1E72F2 CRC64; MDTQAVITHI VRWLDEYAAQ ANAKGFVVGV SGGIDSAVVS TLAARTGRTT LLLDMPIRQH PGQLERARRH IRNLQGQYAN VSAQTANLTD TFQTFEQTVG VHQTAFANQP LSLANARSRL RMLTLYYYGQ IHGLLVTGTG NKVEDFGVGF FTKYGDGGVD ISPIADLTKT QVYRLAEALG VDEAIQKAPP TDGLWDTERT DEEQMGASYP ELEWAMGVYG TRKPEDFEGR RREVLEIYTR LHRAMQHKIN PIPVCRIPPE LLG // ID Q5F6B2_NEIG1 Unreviewed; 318 AA. AC Q5F6B2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 50. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90275.1}; GN ORFNames=NGO_1648 {ECO:0000313|EMBL:AAW90275.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90275.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90275.1; -; Genomic_DNA. DR RefSeq; WP_003694155.1; NC_002946.2. DR RefSeq; YP_208687.1; NC_002946.2. DR EnsemblBacteria; AAW90275; AAW90275; NGO_1648. DR GeneID; 3281292; -. DR KEGG; ngo:NGO1648; -. DR PATRIC; 20336836; VBINeiGon24812_1963. DR HOGENOM; HOG000130878; -. DR OMA; LAKPAYY; -. DR OrthoDB; EOG62VNHT; -. DR BioCyc; NGON242231:GI2G-1544-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 149 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 122 153 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 318 AA; 36786 MW; 557286F197B2C601 CRC64; MNIIGPDISK DTIDATLHKT NGSIHYIKFK NNDDGLKQFR LWIKGNRIRK VYIGMEATGI YYEKAADMLS SYYTVYVINP LKIKDYGKSR FNRTKTDKAD SNLIADYIKR HQDTLIPYQI PKNKALQKLI NLKNQLQQQQ KQIKNRLHST EEDFIRNIHQ DLIDTIQDKM EQVKIAISEQ IKKQTDNNHY RNLQTIPSIG KDTASVLYAQ LTEKHFKTAN QFVSYAGLSP AIIQSGTSVR GRGRLSRYGN RRLKSTLYMP ALCAYRFNAF PKLINNLKKA GKPKMVIIVA IMRKLAKPAY YIVKTGQPYD AERHRLNQ // ID Q5F5A6_NEIG1 Unreviewed; 101 AA. AC Q5F5A6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE RecName: Full=Cell division protein ZapA {ECO:0000256|SAAS:SAAS00072473}; GN ORFNames=NGO_2023 {ECO:0000313|EMBL:AAW90631.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90631.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90631.1; -; Genomic_DNA. DR RefSeq; WP_003686942.1; NC_002946.2. DR RefSeq; YP_209043.1; NC_002946.2. DR ProteinModelPortal; Q5F5A6; -. DR EnsemblBacteria; AAW90631; AAW90631; NGO_2023. DR GeneID; 3282724; -. DR KEGG; ngo:NGO2023; -. DR PATRIC; 20337829; VBINeiGon24812_2438. DR HOGENOM; HOG000263522; -. DR KO; K09888; -. DR OMA; GFDMNEF; -. DR OrthoDB; EOG69SKDP; -. DR BioCyc; NGON242231:GI2G-1924-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00452647}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Septation {ECO:0000256|SAAS:SAAS00452627}. FT DOMAIN 6 70 ZapA. {ECO:0000259|Pfam:PF05164}. SQ SEQUENCE 101 AA; 10951 MW; 1888883E9DB4ECB7 CRC64; MNIEQVYIEV MHARLTVNTP AEEKDTLLQA VGMLNGKAEA IREGGRVADS EKIVIMAALN VVHDLLKTSL NGGDLAIGDF ARKITDMDNA CQKALSRLGQ E // ID Q5F602_NEIG1 Unreviewed; 376 AA. AC Q5F602; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Glycosyl transferase family 1 {ECO:0000313|EMBL:AAW90385.1}; GN ORFNames=NGO_1765 {ECO:0000313|EMBL:AAW90385.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90385.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90385.1; -; Genomic_DNA. DR RefSeq; WP_010951342.1; NC_002946.2. DR RefSeq; YP_208797.1; NC_002946.2. DR ProteinModelPortal; Q5F602; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW90385; AAW90385; NGO_1765. DR GeneID; 3281093; -. DR KEGG; ngo:NGO1765; -. DR PATRIC; 20337148; VBINeiGon24812_2114. DR HOGENOM; HOG000257101; -. DR OMA; SYYREGI; -. DR OrthoDB; EOG6091DG; -. DR BioCyc; NGON242231:GI2G-1660-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90385.1}. FT DOMAIN 2 137 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13477}. FT DOMAIN 198 348 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 376 AA; 42007 MW; 555DD03C7C407A3A CRC64; MKIVFITTVA SSIYGFRAPV IKKLIGKNHQ VYAFVSEFSD NELDIIREMG VTPVTYRSNR SGVNPFSDIK STFLIFKALK KISPDLVFPY FAKPVIFGTF AAKLAGVPRI VGMLEGLGFA FTPQPEGIPL KTKIIKGILI ALYRIALPML ESLIVLNPDD KDELLHQYGI KIKNIHILGG IGLDLRQYPY SEADIPDEKE PVKFLFIGRF LKEKGIDDFI RAAEQVKGKY PDTVFTALGA IDKSRGGGGD LERFIARDII RFPGFVNNVS EVIKAHHIFV LPSYYREGVP RSTQEAMAVG RAVITTDVPG CRETVADKVN GFLIEPWNPR ILAEKMIYFI ENRAAVRLMA NASYAIAKDK FDAEKVDLKF LDILKA // ID Q5FA46_NEIG1 Unreviewed; 354 AA. AC Q5FA46; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Butanediol dehydrogenase {ECO:0000313|EMBL:AAW88941.1}; GN ORFNames=NGO_0186 {ECO:0000313|EMBL:AAW88941.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88941.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88941.1; -; Genomic_DNA. DR RefSeq; WP_003694824.1; NC_002946.2. DR RefSeq; YP_207353.1; NC_002946.2. DR ProteinModelPortal; Q5FA46; -. DR EnsemblBacteria; AAW88941; AAW88941; NGO_0186. DR GeneID; 3281536; -. DR KEGG; ngo:NGO0186; -. DR PATRIC; 20333299; VBINeiGon24812_0232. DR HOGENOM; HOG000294670; -. DR KO; K00004; -. DR OMA; MIVSIFE; -. DR OrthoDB; EOG6N949Q; -. DR BioCyc; NGON242231:GI2G-171-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Zinc {ECO:0000256|RuleBase:RU361277}. SQ SEQUENCE 354 AA; 37933 MW; 9CFD66DEB02F77BA CRC64; MKAARFYNKG DIRIEDIPEP TVAPGTVGIN VAWCGICGTD LHEFMEGPIF IPPCGHPHPI SGESAPVTMG HEFSGVVYAV GEGVDDIKVG QHVVVEPYII RDDVPTGEGS NYHLSKDMNF IGLGGCGGGL SEKIAVKRRW VHPISDKIPL DQAALIEPLS VGHHAYVRSG AKAGDVALVG GAGPIGLLLA AVLKAKGIKV IITELSKARK DKARESGVAD YILDPSEVDV VEEVKKLTNG EGVDVAFECT SVNKVLDTLV EACKPAANLV IVSIWSHPAT VNVHSVVMKE LDVRGTIAYC NDHAETIKLV EEGKINLEPF ITQRIKLDKL VSEGFERLIH NNESAVKIIV NPNL // ID Q5F724_NEIG1 Unreviewed; 412 AA. AC Q5F724; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=Multidrug transporter {ECO:0000313|EMBL:AAW90013.1}; GN ORFNames=NGO_1365 {ECO:0000313|EMBL:AAW90013.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90013.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90013.1; -; Genomic_DNA. DR RefSeq; WP_010951249.1; NC_002946.2. DR RefSeq; YP_208425.1; NC_002946.2. DR ProteinModelPortal; Q5F724; -. DR EnsemblBacteria; AAW90013; AAW90013; NGO_1365. DR GeneID; 3282559; -. DR KEGG; ngo:NGO1365; -. DR PATRIC; 20336115; VBINeiGon24812_1606. DR HOGENOM; HOG000158247; -. DR KO; K03585; -. DR OMA; CGPKQSA; -. DR OrthoDB; EOG6JMMSV; -. DR BioCyc; NGON242231:GI2G-1278-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 412 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256045. FT DOMAIN 64 300 HlyD_D23. {ECO:0000259|Pfam:PF16576}. SQ SEQUENCE 412 AA; 42758 MW; FC8C75CDBFEAE1BB CRC64; MAFYASKAMR AAALAAAVAL ALSSCGKGGD AAQGGQPAGR EAPAPVVGVV TVHPQTVALT VELPGRLESL RTADVRAQVG GIIQKRLFQE GSYVRAGQPL YQIDSSTYEA GLESARAQLA TAQATLAKAD ADLARYKPLV SADAISKQEY DAAVTAKRSA EAGVKAAQAA IKSAGINLNR SRITAPISGF IGQSKVSEGT LLNAGDTTVL ATIRQTNPMY VNVTQSASEV MKLRRQIAEG KLLAADGAIA VGIKFDDGTV YPEKGRLLFA DPTVEESTGQ ITLRAAVSND QNILMPGLYV RVLMDQVAAD NAFIVPQQAV TRGAKDTVMI VNAQGGMEPR EVTVAQQQGT NWIVTSGLKD GDKVVVEGIS IAGMTGAKKV TPKEWAPSEN QAAAPQAGVQ TASEAKPASE AK // ID Q5F4Y0_NEIG1 Unreviewed; 248 AA. AC Q5F4Y0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=3-ketoacyl-ACP reductase {ECO:0000313|EMBL:AAW90757.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AAW90757.1}; GN Name=fabG {ECO:0000313|EMBL:AAW90757.1}; GN ORFNames=NGO_2163 {ECO:0000313|EMBL:AAW90757.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90757.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90757.1; -; Genomic_DNA. DR RefSeq; WP_003690463.1; NC_002946.2. DR RefSeq; YP_209169.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y0; -. DR SMR; Q5F4Y0; 5-247. DR EnsemblBacteria; AAW90757; AAW90757; NGO_2163. DR GeneID; 3282761; -. DR KEGG; ngo:NGO2163; -. DR PATRIC; 20338182; VBINeiGon24812_2613. DR KO; K00059; -. DR OMA; GMMKRRW; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NGON242231:GI2G-2051-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW90757.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 248 AA; 26035 MW; 8650D6CEBA6DF869 CRC64; MSTQDLSGKI ALVTGASRGI GAAIADTLAA AGAKIIGTAT GESGAAAISK RLAQWGGEGR VLNSAEPETV ENLIADIEKT FGKLDILVNN AGITRDNLLM RMKEEEWDDI MQVNLKSVFR ASKAVLRGMM KQRAGRIINI TSVVGVMGNA GQTNYAAAKA GLIGFAKSMA REVGSRGITV NCVAPGFIDT DMTRALPEET RQTFTAQTAL GRFGDAQDIA DAVLFLASDQ AKYITGQTLH VNGGMLMP // ID A0A0H4IW71_NEIG1 Unreviewed; 59 AA. AC A0A0H4IW71; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63678.1}; GN ORFNames=NGO_05310 {ECO:0000313|EMBL:AKO63678.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63678.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63678.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63678; AKO63678; NGO_05310. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6940 MW; 84673BB4F1A4431F CRC64; MNTLKAHAQQ LMMDHIHPAT GKSLFILKQA KTLLLHNRPD VYRAKRPKTK HIIPHERHK // ID A0A0H4IWI2_NEIG1 Unreviewed; 71 AA. AC A0A0H4IWI2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63793.1}; GN ORFNames=NGO_10560 {ECO:0000313|EMBL:AKO63793.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63793.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63793.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63793; AKO63793; NGO_10560. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 8124 MW; 44314DB8E584A773 CRC64; MNIINYTGDD IIISLTREEL QLLRSLVIEI YAGVCIDAEE FEIVSGIRNP QLVQELEQHL IEAYNLMDTS N // ID A0A0H4IWA0_NEIG1 Unreviewed; 112 AA. AC A0A0H4IWA0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63708.1}; GN ORFNames=NGO_06860 {ECO:0000313|EMBL:AKO63708.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63708.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63708.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63708; AKO63708; NGO_06860. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 112 AA; 11765 MW; 0111796D08B9B25A CRC64; MTKLYAEIAE MEAQDDGTVK VWGYASSEAV DSDGEVIAAA MKAAIPDYMK FGEVREMHGS NAAGTAIEIN VEDDGRTFFG AHIVDPVAVK KVKTGVYKGF SIGGSVTAVC LG // ID Q5F9L1_NEIG1 Unreviewed; 655 AA. AC Q5F9L1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 91. 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 ORFNames=NGO_0382 {ECO:0000313|EMBL:AAW89126.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89126.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89126.1; -; Genomic_DNA. DR RefSeq; WP_003687806.1; NC_002946.2. DR RefSeq; YP_207538.1; NC_002946.2. DR ProteinModelPortal; Q5F9L1; -. DR SMR; Q5F9L1; 149-403. DR MEROPS; M41.001; -. DR EnsemblBacteria; AAW89126; AAW89126; NGO_0382. DR GeneID; 3282447; -. DR KEGG; ngo:NGO0382; -. DR PATRIC; 20333769; VBINeiGon24812_0462. DR HOGENOM; HOG000217276; -. DR KO; K03798; -. DR OMA; NMDILHS; -. DR OrthoDB; EOG6PKFBJ; -. DR BioCyc; NGON242231:GI2G-361-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89126.1}; KW Cell division {ECO:0000313|EMBL:AAW89126.1}; 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:UP000000535}; 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:UP000000535}; 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; 72116 MW; 21987F4893FC35C4 CRC64; MGNTFKSILV WVALGIGLMA AFNALDGKKE DNGQIEYSQF IRQVNNGEVS GVNIEGSVVS GYLIKGERTD KSTFFTNAPL DDNLIQTLLN KNVRVKVTPE EKPSALTALF YSLLPVLLLI GAWFYFMRMQ AGGGGKGGAF 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 REKTEAPAPA DTASTESGQQ PENKA // ID Q5F6J5_NEIG1 Unreviewed; 225 AA. AC Q5F6J5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90192.1}; GN ORFNames=NGO_1559 {ECO:0000313|EMBL:AAW90192.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90192.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ompA family. CC {ECO:0000256|RuleBase:RU003859}. CC -!- SIMILARITY: Contains OmpA-like domain. CC {ECO:0000256|SAAS:SAAS00509386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90192.1; -; Genomic_DNA. DR RefSeq; WP_003703604.1; NC_002946.2. DR RefSeq; YP_208604.1; NC_002946.2. DR ProteinModelPortal; Q5F6J5; -. DR EnsemblBacteria; AAW90192; AAW90192; NGO_1559. DR GeneID; 3281400; -. DR KEGG; ngo:NGO1559; -. DR PATRIC; 20336628; VBINeiGon24812_1860. DR HOGENOM; HOG000189914; -. DR OMA; IGNYMDQ; -. DR OrthoDB; EOG6PP9QB; -. DR BioCyc; NGON242231:GI2G-1460-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR Gene3D; 3.30.1330.60; -; 1. DR InterPro; IPR008816; Gly_zipper_2TM_dom. DR InterPro; IPR006664; OMP_bac. DR InterPro; IPR006665; OmpA-like. DR Pfam; PF00691; OmpA; 1. DR Pfam; PF05433; Rick_17kDa_Anti; 1. DR PRINTS; PR01021; OMPADOMAIN. DR SUPFAM; SSF103088; SSF103088; 1. DR PROSITE; PS51123; OMPA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003859}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 225 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256203. FT DOMAIN 98 216 OmpA-like. {ECO:0000259|PROSITE:PS51123}. SQ SEQUENCE 225 AA; 23411 MW; 7FC15986BD9B600C CRC64; MTFFKPSTVV LTASALALSG CVADPVTGQQ SPNKSAMYGL GGAAVCGIVG ALTHSGKGAR NSALACGAIG AGVGGYMDYQ EQRLRQNLAG TQIEIQRQGN QIRLVMPESV TFATGSAALG GSAQYALNTA AQTLVQYPDT TLTINGHTDN TGSDAVNNPL SQHRAQAVAY YLQTRGVAAS RLTVYGYGSH MPVASNATVE GRAQNRRVEI LINPDQRAVN AARHM // ID Q5F592_NEIG1 Unreviewed; 89 AA. AC Q5F592; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Phosphocarrier protein HPr {ECO:0000313|EMBL:AAW90645.1}; GN ORFNames=NGO_2037 {ECO:0000313|EMBL:AAW90645.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90645.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00262299}. CC -!- SIMILARITY: Contains HPr domain. {ECO:0000256|SAAS:SAAS00145659}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90645.1; -; Genomic_DNA. DR RefSeq; WP_003686964.1; NC_002946.2. DR RefSeq; YP_209057.1; NC_002946.2. DR ProteinModelPortal; Q5F592; -. DR EnsemblBacteria; AAW90645; AAW90645; NGO_2037. DR GeneID; 3282710; -. DR KEGG; ngo:NGO2037; -. DR PATRIC; 20337857; VBINeiGon24812_2452. DR HOGENOM; HOG000278398; -. DR KO; K11189; -. DR OMA; AEVWVTR; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; NGON242231:GI2G-1938-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00482562}; KW Kinase {ECO:0000256|SAAS:SAAS00589026}; KW Phosphotransferase system {ECO:0000256|SAAS:SAAS00589044}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00589026}; KW Transferase {ECO:0000256|SAAS:SAAS00589026}. FT DOMAIN 1 88 HPr. {ECO:0000259|PROSITE:PS51350}. SQ SEQUENCE 89 AA; 9622 MW; EE9710B86C4F473B CRC64; MLKQSIEIIN KLGLHARASS KFTQTASQFK SEVWVTKNGS RVNGKSIMGL MMLAAAKGTV IELETDGLDE AAAMKALTDL INDYFGEGE // ID A0A0H4IRX7_NEIG1 Unreviewed; 46 AA. AC A0A0H4IRX7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63676.1}; GN ORFNames=NGO_05205 {ECO:0000313|EMBL:AKO63676.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63676.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63676.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63676; AKO63676; NGO_05205. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 46 AA; 4996 MW; 3B81A12550791DA0 CRC64; MKFVAKCRPE TSVCATRRNL FQGFVNGGCT LISVKPNIIL SIGDLP // ID A0A0H4J5Y6_NEIG1 Unreviewed; 115 AA. AC A0A0H4J5Y6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63782.1}; GN ORFNames=NGO_10085 {ECO:0000313|EMBL:AKO63782.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63782.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63782.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63782; AKO63782; NGO_10085. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR005017; OMPP1/FadL/TodX. DR Pfam; PF03349; Toluene_X; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 115 AA; 12458 MW; DF65741BE991FE39 CRC64; MLPSIHYEAD SATDFTGLPV QGSKNGKITK TTVAPHIYGA YKVNDNLTVG LGVYVPFGSA TEYEKDSVLR HNINKLGLTS IAVEPVAAWK LNERHSFGAG IIAQHNSAEL RKYAD // ID Q5F5Z8_NEIG1 Unreviewed; 678 AA. AC Q5F5Z8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:AAW90389.1}; GN ORFNames=NGO_1770 {ECO:0000313|EMBL:AAW90389.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90389.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90389.1; -; Genomic_DNA. DR RefSeq; WP_010951344.1; NC_002946.2. DR RefSeq; YP_208801.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z8; -. DR EnsemblBacteria; AAW90389; AAW90389; NGO_1770. DR GeneID; 3281147; -. DR KEGG; ngo:NGO1770; -. DR PATRIC; 20337168; VBINeiGon24812_2124. DR HOGENOM; HOG000245986; -. DR KO; K01414; -. DR OMA; NQTPPVD; -. DR OrthoDB; EOG6WHNPN; -. DR BioCyc; NGON242231:GI2G-1664-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; KW Zinc {ECO:0000256|RuleBase:RU003435}. SQ SEQUENCE 678 AA; 75905 MW; 899A0F38147E929A CRC64; MIDNALLHLG EEPRFNQIKT EDIKPAVQTA IAEARGQIAA VKAQTHTGWA NTVERLTGIT ERVGRIWGVV SHLNSVVDTP ELRAVYNELM PEITVFFTEI GQDIELYNRF KTIKNSPEFA TLSPAQKTKL DHDLRDFVLS GAELPPERQA ELAKLQTEGA QLSAKFSQNV LDATDAFGIY FDDAAPLAGI PEDALAMFAA AAQSEGKTGY KIGLQIPHYL AVIQYAGNRE LREQIYRAYV TRASELSNDG KFDNTANIDR TLENALKTAK LLGFKNYAEL SLATKMADTP EQVLNFLHDL ARRAKPYAEK DLAEVKAFAR EHLGLADPQP WDLSYAGEKL REAKYAFSET EVKKYFPVGK VLAGLFAQIK KLYGIGFAEK TVPVWHKDVR YFELQQNGKT IGGVYMDLYA REGKRGGAWM NDYKGRRRFA DGTLQLPTAY LVCNFAPPVG GKEARLSHDE ILTLFHETGH GLHHLLTQVD ELGVSGINGV EWDAVELPSQ FMENFVWEYN VLAQMSAHEE TGEPLPKELF DKMLAAKNFQ RGMFLVRQME FALFDMMIYS ESDECRLKNW QQVLDSVRKE VAVIQPPEYN RFANSFGHIF AGGYSAGYYS YAWAEVLSTD AYAAFEESDD VAATGKRFWQ EILAVGGSRS AAESFKAFRG REPSIDALLR HSGFDNAA // ID Q5F9P5_NEIG1 Unreviewed; 116 AA. AC Q5F9P5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 49. DE SubName: Full=Pilus assembly protein {ECO:0000313|EMBL:AAW89092.1}; GN ORFNames=NGO_0348 {ECO:0000313|EMBL:AAW89092.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89092.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89092.1; -; Genomic_DNA. DR RefSeq; WP_003687757.1; NC_002946.2. DR RefSeq; YP_207504.1; NC_002946.2. DR EnsemblBacteria; AAW89092; AAW89092; NGO_0348. DR GeneID; 3281205; -. DR KEGG; ngo:NGO0348; -. DR PATRIC; 20333693; VBINeiGon24812_0424. DR HOGENOM; HOG000290810; -. DR KO; K02676; -. DR OMA; GIFVPTQ; -. DR OrthoDB; EOG69SKDG; -. DR BioCyc; NGON242231:GI2G-327-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 15 88 PilZ. {ECO:0000259|Pfam:PF07238}. SQ SEQUENCE 116 AA; 12797 MW; 18B72EC6AE6C6BAB CRC64; MSDGQNIPAK MMSLQLKDMN LLYSSYMPFL EHGGLFVQTD DVFSIGDDIL LAVEILNFPK LFLPTKVAWI NPASTSSKPK GVGLAFTKHE NCLKVKDQIE VELGSTISGS RPTFTM // ID Q5F5H0_NEIG1 Unreviewed; 608 AA. AC Q5F5H0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 64. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90567.2}; GN ORFNames=NGO_1956 {ECO:0000313|EMBL:AAW90567.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90567.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90567.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5H0; -. DR EnsemblBacteria; AAW90567; AAW90567; NGO_1956. DR PATRIC; 20337655; VBINeiGon24812_2354. DR HOGENOM; HOG000263477; -. DR OMA; KSATPMH; -. DR OrthoDB; EOG6F81K6; -. DR BioCyc; NGON242231:GI2G-1857-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00560982, KW ECO:0000256|SAAS:SAAS00560990}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00560990}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00560990}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 608 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364412. FT DOMAIN 336 608 Bac_surface_Ag. FT {ECO:0000259|Pfam:PF01103}. SQ SEQUENCE 608 AA; 66866 MW; 1521CB19FC2D95A8 CRC64; MIKPTALLLP ALFFFPHAYA PAADLSENKA AGFALFKSKS PDTESVKLKP KFPVRIDTQD SEIKDMVEEH LPLITQQQEE VLDKEQTGFL AEEAPDNVKT MLRSKGYFSS KVSLTEKDGA YTVHITPGPR TKIANVGVAI LGDILSDGNL AEYYRNALEN WQQPVGSDFD QDSWENSKTS VLGAVTRKGY PLAKLGNTRA AVNPDTATAD LNVVVDSGRP IAFGDFEITG TQRYPEQTVS GLARFQPGTP YDLDLLLDFQ QALEQNGHYS GASVQADFDR LQGDRVPVKV SVTEVKRHKL ETGIRLDSEY GLGGKIAYDY YNLFNKGYIG SVVWDMDKYE TTLAAGISQP RNYRGNYWTS NVSYNRSTTQ NLEKRAFSGG IWYVRDRAGI DARLGAEFLA EGRKIPGSDV DLGNSHATML TASWKRQLLN NVLHPENGHY LDGKIGTTLG TFLSSTALIR TSARAGYFFT PENKKLGTFI IRGQAGYTVA RDNADVPSGL MFRSGGASSV RGYELDSIGL AGPNGSVLPE RALLVGSLEY QLPFTRTLSG AVFHDMGDAA ANFKRMKLKH GSGLGVRWFS PLAPFSFDIA YGHSDKKIRW HISLGTRF // ID A0A0H4IST9_NEIG1 Unreviewed; 59 AA. AC A0A0H4IST9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63674.1}; GN ORFNames=NGO_05060 {ECO:0000313|EMBL:AKO63674.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63674.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63674.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63674; AKO63674; NGO_05060. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 7134 MW; 40C5F59EB8F9B270 CRC64; MNGKCRLKTA RPAFLRRRAT AVCRDKKVQA AVFTVKWRII LQRRQFRRFL IRTVYGFSF // ID A0A0H4J5E3_NEIG1 Unreviewed; 93 AA. AC A0A0H4J5E3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63622.1}; GN ORFNames=NGO_02605 {ECO:0000313|EMBL:AKO63622.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63622.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63622.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63622; AKO63622; NGO_02605. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 93 AA; 9889 MW; C10401CAFD25561E CRC64; MAEEMRTCKA CGGTKPLEKG FNAVPRKEGG VYYYKSCKTC RNKAVRQKRA EKRAAAGAGA MTAARLHGYI RAAHAACPIL GAGLWTQPAG ECA // ID A0A0H4IVJ1_NEIG1 Unreviewed; 104 AA. AC A0A0H4IVJ1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63765.1}; GN ORFNames=NGO_09270 {ECO:0000313|EMBL:AKO63765.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63765.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63765.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63765; AKO63765; NGO_09270. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 104 AA; 11958 MW; A573E4EB8108C441 CRC64; MGRVVMVEAK IFILYGAANK GKSTTLNTLF NQICRKFSKF LVFFERYGNG LDFVAVFDHE GQRIGFYSSG DNEYEVRRNL YKLYSHNCDF ILARQGHGVV VAMQ // ID A0A0H4IW93_NEIG1 Unreviewed; 472 AA. AC A0A0H4IW93; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Sulfatase {ECO:0000313|EMBL:AKO63703.1}; GN ORFNames=NGO_06735 {ECO:0000313|EMBL:AKO63703.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63703.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63703.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63703; AKO63703; NGO_06735. DR Proteomes; UP000000535; 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; IPR012549; DUF1705. DR InterPro; IPR000917; Sulfatase_N. DR Pfam; PF08019; DUF1705; 1. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 102 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 2 133 DUF1705. {ECO:0000259|Pfam:PF08019}. FT DOMAIN 161 452 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 472 AA; 53284 MW; 2B01F23853A61E10 CRC64; MHKVLIPLIL VISAAVSYQE IFFNIYFNKS MLNNVLQTTA AESARLITPG YVLWIVCLGV LPALAYIAVK VKYRVWYKEL LTRLVLAAVS FLCALGIAML QYQDYASFFR NNKSVTHLIV PSNFIGAGVS KYKDWKRSNI PYTQLDMAVV QNRPAGSLRR FVVLVVGETT RAANWGLNGY SRQTTPLLAA RGDEIVNFPQ VRSCGTSTAH SLPCMFSTFD RTDYDEIKAE HQDNLLDIVQ RAGVEVTWLE NDSGCKGVCG KVPNTDVTSL NLPEYCRNGE CLDNILLTKF DEALNKNDKD AVLILHTIGS HGPTYYERYT EAERKFTPTC DTNEIDKCAR ATLVNTYDNT VLYVDQFIDK VIRKLENRDD LESAVYYVSD HGESLGENGM YLHAAPYAIA PSGQTHIPMV MWFSKAFRQH GGIDFQCLKQ KAAENEYSHD HYFSTVLGLM DISNSQTYRK EMDILAACRR PR // ID A0A0H4J5Y2_NEIG1 Unreviewed; 209 AA. AC A0A0H4J5Y2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63777.1}; GN ORFNames=NGO_09870 {ECO:0000313|EMBL:AKO63777.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63777.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63777.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63777; AKO63777; NGO_09870. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 61 193 Lipoprot_C. {ECO:0000259|Pfam:PF08794}. SQ SEQUENCE 209 AA; 23328 MW; 70D4DD974DA552A3 CRC64; MSEQKIEFYG ADKEQNYALL KTWVYEQPYS VVRGYFGYSR KDGNPIEGDG QNPEEIPFDL YLGDIRGVAT DEDKLPKAGS FQYEGRAFGG NGVLSKESLD NHNGVFRYTI DFDRRKGSGS IEGMEQYGKI KLEEAAIERI PYRESGSSLG LKDRVSYFGV NEGVAMLEKD NEIKKYHLGI FGEAANEVAG AVSQEHKHQA VIGFGGEKK // ID Q5F4Y1_NEIG1 Unreviewed; 161 AA. AC Q5F4Y1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 50. DE RecName: Full=UPF0225 protein NGO_2162 {ECO:0000256|HAMAP-Rule:MF_00612}; GN ORFNames=NGO_2162 {ECO:0000313|EMBL:AAW90756.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90756.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0225 family. {ECO:0000256|HAMAP- CC Rule:MF_00612, ECO:0000256|SAAS:SAAS00537632}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90756.1; -; Genomic_DNA. DR RefSeq; WP_003692441.1; NC_002946.2. DR RefSeq; YP_209168.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y1; -. DR EnsemblBacteria; AAW90756; AAW90756; NGO_2162. DR GeneID; 3282762; -. DR KEGG; ngo:NGO2162; -. DR PATRIC; 20338178; VBINeiGon24812_2611. DR HOGENOM; HOG000252587; -. DR KO; K09858; -. DR OMA; CCGHYHA; -. DR OrthoDB; EOG6WMJ4X; -. DR BioCyc; NGON242231:GI2G-2050-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.10.450.50; -; 1. DR HAMAP; MF_00612; UPF0225; 1. DR InterPro; IPR032710; NTF2-like_dom. DR InterPro; IPR004027; SEC_C_motif. DR InterPro; IPR023006; UPF0225. DR Pfam; PF02810; SEC-C; 1. DR SUPFAM; SSF54427; SSF54427; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 161 AA; 18035 MW; ACFB74F0A12B5877 CRC64; MNTHHHPPCP CGSGTSYAGC CRPLHLRQIL PPTAEALIRS RYGAYVLHLI DYIIATTVPA QQTFLDAAEL MQWSREAEWL GLNVIAHRNL GKQHAQVEFE AYFQDGGNRT VHHELSAFVK IAEQWYFIDP TVPLPTMKQP CICGSGKKFK ACCGKYLQPV A // ID Q5FAH6_NEIG1 Unreviewed; 453 AA. AC Q5FAH6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:AAW88811.1}; DE EC=6.4.1.2 {ECO:0000313|EMBL:AAW88811.1}; GN ORFNames=NGO_0044 {ECO:0000313|EMBL:AAW88811.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88811.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88811.1; -; Genomic_DNA. DR RefSeq; WP_003704972.1; NC_002946.2. DR RefSeq; YP_207223.1; NC_002946.2. DR ProteinModelPortal; Q5FAH6; -. DR SMR; Q5FAH6; 1-444. DR PRIDE; Q5FAH6; -. DR EnsemblBacteria; AAW88811; AAW88811; NGO_0044. DR GeneID; 3282361; -. DR KEGG; ngo:NGO0044; -. DR PATRIC; 20332928; VBINeiGon24812_0049. DR HOGENOM; HOG000008988; -. DR KO; K01961; -. DR OMA; EDPYKFI; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; NGON242231:GI2G-39-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro. 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:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW88811.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 49643 MW; 2EEA0D15ADC8263E CRC64; MLKKVLIANR GEIALRVLRA CREMGIATVA VHSETDKGSL HVKLADESVC IGPAASAQSY LNIPAIIAAA EVTCADAVHP GYGFLAENAD FAEQVEQSGF TFIGPKPDTI RLMGDKVSAK HAMIAAGVPC VPGSDGALPD DDAEILKIAD KVGYPVIIKA SGGGGGRGMR VVEKKEDLLQ SVEMTKAEAG AAFGNPMVYM ERYLQRPRHV EIQVLADEHG NAVYLAERDC SLQRRHQKVI EEAPAPFIDE KARKKIGKAC TDACKRIGYR GAGTFEFLYE DGEFFFIEMN TRVQVEHPVT ELITGVDIVQ EQLRIASGLP LQYKQKDIKI EGHAFECRIN AEDPYNFIPS PGPIESCHLP GGFGIRVDSH IYQGYRIPPY YDSLIGKICV HGKTREQAMA KMRVALAELA VTGIKTNTPL HRDLFADAGF QEGGVSIHYL EHWLEARKTK QDK // ID A0A0H4IW20_NEIG1 Unreviewed; 103 AA. AC A0A0H4IW20; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63628.1}; GN ORFNames=NGO_02955 {ECO:0000313|EMBL:AKO63628.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63628.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63628.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63628; AKO63628; NGO_02955. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 103 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206212. SQ SEQUENCE 103 AA; 10991 MW; E0E43E73DD8D3FFF CRC64; MNKKLALMPL LILSAFSSAA DNTPQHGELG QVHVRADAKR VKAAHSYSIA SDGDLRDRVN LGVLGKANAF TAPITVVNYD EQAFNNTEAR TLVDAVAKKD ASV // ID Q5F8N1_NEIG1 Unreviewed; 671 AA. AC Q5F8N1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. 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 ORFNames=NGO_0739 {ECO:0000313|EMBL:AAW89456.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89456.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89456.1; -; Genomic_DNA. DR RefSeq; WP_003706226.1; NC_002946.2. DR RefSeq; YP_207868.1; NC_002946.2. DR ProteinModelPortal; Q5F8N1; -. DR EnsemblBacteria; AAW89456; AAW89456; NGO_0739. DR GeneID; 3281848; -. DR KEGG; ngo:NGO0739; -. DR PATRIC; 20334616; VBINeiGon24812_0880. DR HOGENOM; HOG000033015; -. DR KO; K03656; -. DR OMA; EKVLMQN; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; NGON242231:GI2G-696-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89456.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:AAW89456.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAW89456.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01920, KW ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAW89456.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 75751 MW; F6D2DED44DE705A8 CRC64; MMKLNAQQLE AVRYLGGPLF VLAGAGSGKT GVITQKIKHL IVNVGYLPHT VAAITFTNKA AAEMQERVAK MLPKPQTRGL TICTFHSLGM KILREEANHI GYKKNFSILD STDSAKIIGE LLGGTGKEAV FKAQHQISLW KNDLKTPEDV VQTASNVREQ QTARVYASYQ ETLQSYQAVD FDDLIRLPAV LLQQNSEVRN KWQRRLRYLL VDECQDTNTC QFALMKLLTG AEGMFTAVGD DDQSIYAWRG ANMENLRKMQ ENYPQMKVIK LEQNYRSTAR ILKIANKVIE NNPKLFTKKL WSQLGEGEPV KVVACQNEQH EADWVVSQIV KQKLIGGDKT RYADFAVLYR GKHQARIFEE ALRGARIPYR LSGGQSFFDK AEIKDVLSYV RLLANPNDDP AFLRAVTTPK RGIGDVTLGK LNAYAHEHEC SLYEAAQNEE ALATLNNTNR QHLQAFMDMF GNYRAKAEID EAGEFINSLL EEIDYENHLM QNEEGKAGEI KWRNVGELVS WFARKGERDG KNVIELAQTV ALMTLLEGKD EEETDAVSLS TLHAAKGLEY PYVFLVGCEE GVLPHNDSIE EGNVEEERRL MYVGITRAKR QLTLTHCVKR KKQGIWQFPE PSRFIDEMPQ EDLKILGRKG GEPIVSKEEG RRNLADIIGR IDNLKKSGPA D // ID A0A0H4ISN3_NEIG1 Unreviewed; 127 AA. AC A0A0H4ISN3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AKO63629.1}; GN ORFNames=NGO_02960 {ECO:0000313|EMBL:AKO63629.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63629.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63629.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63629; AKO63629; NGO_02960. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Receptor {ECO:0000313|EMBL:AKO63629.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 127 AA; 14502 MW; 25E0135C8738E34B CRC64; MARFGNNRAQ GTFDLGQRFG ENKAFGVRAN GKLRHGDTPR HGYREDNKEF ALNADYRGEK LRVTFDSIYA KRKINGGRAR MQDIQNAGGR LFDAPDGKIN LLPSWNWQNT VGETNMLTFE WDAFDNT // ID Q5FAI7_NEIG1 Unreviewed; 146 AA. AC Q5FAI7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AAW88800.1}; GN ORFNames=NGO_0031 {ECO:0000313|EMBL:AAW88800.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88800.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88800.1; -; Genomic_DNA. DR RefSeq; WP_003700855.1; NC_002946.2. DR RefSeq; YP_207212.1; NC_002946.2. DR ProteinModelPortal; Q5FAI7; -. DR EnsemblBacteria; AAW88800; AAW88800; NGO_0031. DR GeneID; 3281862; -. DR KEGG; ngo:NGO0031; -. DR PATRIC; 20332892; VBINeiGon24812_0031. DR HOGENOM; HOG000078523; -. DR KO; K03789; -. DR OMA; LEYWYAH; -. DR OrthoDB; EOG6NKR5W; -. DR BioCyc; NGON242231:GI2G-28-MONOMER; -. DR Proteomes; UP000000535; 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; PF00583; Acetyltransf_1; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88800.1}. FT DOMAIN 1 146 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 146 AA; 16069 MW; FB4FBE4A7C6A1E1E CRC64; MNIRPASPSD CAALAALDTV CNPSAWTQRQ FESALVSPSE QVFLAEKDGR IAAFIVWQNL PDESELHLIA TAPECRRRGV ASALLEYWYA HLPEGTQRLL LEVRAGNAAA QALYTKHGFS IAGRRKNYYC AADGQTEDAV LMEKIC // ID A0A0H4IS47_NEIG1 Unreviewed; 163 AA. AC A0A0H4IS47; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63731.1}; GN ORFNames=NGO_07820 {ECO:0000313|EMBL:AKO63731.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63731.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63731.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63731; AKO63731; NGO_07820. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 163 AA; 18139 MW; 7E6A0CAD63527954 CRC64; MRSRVRKHRS ANPKVSAIRR GSRPEAMIRT GSIRLGQSVS DGTQLDWSWN ESAETASAAV SAQEVDPLTE YQVYKQFGYQ GKAAESLAAY LDGIPDGEAK PENLIRELID INLEVGDVDV LADNLQKYGR LIPFELLAKY IEQALQRDSN HLRIRVLAEE GLG // ID A0A0H4J5L1_NEIG1 Unreviewed; 44 AA. AC A0A0H4J5L1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63682.1}; GN ORFNames=NGO_05505 {ECO:0000313|EMBL:AKO63682.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63682.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63682.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63682; AKO63682; NGO_05505. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 44 AA; 5080 MW; E68D1B69D904BA4E CRC64; MPSEGFRRHR RPISADYPSI AFFSLNSTSP FPKIFPHPFQ NTLS // ID A0A0H4IVN5_NEIG1 Unreviewed; 45 AA. AC A0A0H4IVN5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Beta-hexosaminidase {ECO:0000313|EMBL:AKO63820.1}; GN ORFNames=NGO_11540 {ECO:0000313|EMBL:AKO63820.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63820.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63820.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63820; AKO63820; NGO_11540. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 5112 MW; 51857FA6AC8B00E6 CRC64; MPIIKRRTII RLSHKTACNG KPAIIVKKQK SDKHGYKLSA TPNIR // ID Q5F505_NEIG1 Unreviewed; 616 AA. AC Q5F505; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Lytic murein transglycosylase {ECO:0000313|EMBL:AAW90732.1}; GN ORFNames=NGO_2135 {ECO:0000313|EMBL:AAW90732.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90732.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90732.1; -; Genomic_DNA. DR RefSeq; WP_010951413.1; NC_002946.2. DR RefSeq; YP_209144.1; NC_002946.2. DR ProteinModelPortal; Q5F505; -. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR EnsemblBacteria; AAW90732; AAW90732; NGO_2135. DR GeneID; 3282786; -. DR KEGG; ngo:NGO2135; -. DR PATRIC; 20338119; VBINeiGon24812_2582. DR HOGENOM; HOG000265691; -. DR KO; K08309; -. DR OMA; YFRIKPQ; -. DR OrthoDB; EOG6S52QZ; -. DR BioCyc; NGON242231:GI2G-2026-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256561. FT DOMAIN 461 564 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 616 AA; 67531 MW; 7DC5A974909DBD4D CRC64; MYLPSMKHSL PLLAALVLAA CSSTNTLPAG KTPADNIETA DLSASVPTRP AEPEGKTLAD YGGYPSALDA VKQNNDAAAA AYLENAGDSA MAENVRKEWL MYYGVRSQWT LFAQEYAKLK PEGGAQEVEC YADSSRNDYT RAAELVKNTG KLPSGCTKLL EQATASGLLG GNDAWRGVRG LLAGRPTTDG RNLAAALGSP FDGGTQGSRE YALLNVIGKE ARKSPNAAAL LSEMESGLSP EQRSFAWGVL GHYQSQSLNV PAALDYYGKV ADRRQLTDDQ IEWYARAALR ARRWDELASV ISHMPEKLQK SPTWLYWLAR SRAATGNTQE AEKLYKQAAA TGRNFYAVLA GEELGRKIDT RNNVPDAGKN SVLRMAEDGA IKRALVLFRN SRTAGDAKMR RQAQAEWRFA TRGFDEDKLL TAAQTAFDHG FYDMAVNSAE RTDRKLNYTL RYISPFKDTV IRHAQNVNVD PAWVYGLIRQ ESRFVIGAQS RVGAQGLMQV MPATAREIAG KIGMDAAQLY TADGNIRMGT WYMADTKRRL QNNEILATAG YNAGPGRARR WQADTPLEGA VYAETIPFSE TRDYVKKVMT NAAYYASLFG APHIPLKQRM GTVPAR // ID A0A0H4IW08_NEIG1 Unreviewed; 158 AA. AC A0A0H4IW08; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE RecName: Full=UPF0114 protein NGO_01540 {ECO:0000256|HAMAP-Rule:MF_00143}; GN ORFNames=NGO_01540 {ECO:0000313|EMBL:AKO63613.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63613.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00143, ECO:0000256|SAAS:SAAS00020503}; Multi-pass membrane CC protein {ECO:0000256|HAMAP-Rule:MF_00143, CC ECO:0000256|SAAS:SAAS00020503}. CC -!- SIMILARITY: Belongs to the UPF0114 family. {ECO:0000256|HAMAP- CC Rule:MF_00143, ECO:0000256|SAAS:SAAS00542909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AKO63613.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63613; AKO63613; NGO_01540. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR HAMAP; MF_00143; UPF0114; 1. DR InterPro; IPR005134; UPF0114. DR InterPro; IPR020761; UPF0114_bac. DR InterPro; IPR020765; UPF0114_gbac. DR Pfam; PF03350; UPF0114; 1. DR TIGRFAMs; TIGR00645; HI0507; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00143, KW ECO:0000256|SAAS:SAAS00426128}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00143, KW ECO:0000256|SAAS:SAAS00426128, ECO:0000256|SAAS:SAAS00426138}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00143, KW ECO:0000256|SAAS:SAAS00426138}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00143, KW ECO:0000256|SAAS:SAAS00426138}. FT TRANSMEM 26 46 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00143}. FT TRANSMEM 76 96 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00143}. SQ SEQUENCE 158 AA; 17643 MW; 6F6333DB8A70E479 CRC64; MESRAFVAAR KGNVSSKISK TRTGYGFFAK MIFASRWLQV PIYAGLTVVR AICAYKFLKS LKHLVMNLDV SDENAIMLAV LNLIDVVMIA NLLTMVQIGG YESFVSRLRI DDHPDRPEWL SHVNAPVLKV RLSMSIIGIH PSICSKHLSI PPICRKSS // ID A0A0H4IWJ8_NEIG1 Unreviewed; 95 AA. AC A0A0H4IWJ8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63813.1}; GN ORFNames=NGO_11150 {ECO:0000313|EMBL:AKO63813.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63813.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63813.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63813; AKO63813; NGO_11150. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 95 AA; 10188 MW; BC1B88EEB3382250 CRC64; MASPADKIKG KYVQKVEVAK GVVTAEMKPS GVNKEIKGKK LSLWAKREDG SVKWFCGQPV KRDAGAKADD VKADAANAIE TKHLPSTCRD ESSAT // ID A0A0H4J5W6_NEIG1 Unreviewed; 82 AA. AC A0A0H4J5W6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63757.1}; GN ORFNames=NGO_08685 {ECO:0000313|EMBL:AKO63757.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63757.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63757.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63757; AKO63757; NGO_08685. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 8971 MW; 1AA6F794D49222CC CRC64; MRETCFFCKY ADFKTQPDTP VHAFAKCAKA RNAEERAKHY PRTNPCAAGA FQTASGAAVA KRTAVLGEYP PPQCAEFERE GG // ID A0A0H4IW41_NEIG1 Unreviewed; 187 AA. AC A0A0H4IW41; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63648.1}; GN ORFNames=NGO_03840 {ECO:0000313|EMBL:AKO63648.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63648.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63648.1; -; Genomic_DNA. DR RefSeq; WP_003695326.1; NC_002946.2. DR RefSeq; YP_009115482.1; NC_002946.2. DR EnsemblBacteria; AKO63648; AKO63648; NGO_03840. DR GeneID; 22847890; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006521; Tail_protein_I. DR Pfam; PF09684; Tail_P2_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 187 AA; 21228 MW; 159D4113120D2818 CRC64; MNSTVPANNS PLQHALAKLT ERETAAVSRQ LDPARCDPGF LPFHAFARSI GTEEGWDFAE TDEARRNLIA GFAEIHARKG TPYAIRALFP ILRLGEIQII ERDGEFKWDG SVLFDGSRTF GRREGDWAEY RIVLTRPVSI RQTARIRAML AEIAPLRCEL TALDYRNHPH RWNGKIRFNG EYGFGTT // ID A0A0H4J626_NEIG1 Unreviewed; 235 AA. AC A0A0H4J626; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:AKO63822.1}; GN ORFNames=NGO_11610 {ECO:0000313|EMBL:AKO63822.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63822.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63822.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63822; AKO63822; NGO_11610. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63822.1}. SQ SEQUENCE 235 AA; 27855 MW; B0412A9BD91AC47F CRC64; MEKDRSIIAM GAWLEILSEE KDGNRLARHH KHGKIWKKPT RHEDIAAFFP FGNPIHNNTM IMRRSVIDGG LRYNTGRDWA EDYQFWYDVS KLGRLAYYPE ALVKYRLHAN QVSSKHSVRQ HEIAQGIQKT ARNDFLQSMG FKTRFDSLEY RQTKAAAYEL PEKDLPEEDF ERARRFLYRC FKRTDTPPSG AWLDFAADGR MRRLFTLRQY FGILYRLIKN RRQARSDSAG KEQEI // ID A0A0H4IRY1_NEIG1 Unreviewed; 86 AA. AC A0A0H4IRY1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63681.1}; GN ORFNames=NGO_05425 {ECO:0000313|EMBL:AKO63681.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63681.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63681.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63681; AKO63681; NGO_05425. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 5 44 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 86 AA; 10586 MW; 8CC87178C6FD2075 CRC64; MSSLAACAAE EKRREEKRRE EKRREEKRRE EKRREEKRRE EKRRFFAGWI HFRLLIRFNR LKKRFSLMLK GGLYRVPGGV STQYGG // ID Q5F538_NEIG1 Unreviewed; 406 AA. AC Q5F538; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}; DE Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120}; DE Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120}; DE EC=4.1.1.20 {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}; GN Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120}; GN ORFNames=NGO_2098 {ECO:0000313|EMBL:AAW90699.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90699.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso- CC diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP- CC Rule:MF_02120}. CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine + CC CO(2). {ECO:0000256|HAMAP-Rule:MF_02120, CC ECO:0000256|RuleBase:RU003738}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02120, CC ECO:0000256|RuleBase:RU003738}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_02120, ECO:0000256|RuleBase:RU003738}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. LysA subfamily. {ECO:0000256|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; AE004969; AAW90699.1; -; Genomic_DNA. DR RefSeq; WP_003690402.1; NC_002946.2. DR RefSeq; YP_209111.1; NC_002946.2. DR ProteinModelPortal; Q5F538; -. DR EnsemblBacteria; AAW90699; AAW90699; NGO_2098. DR GeneID; 3282819; -. DR KEGG; ngo:NGO2098; -. DR PATRIC; 20338033; VBINeiGon24812_2539. DR HOGENOM; HOG000045070; -. DR KO; K01586; -. DR OMA; LKGNKFG; -. DR OrthoDB; EOG6Z9B18; -. DR BioCyc; NGON242231:GI2G-1993-MONOMER; -. DR UniPathway; UPA00034; UER00027. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_02120, KW ECO:0000256|RuleBase:RU003738}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120, KW ECO:0000256|RuleBase:RU003738}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_02120, KW ECO:0000256|RuleBase:RU003738}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02120, KW ECO:0000256|RuleBase:RU003738}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02120, KW ECO:0000256|SAAS:SAAS00418093}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 45 272 Orn_Arg_deC_N. FT {ECO:0000259|Pfam:PF02784}. FT DOMAIN 277 380 Orn_DAP_Arg_deC. FT {ECO:0000259|Pfam:PF00278}. FT REGION 265 268 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_02120}. FT BINDING 231 231 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_02120}. FT BINDING 268 268 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT BINDING 304 304 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT BINDING 308 308 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT BINDING 335 335 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT BINDING 362 362 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT BINDING 362 362 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_02120}. FT MOD_RES 52 52 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_02120}. SQ SEQUENCE 406 AA; 43649 MW; BE7CE06EF9FACF3E CRC64; MTLFCEQVPY PRLAEEFGTP LYVYSQSALT GAFENYQTAF AALNPLVCYA VKANGNLSII KHFASLGSGF DIVSGGELAR VLAAGGDAAK TIFSGVGKSE AEIEFALNAG VKCFNMESIP EIDRIQKIAA RLGKTAPVSL RVNPDVDAKT HPYISTGLKA NKFGIAYADA LEAYRHAAQQ PNLKIIGIDC HIGSQLTDLS PLVEACERIL ILVDALAAEG IVLEHLDLGG GVGIVYKDEG VPDLGAYARA VQKLMGTRRL KLILEPGRSL VGNAGALLTR VEFVKHGEEK NFVMVDAAMN DLMRPALYDA YHHIEAVETK NIEPLTANIV GPICETGDFL GKDRTIACEE GDLLLIRSAG AYGASMASNY NTRNRAAEVL VDGGGYKLIR RRETLEQQMA NELACL // ID Q5F734_NEIG1 Unreviewed; 354 AA. AC Q5F734; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Alpha 1,2 N-acetylglucosamine transferase {ECO:0000313|EMBL:AAW90003.1}; GN ORFNames=NGO_1354 {ECO:0000313|EMBL:AAW90003.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90003.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90003.1; -; Genomic_DNA. DR RefSeq; WP_003691706.1; NC_002946.2. DR RefSeq; YP_208415.1; NC_002946.2. DR ProteinModelPortal; Q5F734; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW90003; AAW90003; NGO_1354. DR GeneID; 3282072; -. DR KEGG; ngo:NGO1354; -. DR PATRIC; 20336089; VBINeiGon24812_1593. DR HOGENOM; HOG000219076; -. DR OMA; DCTMFTA; -. DR OrthoDB; EOG68DD0W; -. DR BioCyc; NGON242231:GI2G-1268-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90003.1}. 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; 39943 MW; C0BC40D2A41D7C7E CRC64; MEKEFRILNI VSAKIWGGGE QYVYDVSKAL GLRGCTMFTA VNKNDELMRR RFSEVSSVFT TRLHTFNGLF SLYALTRFIR ENHISHLMIH TGKIAALSVL LKKLTGVRLI FVKHNVVANK TDFYHRLIQK NTDRFICVSR LVYDVQTADN PFKEKYRIVH NGIDTGRFPP SQEKPDSRFF TVAYAGRISP EKGLENLIEA CVILHRKYPQ IRLKLAGHGH PDYMCRLKRG VSASGAEPFV SFEGFTEKLA SFYRQSDVVV LPSLVPEAFG LSLCEAMYCR TAVISNTLGA QKEIIEHHQS GILLDRLTPE SLADEIERLV LNPEAKNALA TAGHQCVAAR FTINHTADKL LDAI // ID Q5F8A7_NEIG1 Unreviewed; 201 AA. AC Q5F8A7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=DNA mismatch repair protein MutS {ECO:0000313|EMBL:AAW89580.1}; GN ORFNames=NGO_0880 {ECO:0000313|EMBL:AAW89580.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89580.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89580.1; -; Genomic_DNA. DR RefSeq; WP_003698367.1; NC_002946.2. DR RefSeq; YP_207992.1; NC_002946.2. DR ProteinModelPortal; Q5F8A7; -. DR EnsemblBacteria; AAW89580; AAW89580; NGO_0880. DR GeneID; 3282161; -. DR KEGG; ngo:NGO0880; -. DR PATRIC; 20334935; VBINeiGon24812_1037. DR HOGENOM; HOG000257488; -. DR OMA; RCILIIH; -. DR OrthoDB; EOG6XDGX6; -. DR BioCyc; NGON242231:GI2G-822-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 116 194 Smr. {ECO:0000259|PROSITE:PS50828}. FT COILED 9 43 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 201 AA; 23074 MW; 1BC2ED8A9801E968 CRC64; MNTDFQKILK QLGKQAKKEA AEKQEAEKNK QKQEQDLDFS QAVGQVSPLK NRQQYYAQSD KTPIKARPKD NRTDEENYFY IGSTYNDPPA SFCKNGQGKN DIQRLKNGYY PVVTDVDLHG YTQEEAQKVL NEFIAFTQKR GVCGEIIHGS GLGSKGYKPV LKNMTRNWLM QHPDVLAYVE PREGNDGCVR ILLKRKLRQQ D // ID Q5F4Z9_NEIG1 Unreviewed; 286 AA. AC Q5F4Z9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Chromosome partitioning protein ParB {ECO:0000313|EMBL:AAW90738.1}; GN ORFNames=NGO_2141 {ECO:0000313|EMBL:AAW90738.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90738.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ParB family. CC {ECO:0000256|SAAS:SAAS00571585}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90738.1; -; Genomic_DNA. DR RefSeq; WP_003687145.1; NC_002946.2. DR RefSeq; YP_209150.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z9; -. DR EnsemblBacteria; AAW90738; AAW90738; NGO_2141. DR GeneID; 3282780; -. DR KEGG; ngo:NGO2141; -. DR PATRIC; 20338135; VBINeiGon24812_2590. DR HOGENOM; HOG000088074; -. DR KO; K03497; -. DR OMA; LIQRGKY; -. DR OrthoDB; EOG6Z3KMS; -. DR BioCyc; NGON242231:GI2G-2032-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 29 119 ParB. {ECO:0000259|SMART:SM00470}. SQ SEQUENCE 286 AA; 31532 MW; 503B2D8CB2CB3AE8 CRC64; MAKVKGGLGR GLDSLLANGA DNSSGDRLTA VAVKDIRPGR YQARVQIDDE ALQELADSIK AQGVIQPVIV REHGLSRYEL IAGERRWRAA QIAGLSEIPA VIKTISDETA LAMGLIENLQ RENLNPIEEA QGLKRLADEF GLTHETIAQA VGKSRSAISN SLRLLSLPES VQEMLYQRRL EMGHARALLT LPVVEQLELA QKAVKNGWSV REVERRSQAA LQNKRPEPKK TAAADIGRLN DLLTEKLGVN AEIKTANHKK GKIILHFDTP ETFDHILKQL GIDYRP // ID A0A0H4J5L9_NEIG1 Unreviewed; 135 AA. AC A0A0H4J5L9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63687.1}; GN ORFNames=NGO_05680 {ECO:0000313|EMBL:AKO63687.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63687.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63687.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63687; AKO63687; NGO_05680. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 135 AA; 15038 MW; 769D096BB89A2F28 CRC64; MCLKLVSPEA ADVCAPGWRD GAQTGLPVYA VQGDGKLTLA PAPDRDGRLF AGGYCLPRDM AGDGDEPEIN SIHHRNLVYW ALAEAFGIPD AETFDPQRSE SARRRFELYF GLPADSDLRR ITREDAPHLN RHFWI // ID A0A0H4ISU6_NEIG1 Unreviewed; 78 AA. AC A0A0H4ISU6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63679.1}; GN ORFNames=NGO_05410 {ECO:0000313|EMBL:AKO63679.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63679.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63679.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63679; AKO63679; NGO_05410. DR Proteomes; UP000000535; 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 Pfam; PF01609; DDE_Tnp_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 65 DDE_Tnp_1. {ECO:0000259|Pfam:PF01609}. SQ SEQUENCE 78 AA; 8996 MW; B3FB902FD7DEED11 CRC64; MRKARRNRPL TEAQTKRNRY LSKTRYVVEQ SFGTLHRKFR YARAAYFGLI KVSAQSHLKA MCLNLLKAAN RLSVPAAA // ID Q5F7F4_NEIG1 Unreviewed; 208 AA. AC Q5F7F4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. 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 ORFNames=NGO_1224 {ECO:0000313|EMBL:AAW89883.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89883.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89883.1; -; Genomic_DNA. DR RefSeq; WP_003700925.1; NC_002946.2. DR RefSeq; YP_208295.1; NC_002946.2. DR ProteinModelPortal; Q5F7F4; -. DR EnsemblBacteria; AAW89883; AAW89883; NGO_1224. DR GeneID; 3281934; -. DR KEGG; ngo:NGO1224; -. DR PATRIC; 20335761; VBINeiGon24812_1439. DR HOGENOM; HOG000033575; -. DR KO; K11175; -. DR OMA; GDSEHGT; -. DR OrthoDB; EOG615VP4; -. DR BioCyc; NGON242231:GI2G-1135-MONOMER; -. DR UniPathway; UPA00074; UER00126. DR Proteomes; UP000000535; 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:UP000000535}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01930}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01930, KW ECO:0000256|SAAS:SAAS00476799, ECO:0000313|EMBL:AAW89883.1}. 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; 22372 MW; EA9DA1F1B252BCC1 CRC64; MKNIVILISG RGSNMQAIVN AAIPNVRIAA VLSNSETAAG LQWAAERGIP TDSLNHKNFE SRLAFDTAMM EKIDAYQPDL VVLAGFMRIL TPEFCAHYEG RLMNIHPSIL PSFTGLHTHE RALEAGCRVA GCTIHFVTAE LDCGPIVSQG IVPILDGDTA DDVAARVLAV EHKLYPKAVA DVAAGRLIIE GNRVRNSENA DAARFLTA // ID Q5F8K7_NEIG1 Unreviewed; 124 AA. AC Q5F8K7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Arsenate reductase {ECO:0000313|EMBL:AAW89480.1}; GN ORFNames=NGO_0765 {ECO:0000313|EMBL:AAW89480.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89480.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89480.1; -; Genomic_DNA. DR RefSeq; WP_003688664.1; NC_002946.2. DR RefSeq; YP_207892.1; NC_002946.2. DR ProteinModelPortal; Q5F8K7; -. DR EnsemblBacteria; AAW89480; AAW89480; NGO_0765. DR GeneID; 3282343; -. DR KEGG; ngo:NGO0765; -. DR PATRIC; 20334680; VBINeiGon24812_0912. DR HOGENOM; HOG000059714; -. DR OMA; FGIKNCD; -. DR OrthoDB; EOG6NSGMX; -. DR BioCyc; NGON242231:GI2G-720-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 124 AA; 13990 MW; E7B582D0F755DD5B CRC64; MIILHGIPNC DTVKKAKNRL AGYGLEFGFR DFKKQMPSEA EICSWLEQVP LATLFNKRGT SWRKLDAETQ QKALSSTAEA VKLMSEMPSL IKRPVLECGS RVYVGFSEET YDGIFNRQAP CRQG // ID A0A0H4IT86_NEIG1 Unreviewed; 185 AA. AC A0A0H4IT86; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000313|EMBL:AKO63784.1}; GN ORFNames=NGO_10165 {ECO:0000313|EMBL:AKO63784.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63784.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63784.1; -; Genomic_DNA. DR RefSeq; WP_003690256.1; NC_002946.2. DR RefSeq; YP_009115485.1; NC_002946.2. DR EnsemblBacteria; AKO63784; AKO63784; NGO_10165. DR GeneID; 22847893; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 185 AA; 20798 MW; B62D402F10B10574 CRC64; MDIIDTALPD VKLLKPQVFT DGRGFFMETF RDGWFKENIA DRTFVQENHS NSSKGVLRGL HYQTENTQGK LVRIVVGEVF DVAVDMREGS PTFGKWAGAT LSAQNRYQLW IPEGFAHGFC VLGDAAEVVY KCTDYYNPET EQVLIWNDPA IGIGWPLQTA PLLSPKDLAG KTWAQAEKLR LTLSR // ID A0A0H4IW57_NEIG1 Unreviewed; 333 AA. AC A0A0H4IW57; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Sulfate-binding protein {ECO:0000313|EMBL:AKO63663.1}; GN ORFNames=NGO_04615 {ECO:0000313|EMBL:AKO63663.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63663.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63663.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63663; AKO63663; NGO_04615. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 333 AA; 37996 MW; 6E00C67B179783C8 CRC64; MQPRSRFKPS VRTKCPGQYR IRRKKHYPAQ CLIRCDTVFL QRIQPLIYQN IPIRTPRHIR QHPTIPRRLQ QTGIIRSQRP SSRCRNHEPI FRHRPARKKG LVEKGWQQAL PDHAAPYTST MVFLVRKNNP KQIRDWNDLA KDGVNIVIAK TSGNGRYAFL GAYGYGLKAN NGNEQEAQKL VASILKNTPV FENGGRAAAT TFTQRNIGDV LITFENEANY VSKKLTQGQF EIVYPSYTIS AESPVAVVNS VVAKKGTQKT ARAYLEYLWS EPAQELAASL YLRPRNPEVL ARHKADFPDL DTFPPEEKFG GWDNIMKTYF ADGGVFDRLT AQK // ID Q5F7D1_NEIG1 Unreviewed; 187 AA. AC Q5F7D1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000313|EMBL:AAW89906.1}; GN ORFNames=NGO_1247 {ECO:0000313|EMBL:AAW89906.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89906.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89906.1; -; Genomic_DNA. DR RefSeq; WP_003697959.1; NC_002946.2. DR RefSeq; YP_208318.1; NC_002946.2. DR EnsemblBacteria; AAW89906; AAW89906; NGO_1247. DR GeneID; 3282598; -. DR KEGG; ngo:NGO1247; -. DR PATRIC; 20335823; VBINeiGon24812_1466. DR HOGENOM; HOG000010898; -. DR KO; K00995; -. DR OMA; VQMVAIP; -. DR OrthoDB; EOG6WMJ3D; -. DR BioCyc; NGON242231:GI2G-1164-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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:UP000000535}; 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:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003750, KW ECO:0000256|SAAS:SAAS00461509, ECO:0000313|EMBL:AAW89906.1}; 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 152 179 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 187 AA; 21277 MW; A9C25B93F6492F7C CRC64; MPWNIPIFLT WLRVLLIPVL IVLFYLPFSW FSEEAVNVAA AVIFAVAALT DWFDGFLARL WKQTSDFGAF LDPVADKLMV AVSLLLLVKL DRTYVLFAMI IIGREITISA LREWMAQMGK RSSVAVATVG KFKTAAQMLA IFFLLLNFPD FYGFNLVVIG NILMFIASLL TVWSMLYYLK MAWKEIA // ID A0A0H4J5E9_NEIG1 Unreviewed; 508 AA. AC A0A0H4J5E9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AKO63627.1}; GN ORFNames=NGO_02845 {ECO:0000313|EMBL:AKO63627.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63627.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63627.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63627; AKO63627; NGO_02845. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AKO63627.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63627.1}. FT DOMAIN 46 153 Methyltranfer_dom. FT {ECO:0000259|Pfam:PF13847}. FT DOMAIN 219 302 MethyTransf_Reg. FT {ECO:0000259|Pfam:PF10119}. SQ SEQUENCE 508 AA; 57165 MW; E2B9985B51853DEF CRC64; MPGVSDIKNS YDDLMYESKA FSQTAINALE ACARMMGLKP TAAAKAKVLE LGCSMGRNII TQALYYPDAE FVGIDLSGRQ VAQGNAIIEK MGLENVRLEE KDILTVDESF GKFDYIIVHG IWSRVPDAVK DKIFSICRNN LTEYGIAYIS YNVYPGWKRQ EQLRDIMQFA GRDALGEPLE ARTRKGLDAI KALAEILEND KGLGGGKLPA IQKILNHNTY YVAHEYMEIF NDPIYVNGFI EWANRHRLAY IGDTDLHVSF VSWMAEHTRE RILALAGGDY IAKEFYSDIL SDRQFHRSLL CREEVGDTVR RDESVAVEVI ESLNFRPARG ETINFDENDT LLSGIRDVMK TGEAFKTEDV AENLARRFPG LEFDRMKINS QLLLQTILGR FSVSSDNAGK PFFEDHKTYV PARFTNYAAA FVEHGAGAFV RPANRYNEST PSFGYGHLYI MRQLSRPTSK QALIETVAEN LNIVSATPDG LTFHPPAEVY VEEILADLAD RHFLVSAD // ID A0A0H4IVA4_NEIG1 Unreviewed; 59 AA. AC A0A0H4IVA4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63705.1}; GN ORFNames=NGO_06800 {ECO:0000313|EMBL:AKO63705.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63705.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63705.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63705; AKO63705; NGO_06800. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6454 MW; E8EA21B89F7659DC CRC64; MYFFGHCADK SPFCPLSGFV HIGKTEIVRT CAGVDSSLAI SGYIQQNRHI GILIGVLRK // ID A0A0H4J5K6_NEIG1 Unreviewed; 81 AA. AC A0A0H4J5K6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63677.1}; GN ORFNames=NGO_05250 {ECO:0000313|EMBL:AKO63677.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63677.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63677.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63677; AKO63677; NGO_05250. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006482; Cas7_Csh2/Csh2. DR Pfam; PF05107; Cas_Cas7; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 81 AA; 9101 MW; 7D848B738C5AAFC1 CRC64; MVTDVCLKRK IRNFVEISSE NEAGYEIYVK EKSVLNLQNK RAYEALGIES EAKNCRRTKP KPVTLPRGCV KTSSISEPSA P // ID A0A0H4ISC3_NEIG1 Unreviewed; 48 AA. AC A0A0H4ISC3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AKO63816.1}; GN ORFNames=NGO_11170 {ECO:0000313|EMBL:AKO63816.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63816.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63816.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63816; AKO63816; NGO_11170. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5746 MW; 717AD3C74AA93183 CRC64; MPEQARARPI QTAMTLCRRF GAGWRHPRRP HRFISHRPSE TRPIRRAV // ID Q5F9P8_NEIG1 Unreviewed; 233 AA. AC Q5F9P8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; 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}; 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=mtnN {ECO:0000256|HAMAP-Rule:MF_01684}; GN ORFNames=NGO_0345 {ECO:0000313|EMBL:AAW89089.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89089.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89089.1; -; Genomic_DNA. DR RefSeq; WP_003687752.1; NC_002946.2. DR RefSeq; YP_207501.1; NC_002946.2. DR ProteinModelPortal; Q5F9P8; -. DR EnsemblBacteria; AAW89089; AAW89089; NGO_0345. DR GeneID; 3281177; -. DR KEGG; ngo:NGO0345; -. DR PATRIC; 20333687; VBINeiGon24812_0421. DR HOGENOM; HOG000259346; -. DR KO; K01243; -. DR OMA; LLERCKP; -. DR OrthoDB; EOG64JFVR; -. DR BioCyc; NGON242231:GI2G-324-MONOMER; -. DR UniPathway; UPA00904; UER00871. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01684, KW ECO:0000256|SAAS:SAAS00432671}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Glycosidase {ECO:0000313|EMBL:AAW89089.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89089.1}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01684, KW ECO:0000256|SAAS:SAAS00432671}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 24806 MW; AFBBD9C83675B0AF CRC64; MSLKTVAVIG AMEQEIELLR EMMENVKAVS FGRFSAYEGE LAGKRIVLAL SGIGKVNAAV ATAWLIRQFA PDCVINTGSA GGLGKGLKVG DVVIGTETEH HDVDVTAFGY ARGQVPQLPA RFASDGILIE TAKRAARTFE GAEVEQGLIV SGDRFVHSSE GVAEIRKHFP EVKAVEMEAA AIAQTCHQLE TPFVIIRAVS DSADEKADIS FEEFLKTAAA SSAKMVAEIV KSL // ID Q5F8G8_NEIG1 Unreviewed; 218 AA. AC Q5F8G8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 66. DE SubName: Full=Nickel-dependent hydrogenase b-type cytochrome subunit {ECO:0000313|EMBL:AAW89519.2}; GN ORFNames=NGO_0805 {ECO:0000313|EMBL:AAW89519.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89519.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89519.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8G8; -. DR EnsemblBacteria; AAW89519; AAW89519; NGO_0805. DR PATRIC; 20334764; VBINeiGon24812_0952. DR HOGENOM; HOG000271303; -. DR OMA; RWSRFAS; -. DR OrthoDB; EOG6WMHZQ; -. DR BioCyc; NGON242231:GI2G-761-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {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; 24043 MW; 580E80919C386EEB CRC64; MKNKTKVWDF PTRLFHWLLA ASLPFMWYSA KAGGDMLQWH TRVGLLVLFL LVFRLCWGIW GSDTARFSRF VRGWAGIRGY LKNGIPEHIQ PGHNPLGALM VVALLAAVSF QVGTGLFAAN ENTFSTNGYL NHLVSEHTGS LIRKIHLNFF KLLAVFSAVH IAAVAAYRIF KKKNLVRPMI TGFKYIEGKT SIRFAGKAAL AAALSVAALA AAAILLLS // ID Q5F707_NEIG1 Unreviewed; 737 AA. AC Q5F707; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AAW90030.1}; GN ORFNames=NGO_1382 {ECO:0000313|EMBL:AAW90030.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90030.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90030.1; -; Genomic_DNA. DR RefSeq; WP_003695653.1; NC_002946.2. DR RefSeq; YP_208442.1; NC_002946.2. DR ProteinModelPortal; Q5F707; -. DR DNASU; 3281790; -. DR EnsemblBacteria; AAW90030; AAW90030; NGO_1382. DR GeneID; 3281790; -. DR KEGG; ngo:NGO1382; -. DR PATRIC; 20336153; VBINeiGon24812_1625. DR HOGENOM; HOG000018300; -. DR KO; K00951; -. DR OMA; TEIGHNC; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; NGON242231:GI2G-1295-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. 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:UP000000535}; KW Kinase {ECO:0000313|EMBL:AAW90030.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90030.1}. FT DOMAIN 666 737 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 737 AA; 82397 MW; A78B8F9BD62F9F50 CRC64; MTAISPIQDT QSATLQELRE WFDSYCAALP DNDKNLIGTA WSLAQEHYPA DAATPYGEPL PDHFLGAAQM VDELDLLPDA VAATLLADIG RYVPDWNLLV SERCNSTVAE LVKGVDEVQK LTHFARVDSL ATPEERAQQA ETMRKMLLAM VTDIRVVLIK LAMRTRTLQF LSNAPDSPEK RAVAKETLDI FAPLANRLGV WQLKWQLEDL GFRHQEPEKY REIALLLDEK RTERLEYIEN FLDILRTELK KYNIHFEVAG RPKHIYSIYK KMVKKKLSFD GLFDIRAVRI LVDTVPECYT TLGIVHSLWQ PIPGEFDDYI ANPKGNGYKS LHTVIVGPED KGVEVQIRTF DMHQFNEFGV AAHWRYKEGG KGDSAYEQKI AWLRQLLDWR ENMAESGKED LAAAFKTELF NDTIYVLTPH GKVLSLPTGA TPIDFAYALH SSIGDRCRGA KVEGQIVPLS TPLENGQRVE IITAKEGHPS VNWLYEGWVK SGKAIGKIRA YIRQQNADTV REEGRVQLDK QLAKLTPKPN LQELAENLGY KKPEDLYTAV GQGEISNRAI QKACGTLNEP PPVPVSATTI VKQSKIKKGG KTGVLIDGED GLMTTLAKCC KPAPPDDIAG FVTRERGISV HRKTCPSFRH LAEHAPEKVL DASWAALQEG QVFAVDIEIR AQDRSGLLRD VSDALARHKL NVTAVQTQSR DLEASMRFTL EVKQVNDLPR VLAGLGDVKG VLSVTRL // ID Q5F8U2_NEIG1 Unreviewed; 418 AA. AC Q5F8U2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:AAW89395.1}; GN ORFNames=NGO_0668 {ECO:0000313|EMBL:AAW89395.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89395.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89395.1; -; Genomic_DNA. DR RefSeq; WP_003688821.1; NC_002946.2. DR RefSeq; YP_207807.1; NC_002946.2. DR ProteinModelPortal; Q5F8U2; -. DR EnsemblBacteria; AAW89395; AAW89395; NGO_0668. DR GeneID; 3282060; -. DR KEGG; ngo:NGO0668; -. DR PATRIC; 20334432; VBINeiGon24812_0788. DR HOGENOM; HOG000037301; -. DR KO; K03500; -. DR OMA; RRMEFAH; -. DR OrthoDB; EOG6091D0; -. DR BioCyc; NGON242231:GI2G-635-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR023267; RCMT. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89395.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89395.1}. FT DOMAIN 141 418 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. SQ SEQUENCE 418 AA; 46467 MW; AA0E34175BB79C2D CRC64; MNAAQLDHTA KVLAEMLTFK QPADAVLSAY FRKHKKLGRQ DRHEIAETAF AALRHYQKIS TALRRPHAQP RKAALAALVL GRSTNISQIK DLLDEEETEF FGNLKARKTE FSDGLNTAAE LPQWLVEQLQ QHWSEEEILA FGRSINQAAP LDIRVNTLKG KRDKVLPLLQ AESPDAEATP YSPWGIRLKN KIALNKHELF LDGTLEVQGE GSQLLALLVG AKRGEIIVDF CAGAGGKTLA VGAQMANKGR IYAFDIAEKR LANLKPRMTR AGLTNIHPER IGSEHDTRIA RLAGKADRVL VDAPCSGLGT LRRNPDLKYR QSAETVAKLL EQQHSILDAA SKLVKPQGCL VYATCSVLPE ENELQIKRFL SEHPEFEPVN CAELLQNLKV DLDTGKYLRL DSARHQTDGF FAAVLQRK // ID Q5F769_NEIG1 Unreviewed; 217 AA. AC Q5F769; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 41. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89968.1}; GN ORFNames=NGO_1317 {ECO:0000313|EMBL:AAW89968.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89968.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89968.1; -; Genomic_DNA. DR RefSeq; WP_010951239.1; NC_002946.2. DR RefSeq; YP_208380.1; NC_002946.2. DR DNASU; 3281895; -. DR EnsemblBacteria; AAW89968; AAW89968; NGO_1317. DR GeneID; 3281895; -. DR KEGG; ngo:NGO1317; -. DR PATRIC; 20335997; VBINeiGon24812_1549. DR HOGENOM; HOG000218644; -. DR OMA; RINRSEE; -. DR BioCyc; NGON242231:GI2G-1231-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 23896 MW; E3ECCC918DF3C9F7 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV ANHRLALAAD GVFEGPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADNA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSEEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F7E7_NEIG1 Unreviewed; 861 AA. AC Q5F7E7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. 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 ORFNames=NGO_1231 {ECO:0000313|EMBL:AAW89890.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89890.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89890.1; -; Genomic_DNA. DR RefSeq; WP_003689681.1; NC_002946.2. DR RefSeq; YP_208302.1; NC_002946.2. DR ProteinModelPortal; Q5F7E7; -. DR SMR; Q5F7E7; 1-859. DR PRIDE; Q5F7E7; -. DR EnsemblBacteria; AAW89890; AAW89890; NGO_1231. DR GeneID; 3282479; -. DR KEGG; ngo:NGO1231; -. DR PATRIC; 20335779; VBINeiGon24812_1448. DR HOGENOM; HOG000205991; -. DR KO; K01682; -. DR OMA; HATTRPD; -. DR OrthoDB; EOG6N944W; -. DR BioCyc; NGON242231:GI2G-1142-MONOMER; -. DR UniPathway; UPA00223; UER00718. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW89890.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1, KW ECO:0000256|SAAS:SAAS00436230}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 92732 MW; 4F1D723F056B3AF9 CRC64; MLEAYRKAAA ERAALGIPAL PLNAQQTADL VELLKNPPAG EGEFLVELLA HRVPPGVDDA AKVKASFLAA VAEGSASSPL VSPKYATELL GTMLGGYNIH ALIELLDDDK LAPIAAKGLK HTLLMFDSFH DVQEKAEKGN KYAQEVLQSW ADAEWFASRA KVPEKITVTV FKVDGETNTD DLSPAPDAWS RPDIPLHALA MLKNPRDGIT PDKPGEVGPI KLLEELKAKG HPVAYVGDVV GTGSSRKSAT NSVIWHTGED IPFVPNKRFG GVCLGGKIAP IFFNTQEDSG ALPIEVDVSA LKMGDVVNIL PYEGKIVKNG ETVAEFELKS QVLLDEVQAG GRINLIIGRG LTAKAREALK LPASTAFRLP QAPAESKVGF TLAQKMVGRA CGLPEGQGVR PGTYCEPRMT TVGSQDTTGP MTRDELKDLA CLGFSADMVM QSFCHTAAYP KPVDVKTHKE LPAFISTRGG VSLRPGDGVI HSWLNRLLLP DTVGTGGDSH TRFPIGISFP AGSGLVAFAA ATGVIPLDMP ESVLVRFSGK LQPGVTLRDL VNAIPLYAIK QGLLTVAKAG KKNIFSGRIL EIEGLPDLKV EQAFELTDAS AERSAAGCTV KLNKEPIIEY MKSNVVLMKN MIANGYQDPR ALERRIKAME KWLANPELLE ADKDAEYAAV IEINMDDIKE PIIACPNDPD DVCFMSERSG TKIDEVFIGS CMTNIGHFRA ASKLLEGKSD IPVRLWVAPP TKMDAKELSD EGHYGVLGRA GARMEMPGCS LCMGNQAQVR EGATVMSTST RNFPNRLGKN TFVYLGSAEL AAICSKLGKI PTVEEYQANI GIINEQGDKI YRYMNFNEID SYNEVAETVN V // ID Q5FAH2_NEIG1 Unreviewed; 1071 AA. AC Q5FAH2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|SAAS:SAAS00511136}; DE EC=6.3.5.5 {ECO:0000256|SAAS:SAAS00511136}; GN Name=carB {ECO:0000313|EMBL:AAW88815.1}; GN ORFNames=NGO_0048 {ECO:0000313|EMBL:AAW88815.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88815.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000256|SAAS:SAAS00511129}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|SAAS:SAAS00086141}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|SAAS:SAAS00086104}. 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:0000256|SAAS:SAAS00570548}. CC -!- SIMILARITY: Belongs to the CarB family. CC {ECO:0000256|SAAS:SAAS00570556}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88815.1; -; Genomic_DNA. DR RefSeq; WP_003704965.1; NC_002946.2. DR RefSeq; YP_207227.1; NC_002946.2. DR ProteinModelPortal; Q5FAH2; -. DR EnsemblBacteria; AAW88815; AAW88815; NGO_0048. DR GeneID; 3282357; -. DR KEGG; ngo:NGO0048; -. DR PATRIC; 20332936; VBINeiGon24812_0053. DR HOGENOM; HOG000234582; -. DR KO; K01955; -. DR OMA; AVFPFNK; -. DR OrthoDB; EOG6J1DC6; -. DR BioCyc; NGON242231:GI2G-43-MONOMER; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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 {ECO:0000256|SAAS:SAAS00459920}; KW Arginine biosynthesis {ECO:0000256|SAAS:SAAS00459920}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW88815.1}; KW Magnesium {ECO:0000256|SAAS:SAAS00459944}; KW Manganese {ECO:0000256|SAAS:SAAS00511130}; KW Metal-binding {ECO:0000256|SAAS:SAAS00511109}; KW Pyrimidine biosynthesis {ECO:0000256|SAAS:SAAS00459990}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 673 864 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. SQ SEQUENCE 1071 AA; 117486 MW; 3D6B203EDF5907DF CRC64; MPKRTDLKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVILVNSN PATIMTDPEM ADVTYIEPIM WQTVEKIIAK ERPDAILPTM GGQTALNCAL DLARNGVLAK YNVELIGATE DAIDKAEDRG RFKEAMEKIG LSCPKSFVCH TMNEALAAQE QVGFPTLIRP SFTMGGSGGG IAYNKDEFLA ICERGFDASP THELLIEQSV LGWKEYEMEV VRDKADNCII ICSIENFDPM GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVDTG GSNVQFAVNP ENGEMIVIEM NPRVSRSSAL ASKATGFPIA KVAAKLAVGF TLDELRNDIT GGRTPASFEP SIDYVVTKIP RFAFEKFPAA DDRLTTQMKS VGEVMAMGRT IQESFQKALR GLETGLCGFN PRSEDKAEIR RELANPGPER MLFVADAFRA GFTPEEIHEI CAIDPWFLAQ IEDLMKEEKS VSDGQLQDLD YAALRRLKRK GFSDKRLAQL LNVSEKEVRE HRYALKLHPV YKRVDTCAAE FATETAYLYS TYEEECESRP SDRKKVMILG GGPNRIGQGI EFDYCCVHAA LALRESGFET IMVNCNPETV STDFDTSDRL YFEPLTLEDV LEIVRTENPW GVIVHYGGQT PLKLANALVE NGVNIIGTSA DSIDAAEDRE RFQKVLNDLG LRQPPNRIAH NEEEALVKAE EIGYPLVVRP SYVLGGRAMQ IIHSAEQLQK YMREAVQVSE DSPVLLDFFL NNAIEVDVDC VSDGKDVVIG GIMQHVEQAG IHSGDSGCSL PPYSLSEEIQ DEIRRQTKAM AYALGVVGLM NVQFAVQDGV VFVLEVNPRA SRTVPFVSKA TGVPLAKVGA RCMAGISLKE QGVEKEVVPD FYAVKEAVFP FIKFPGVDTI LGPEMRSTGE VMGVGASFGE AYYKAQLGAG ERLNPTGKIF LSVREEDKER VIKTAKNFQA LGYGICATRG TAQYLTEHGL IVQAINKVPE GRPHIGDALK NGEIALVVNT VSSDPQSVSD SHIIRQSALQ QRVPQYTTTA GGEAMSEGAK SRDYLGVYSV QELHGRLKNR N // ID Q5F6M3_NEIG1 Unreviewed; 392 AA. AC Q5F6M3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}; GN Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909}; GN ORFNames=NGO_1528 {ECO:0000313|EMBL:AAW90164.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90164.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00909, CC ECO:0000256|RuleBase:RU000631}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|HAMAP- CC Rule:MF_00909, ECO:0000256|RuleBase:RU000631}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90164.1; -; Genomic_DNA. DR RefSeq; WP_003689432.1; NC_002946.2. DR RefSeq; YP_208576.1; NC_002946.2. DR ProteinModelPortal; Q5F6M3; -. DR SMR; Q5F6M3; 14-321. DR EnsemblBacteria; AAW90164; AAW90164; NGO_1528. DR GeneID; 3281491; -. DR KEGG; ngo:NGO1528; -. DR PATRIC; 20336552; VBINeiGon24812_1824. DR HOGENOM; HOG000049094; -. DR KO; K03531; -. DR OMA; AQVIWGI; -. DR OrthoDB; EOG6S7XZG; -. DR BioCyc; NGON242231:GI2G-1430-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Septation {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}. FT DOMAIN 16 207 Tubulin. {ECO:0000259|SMART:SM00864}. FT DOMAIN 210 330 Tubulin_C. {ECO:0000259|SMART:SM00865}. FT NP_BIND 24 28 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT NP_BIND 111 113 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT BINDING 142 142 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT BINDING 145 145 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT BINDING 189 189 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. SQ SEQUENCE 392 AA; 41511 MW; FF64B713FDD69DE8 CRC64; MEFVYDVAES AVSPAVIKVI GLGGGGCNAI NNMVANNVRS VEFISANTDA QSLAKNHAAK RIQLGTNLTR GLGAGANPDI GRAAAQEDRE AIEEAIRGAN MLFITTGMGG GTGTGSAPVV AEIAKSLGIL TVAVVTRPFS YEGKRVHVAQ AGLEQLKEYV DSLIIIPNDK LMTALGEDVT MREAFRAADN VLRDAVAGIS EVVTCPSEII NLDFADVKTV MSNRGIAMMG SGYAQGIDRA RMATDQAISS PLLDDVTLDG ARGVLVNITT APGCLKMSEL SEVMKIVNQS AHPDLECKFG AAEDETMSED AIRITIIATG LKEKGAVDPT PAREVEAVAP SKQEQSHNVE GMIRTNRGIR TMNLTAADFD NQSVLDDFEI PAILRRQHNS DK // ID Q5F939_NEIG1 Unreviewed; 887 AA. AC Q5F939; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156}; DE EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156}; GN Name=aceE {ECO:0000313|EMBL:AAW89298.1}; GN ORFNames=NGO_0565 {ECO:0000313|EMBL:AAW89298.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89298.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89298.1; -; Genomic_DNA. DR RefSeq; WP_003691347.1; NC_002946.2. DR RefSeq; YP_207710.1; NC_002946.2. DR ProteinModelPortal; Q5F939; -. DR SMR; Q5F939; 58-880. DR PRIDE; Q5F939; -. DR EnsemblBacteria; AAW89298; AAW89298; NGO_0565. DR GeneID; 3282501; -. DR KEGG; ngo:NGO0565; -. DR PATRIC; 20334192; VBINeiGon24812_0668. DR HOGENOM; HOG000115215; -. DR KO; K00163; -. DR OMA; GFVPQRR; -. DR OrthoDB; EOG6BW4TW; -. DR BioCyc; NGON242231:GI2G-538-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156}; KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:AAW89298.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}. FT DOMAIN 137 292 TRANSKETOLASE_1. FT {ECO:0000259|Pfam:PF00456}. SQ SEQUENCE 887 AA; 99593 MW; 236D9F0A36066FCD CRC64; MSTQLHDVDP IETQEWLDAL SSVLEYEGGE RAQYLLENLL 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 AAATSYANSD FAMIPFYIYY SMFGFQRIGD LAWAAGDMHA RGFLLGGTAG RTTLNGEGLQ HEDGHSHIQA DLIPNCVSYD PTFQYEVAVI VQDGLRRMYA NNEDVFYYIT LMNENYTHPD MPEGAEQDIL KGMYLLKAGG KGDKKVQLMG SGTILQEVIA GAELLKADFG VEADIWSCPS FNLLHRDAIE TERFNRLHPL EAEKVPFVTS QLQGHDGPVI AATDYIRSYA DRIRAYIPND YHVLGTDGFG RSDSRANLRR FFEVDRYNVA VAALAALAEQ GKVSKETVQQ AIEKYGIKAD SAPSWKR // ID Q5F609_NEIG1 Unreviewed; 735 AA. AC Q5F609; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=DNA helicase {ECO:0000256|SAAS:SAAS00553569}; DE EC=3.6.4.12 {ECO:0000256|SAAS:SAAS00553569}; GN ORFNames=NGO_1757 {ECO:0000313|EMBL:AAW90378.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90378.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90378.1; -; Genomic_DNA. DR RefSeq; WP_003698962.1; NC_002946.2. DR RefSeq; YP_208790.1; NC_002946.2. DR ProteinModelPortal; Q5F609; -. DR SMR; Q5F609; 8-645. DR EnsemblBacteria; AAW90378; AAW90378; NGO_1757. DR GeneID; 3281425; -. DR KEGG; ngo:NGO1757; -. DR PATRIC; 20337124; VBINeiGon24812_2102. DR HOGENOM; HOG000033016; -. DR KO; K03657; -. DR OMA; HYRTQKG; -. DR OrthoDB; EOG64N9TW; -. DR BioCyc; NGON242231:GI2G-1653-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90378.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000256|SAAS:SAAS00493105, ECO:0000313|EMBL:AAW90378.1}; KW Hydrolase {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAW90378.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00493105, KW ECO:0000313|EMBL:AAW90378.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 82116 MW; 6AA2F3E2D6204EBC CRC64; MFPDQSAPNL LQGLNPEQLS AVTWPPQSAL VLAGAGSGKT RVLTTRIAWL LQSGQASVHS IMAVTFTNKA AKEMQTRLGA MIPINVRAMW LGTFHGLCHR FLRLHHRDAG LPSSFQILDS GDQLSLIKRL LKSLNIAEEI IAPRSLQGFI NAQKESGLRA SVLGAPDPHT SRMIGCYAEY DKICQREGVV DFAELMLRSY EMLQSNEILR RHYQNRFNHI LVDEFQDTNK LQYAWLKLMA GGNAAVFAVG DDDQSIYRFR GANVGNMTAL MEEFHIDAPV KLEQNYRSVG NILAAANAVI ENNDERLGKN LRTDAEAGDK IRYYSAFTDL EEARFIVDET KALEREGWDL DEIAVLYRSN AQSRVIEQSL FRSGIPYKIY GGLRFYERQE IKHALAYLRL AVNPDDDNAL LRVINFPPRG IGARTVENLQ TASNEQGITL WQAACNAGAK AAKVVAFVRL IEALRNQVGQ MHLSEIIVGI LKDSGLTEHY RTQKGDNQDR LDNLDELVNA AIEFKPEDSN FETLPENISD DPAFPILAFL SNAALESGEN QAGAGEKAVQ LMTVHAAKGL EFNAVFLTGM EEGRFPSEMS LAERGGLEEE RRLMYVAITR ARKRLYITMA QQRMLHGQTQ FGIASRFVEE IPPEVLHYLS VKKPAFDSYG NTRQTTVQRD KIIDDFKQPQ TYAGFRIGQN VRHAKFGTGV IIDAADKGES ARLTINFGKQ GVKELDTKFA KLEAM // ID Q5F8S7_NEIG1 Unreviewed; 426 AA. AC Q5F8S7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 50. DE SubName: Full=Serine protease {ECO:0000313|EMBL:AAW89410.1}; GN ORFNames=NGO_0683 {ECO:0000313|EMBL:AAW89410.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89410.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89410.1; -; Genomic_DNA. DR RefSeq; WP_003693022.1; NC_002946.2. DR RefSeq; YP_207822.1; NC_002946.2. DR EnsemblBacteria; AAW89410; AAW89410; NGO_0683. DR GeneID; 3281810; -. DR KEGG; ngo:NGO0683; -. DR PATRIC; 20334464; VBINeiGon24812_0804. DR HOGENOM; HOG000218976; -. DR OMA; GSFERAC; -. DR OrthoDB; EOG67DPJ4; -. DR BioCyc; NGON242231:GI2G-650-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR014044; CAP_domain. DR Pfam; PF00188; CAP; 1. DR SUPFAM; SSF55797; SSF55797; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89410.1}; KW Protease {ECO:0000313|EMBL:AAW89410.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 426 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255546. FT DOMAIN 46 173 SCP. {ECO:0000259|Pfam:PF00188}. SQ SEQUENCE 426 AA; 47901 MW; 1B8B144DB46F6363 CRC64; MKSLFIWLLL LGSAAGVFYH TQNQSLPAGE LVYPSAPQIR DGGDALHYLN RIRTQIGLHA LAHAPVLENS ARRHARYLTL NPEDGHGEHH PDNPHYTAQK LTERTRLAGY LYNGVHENIS TEEEAAESSD SDIRTQQRQV DALMSAIYHR LSLLDRHTDE AGAAFVRENG KTVLVFNQGN GSFERACAKG RRQPEAGRKY YRNACHNGAA VYADEAMPVT ELLYTAYPVG GGALPYFYGE RPDPVPEYEI TGNPASIDFS EAAGKIAMKS FKLYQGKNEI RPVRVLTAGN DPNGRLTAHQ FALFPLKPLE YGTLYTAVFD YVRNGRHAQA KWQFRTRKPD YPYFEVNGGE TLAVRKGEKY FIHWRGRWCL EACTRYTYRR QFGNSLSILR HEAGGIVFSV SGMAGSRIRL TPEDSPERGV TLYLQD // ID A0A0H4ISP1_NEIG1 Unreviewed; 73 AA. AC A0A0H4ISP1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63634.1}; GN ORFNames=NGO_03320 {ECO:0000313|EMBL:AKO63634.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63634.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63634.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63634; AKO63634; NGO_03320. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR005589; DUF331. DR Pfam; PF03889; DUF331; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 73 AA; 8452 MW; 0579DF894F4F92F1 CRC64; MGGKAQHNKG KIRDNALKAL VKSDLFRHKV ERKRKGKGSY NRQEAKKRRD GFDTVPPFLC LKRGSSRRSR RSL // ID A0A0H4IWH1_NEIG1 Unreviewed; 268 AA. AC A0A0H4IWH1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63783.1}; GN ORFNames=NGO_10090 {ECO:0000313|EMBL:AKO63783.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63783.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63783.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63783; AKO63783; NGO_10090. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR005017; OMPP1/FadL/TodX. DR Pfam; PF03349; Toluene_X; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 268 AA; 29878 MW; E24F2938822D3D77 CRC64; MLQATPSNPT AAAQIKADGH ADVKGSDWGV GYQLAWMWDI NDRARVGVNY RSKVSHTLKG DAEWAADGAA AKQQWNDNML TPLGYTANEK ASVKIVTPES LSVHGMYKVS DKADLFGDVT WTRHSRFNKA ELFFEKEKNI ANGKKSDRTT ITPNWRNTYK VGLGGSYQIS EPLQLRVGIA FDKPPVRNAD YRMNSLPDGN RIWFSAGMKY HIGKNHVVDA AYTHIHINDT SYRTAKASGN DVDSKGASCA RFKNHADIIG LQYTYKFK // ID A0A0H4IRQ7_NEIG1 Unreviewed; 116 AA. AC A0A0H4IRQ7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63636.1}; GN ORFNames=NGO_03645 {ECO:0000313|EMBL:AKO63636.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63636.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63636.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63636; AKO63636; NGO_03645. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 116 AA; 12473 MW; 0A5895246F25BB80 CRC64; MGVNGLQSNS PYSGHTTGTF INNQPSNTTQ PSLDGTSTIE LKAVKGNNEV DLNVKNHASV KGIITSHSAK ATLEAEEDNI VRVKNPDTKT ALINAWKEKY PNNSPEPYRV GGSIHD // ID Q5F5B8_NEIG1 Unreviewed; 219 AA. AC Q5F5B8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=Amino acid ABC transporter permease {ECO:0000313|EMBL:AAW90619.1}; GN ORFNames=NGO_2011 {ECO:0000313|EMBL:AAW90619.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90619.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90619.1; -; Genomic_DNA. DR RefSeq; WP_003686917.1; NC_002946.2. DR RefSeq; YP_209031.1; NC_002946.2. DR ProteinModelPortal; Q5F5B8; -. DR EnsemblBacteria; AAW90619; AAW90619; NGO_2011. DR GeneID; 3282615; -. DR KEGG; ngo:NGO2011; -. DR PATRIC; 20337803; VBINeiGon24812_2425. DR HOGENOM; HOG000267552; -. DR KO; K02029; -. DR OMA; YEMLAVM; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NGON242231:GI2G-1912-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450258, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 23 44 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 65 83 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 89 112 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 133 155 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 186 205 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 17 205 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 219 AA; 24091 MW; A9C178F44C56A50A CRC64; MNWPYLIDAV PKFADAAKLT LELSVYGVVL SLLFGLPVAV VTAYRIRPFY ALARAYIELS RNTPLLIQLF FLYYGLPKMG IKWDGFTCGV IALVFLGASY MAEAVRAGIL AVPKGQVGAG KAIGLSRFQV FRYVELPQVW AVAVPAIGAN ILFLMKETSV VSTVGIAELL FVTKDVIGMD YKTNEALFLL FAAYLIILLP VSLLARRIEN RVRSAKYGV // ID A0A0H4IS83_NEIG1 Unreviewed; 37 AA. AC A0A0H4IS83; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE RecName: Full=50S ribosomal protein L36 {ECO:0000256|HAMAP-Rule:MF_00251, ECO:0000256|RuleBase:RU000571}; GN Name=rpmJ {ECO:0000256|HAMAP-Rule:MF_00251, GN ECO:0000313|EMBL:AKO63776.1}; GN ORFNames=NGO_09710 {ECO:0000313|EMBL:AKO63776.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63776.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein L36P family. CC {ECO:0000256|HAMAP-Rule:MF_00251, ECO:0000256|RuleBase:RU000571}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AKO63776.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63776; AKO63776; NGO_09710. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00251, KW ECO:0000256|RuleBase:RU000571, ECO:0000313|EMBL:AKO63776.1}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00251, KW ECO:0000256|RuleBase:RU000571, ECO:0000313|EMBL:AKO63776.1}. SQ SEQUENCE 37 AA; 4473 MW; 53BD743EF9940F0D CRC64; MRVQPSVKKI CRNCKIIRRN RVVRVICTDP RHKQRQG // ID Q5F8N8_NEIG1 Unreviewed; 217 AA. AC Q5F8N8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 45. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89449.1}; GN ORFNames=NGO_0730 {ECO:0000313|EMBL:AAW89449.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89449.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89449.1; -; Genomic_DNA. DR RefSeq; WP_010951115.1; NC_002946.2. DR RefSeq; YP_207861.1; NC_002946.2. DR EnsemblBacteria; AAW89449; AAW89449; NGO_0730. DR GeneID; 3282091; -. DR KEGG; ngo:NGO0730; -. DR PATRIC; 20334602; VBINeiGon24812_0873. DR HOGENOM; HOG000218644; -. DR OMA; RETIAHH; -. DR BioCyc; NGON242231:GI2G-689-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24047 MW; CD51EB6F68CCB15F CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFECPAGPG GSYFGGRRKG GRGRGAAGKA VVFGIPKRNG RAYTVAADDA EPETLLPAVK KKIMPDGIVY ADSPGSRGKL DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F6Y1_NEIG1 Unreviewed; 217 AA. AC Q5F6Y1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 48. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW90056.1}; GN ORFNames=NGO_1412 {ECO:0000313|EMBL:AAW90056.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90056.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90056.1; -; Genomic_DNA. DR RefSeq; WP_010951260.1; NC_002946.2. DR RefSeq; YP_208468.1; NC_002946.2. DR EnsemblBacteria; AAW90056; AAW90056; NGO_1412. DR GeneID; 3281165; -. DR KEGG; ngo:NGO1412; -. DR PATRIC; 20336231; VBINeiGon24812_1664. DR HOGENOM; HOG000218644; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-1321-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24160 MW; 0D25F770CD55C44F CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFERPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RTYTVAADNA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP FLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F8X7_NEIG1 Unreviewed; 106 AA. AC Q5F8X7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Iron-sulfur cluster assembly protein {ECO:0000313|EMBL:AAW89360.1}; GN Name=iscA {ECO:0000313|EMBL:AAW89360.1}; GN ORFNames=NGO_0632 {ECO:0000313|EMBL:AAW89360.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89360.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89360.1; -; Genomic_DNA. DR RefSeq; WP_010951096.1; NC_002946.2. DR RefSeq; YP_207772.1; NC_002946.2. DR ProteinModelPortal; Q5F8X7; -. DR SMR; Q5F8X7; 2-96. DR EnsemblBacteria; AAW89360; AAW89360; NGO_0632. DR GeneID; 3281279; -. DR KEGG; ngo:NGO0632; -. DR PATRIC; 20334348; VBINeiGon24812_0746. DR HOGENOM; HOG000228314; -. DR KO; K13628; -. DR OMA; LAYSVDY; -. DR OrthoDB; EOG6VXF8J; -. DR BioCyc; NGON242231:GI2G-600-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 102 Fe-S_biosyn. {ECO:0000259|Pfam:PF01521}. SQ SEQUENCE 106 AA; 11638 MW; A394EE573DE3A09F CRC64; MITLTENAAK HINDYLAKRG KGLGVRLGVK TSGCSGMAYN LEFVDEANGD DLIFEGHGAR IYIDPKSLVY LDGTQVDYTK EDLQEGFKFE NPNVKDSCGC GESFHV // ID Q5F666_NEIG1 Unreviewed; 456 AA. AC Q5F666; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 90. 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 ORFNames=NGO_1700 {ECO:0000313|EMBL:AAW90321.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90321.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90321.1; -; Genomic_DNA. DR RefSeq; WP_010951325.1; NC_002946.2. DR RefSeq; YP_208733.1; NC_002946.2. DR ProteinModelPortal; Q5F666; -. DR SMR; Q5F666; 2-429. DR EnsemblBacteria; AAW90321; AAW90321; NGO_1700. DR GeneID; 3281202; -. DR KEGG; ngo:NGO1700; -. DR PATRIC; 20336992; VBINeiGon24812_2036. DR HOGENOM; HOG000036164; -. DR KO; K03106; -. DR OMA; MLPGMGQ; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; NGON242231:GI2G-1596-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 49501 MW; C99B59FA7DBC3C01 CRC64; MLDNLTGRFS NVFKNIRGQA KLTEDNIKEA LREVRLALLE ADVALPVVKE FVNNVKEKAL GQEVAGSLTP DQAFIGVVNQ ALVELMGKEN KTLDLSVSPP AIILMAGLQG AGKTTTVGKL ARLLKNDQKK KVLVVSADVY RPAAIEQLRL LAEQVGVDFF PSDTNQKPVE IATAAVDYAK KHFYDVLMVD TAGRLAIDEE MMNEIKALHA VVNPVETLFV IDAMLGQDAV NTAQAFNEAL PLNGVVLTKM DGDSRGGAAL SVRHVTGKPI KFIGVGEKIN GLEPFHPDRL ASRILGMGDV LTLIEDVQKG IDEEAAAKMA KKLQKGKGFD LNDFKEQIQQ MRNMGGLENL MSKMPGELGQ ISKQIPEGTA EKAMGKVEAI INSMTPKERA NPALLKAGRK RRIAMGAGTT VQEVNKLLKQ FEQMQQMMKM FSGNGLGKLM RLAKGMKGIK GMFPGL // ID A0A0H4J5B4_NEIG1 Unreviewed; 229 AA. AC A0A0H4J5B4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63587.1}; GN ORFNames=NGO_00350 {ECO:0000313|EMBL:AKO63587.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63587.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63587.1; -; Genomic_DNA. DR RefSeq; WP_030003509.1; NC_002946.2. DR RefSeq; YP_008914846.1; NC_002946.2. DR EnsemblBacteria; AKO63587; AKO63587; NGO_00350. DR GeneID; 19592999; -. DR KEGG; ngo:NGO0066a; -. DR Proteomes; UP000000535; 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; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 229 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 229 AA; 26013 MW; 2EBA2B08F6F0EC9C CRC64; MQADLAYAAE RITHDYPEPT GAKKGKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWNNS KYSVNTKKVN ENKGEKINVT QYLKAENQEN GTFHAVSSLG LSAVYDFKLN DKFKPYIGMR VGYGHVRHQV RSVEQETTTV TTYLQSGKPS PIVRGSTLKL PHHESRSSRR LGFGAMAGVG IDVAPGLTLD AGYRYHYWGR LENTRFKTHE ASLGVRYRF // ID Q5F8L8_NEIG1 Unreviewed; 204 AA. AC Q5F8L8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE RecName: Full=Molybdenum cofactor guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316, ECO:0000256|SAAS:SAAS00049907}; DE Short=MoCo guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316}; DE EC=2.7.7.77 {ECO:0000256|HAMAP-Rule:MF_00316, ECO:0000256|SAAS:SAAS00049907}; DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316}; DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000256|HAMAP-Rule:MF_00316}; GN Name=mobA {ECO:0000256|HAMAP-Rule:MF_00316}; GN ORFNames=NGO_0754 {ECO:0000313|EMBL:AAW89469.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89469.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00316, ECO:0000256|SAAS:SAAS00049938}. CC -!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate + CC guanylyl molybdenum cofactor. {ECO:0000256|HAMAP-Rule:MF_00316, CC ECO:0000256|SAAS:SAAS00049917}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00316}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00316}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316, CC ECO:0000256|SAAS:SAAS00049910}. 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:0000256|HAMAP- CC Rule:MF_00316}. CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000256|HAMAP- CC Rule:MF_00316, ECO:0000256|SAAS:SAAS00554780}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89469.1; -; Genomic_DNA. DR RefSeq; WP_003691204.1; NC_002946.2. DR RefSeq; YP_207881.1; NC_002946.2. DR ProteinModelPortal; Q5F8L8; -. DR EnsemblBacteria; AAW89469; AAW89469; NGO_0754. DR GeneID; 3282496; -. DR KEGG; ngo:NGO0754; -. DR PATRIC; 20334654; VBINeiGon24812_0899. DR HOGENOM; HOG000280423; -. DR KO; K03752; -. DR OMA; RTSAMKT; -. DR OrthoDB; EOG61041R; -. DR BioCyc; NGON242231:GI2G-709-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440752}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440756}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440765}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440770}; KW Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440784}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440756}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00316, KW ECO:0000256|SAAS:SAAS00440748}. FT DOMAIN 17 179 NTP_transf_3. {ECO:0000259|Pfam:PF12804}. FT NP_BIND 20 22 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}. FT METAL 113 113 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00316}. FT BINDING 33 33 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}. FT BINDING 79 79 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}. FT BINDING 113 113 GTP. {ECO:0000256|HAMAP-Rule:MF_00316}. SQ SEQUENCE 204 AA; 23024 MW; DFFDB1CC08118F5A CRC64; MKTSNFPKSP PALKTFALIL AGGLADRMGG EDKGLALLEG RPLIDRVIGK IRPQVSHIVI SANRNLEEYA RRSPHVFPDA RQWQHFGPLS ALCTAANDLQ LAAADWLLIV PCDMPYLPDD LVARFESVSK RTPLCNAFYV ETPVTMHYNI MYIRPQILQS AIPYLFSGMK TLRSWLQQQR ARPVRFEFDG HFADLNTQTD LQEG // ID Q5F8J6_NEIG1 Unreviewed; 89 AA. AC Q5F8J6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=Transcriptional regulator HU subunit alpha {ECO:0000313|EMBL:AAW89491.1}; GN ORFNames=NGO_0777 {ECO:0000313|EMBL:AAW89491.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89491.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|SAAS:SAAS00560778}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000256|RuleBase:RU003939, ECO:0000256|SAAS:SAAS00560676}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89491.1; -; Genomic_DNA. DR RefSeq; WP_003688640.1; NC_002946.2. DR RefSeq; YP_207903.1; NC_002946.2. DR ProteinModelPortal; Q5F8J6; -. DR PRIDE; Q5F8J6; -. DR EnsemblBacteria; AAW89491; AAW89491; NGO_0777. DR GeneID; 3281874; -. DR KEGG; ngo:NGO0777; -. DR PATRIC; 20334700; VBINeiGon24812_0922. DR HOGENOM; HOG000043828; -. DR KO; K03530; -. DR OMA; AVARDCE; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NGON242231:GI2G-731-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW DNA condensation {ECO:0000256|SAAS:SAAS00560671}; KW DNA-binding {ECO:0000256|SAAS:SAAS00560702}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 89 AA; 9377 MW; A61F833CDE7954DB CRC64; MNKSELIEAI AQEADISKAA AQKALDATTN AVTNALKQGD TVTLVGFGTF YVGERAERQG RNPKTGEPLT IAAAKTLKFR AGKALKDAL // ID Q5F921_NEIG1 Unreviewed; 268 AA. AC Q5F921; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 55. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89316.1}; GN ORFNames=NGO_0585 {ECO:0000313|EMBL:AAW89316.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89316.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89316.1; -; Genomic_DNA. DR RefSeq; WP_003688964.1; NC_002946.2. DR RefSeq; YP_207728.1; NC_002946.2. DR EnsemblBacteria; AAW89316; AAW89316; NGO_0585. DR GeneID; 3282250; -. DR KEGG; ngo:NGO0585; -. DR PATRIC; 20334242; VBINeiGon24812_0693. DR HOGENOM; HOG000068439; -. DR KO; K07090; -. DR OMA; FKTLHTG; -. DR OrthoDB; EOG6RZB3C; -. DR BioCyc; NGON242231:GI2G-556-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363041}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 109 128 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 140 160 Helical. {ECO:0000256|RuleBase:RU363041}. FT TRANSMEM 216 236 Helical. {ECO:0000256|RuleBase:RU363041}. SQ SEQUENCE 268 AA; 27942 MW; 456305CE9CD32D59 CRC64; MWHWDIILIL LAVGSAAGFI AGLFGVGGGT LIVPVVLWVL DLQGLAQHPY AQHLAVGTSF AVMVFTAFSS MLGQHKKQAV DWKTIFAMMP GMIFGVFAGA LSAKYIPAFG LQIFFILFLT AVAFKTLHTG RQTASRPLPG LPGLTAVSTL FGAMSSWVGI GGGSLSVPFL IHCGFPAHKA IGTSSGLAWP IALSGAISYL VNGLNIAGLP EGSLGFLYLP AVAVLSAATI AFAPLGVKTA HKLSSAKLKE SFGIMLLLIA GKMLYNLL // ID Q5F845_NEIG1 Unreviewed; 922 AA. AC Q5F845; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 76. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAW89642.1}; GN ORFNames=NGO_0952 {ECO:0000313|EMBL:AAW89642.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89642.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89642.1; -; Genomic_DNA. DR RefSeq; WP_003706334.1; NC_002946.2. DR RefSeq; YP_208054.1; NC_002946.2. DR ProteinModelPortal; Q5F845; -. DR EnsemblBacteria; AAW89642; AAW89642; NGO_0952. DR GeneID; 3282122; -. DR KEGG; ngo:NGO0952; -. DR PATRIC; 20335089; VBINeiGon24812_1114. DR HOGENOM; HOG000219020; -. DR KO; K16087; -. DR OMA; NNQELQK; -. DR OrthoDB; EOG6T7N3H; -. DR BioCyc; NGON242231:GI2G-884-MONOMER; -. DR Proteomes; UP000000535; 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 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 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00444644}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00444644, KW ECO:0000256|SAAS:SAAS00447760}; KW Receptor {ECO:0000313|EMBL:AAW89642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW TonB box {ECO:0000256|RuleBase:RU003357, KW ECO:0000256|SAAS:SAAS00444615}; KW Transmembrane {ECO:0000256|SAAS:SAAS00447760}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00447760}. FT DOMAIN 60 167 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 577 921 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 922 AA; 104164 MW; 2E859A2DD0DAF4F3 CRC64; MRSSFRLKPI CFYLMGVMLY HHSYAEDAGR AGSEAQIQVL EDVHVKAKRV PKDKKVFTDA RAVSTRQDVF KSGENLDNIV RSIPGAFTQQ DKSSGIVSLN IRGDSGFGRV NTMVDGITQT FYSTSTDAGR AGGSSQFGAS VDSNFIAGLD VVKGSFSGSA GINSLAGSAN LRTLGVDDVV QGNNTYGLLL KGLTGTNSTK GNAMAAIGAR KWLESGASVG VLYGHSRRGV AQNYRVGGGG QHIGNFGEEY LERRKQQYFV QEGGLKFNAG SGKWERDLQR QYWKTKWYKK YEDPQELQKY IEEHDKSWRE NLAPQYDITP IDPSGLKQQS AGNLFKLEYD GVFNKYTAQF RDLNTRIGSR KIINRNYQFN YGLSLNPYTN LNLTAAYNSG RQKYPKGAKF TGWGLLKDFE TYNNAKILDL NNTATFRLPR ETELQTTLGF NYFHNEYGKN RFPEELGLFF DGPDQDNGLY SYLGRFKGDK GLLPQKSTIV QPAGSQYFNT FYFDAALKKD IYRLNYSTNA INYRFGGEYT GYYGSENEFK RAFGENSPAY KEHCDPSCGL YEPVLKKYGK KRANNHSVSI SADFGDYFMP FAGYSRTHRM PNIQEMYFSQ IGDSGVHTAL KPERANTWQF GFNTYKKGLL KQDDILGLKL VGYRSRIDNY IHNVYGKWWD LNGDIPSWVG STGLAYTIRH RNFKDKVHKH GFELELNYDY GRFFTNLSYA YQKSTQPTNF SDASESPNNA SKEDQLKQGY GLSRVSALPR DYGRLEVGTR WLGNKLTLGG AMRYFGKSIR ATAEERYIDG TNGGNTSNVR QLGKRSIKQT ETLARQPLIF DFYAAYEPKK NLIFRAEVKN LFDRRYIDPL DAGNDAATQR YYSSFDPKDK DEDVTCNADK TLCNGKYGGT SKSVLTNFAR GRTFLMTMSY KF // ID A0A0H4IS99_NEIG1 Unreviewed; 71 AA. AC A0A0H4IS99; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63791.1}; GN ORFNames=NGO_10520 {ECO:0000313|EMBL:AKO63791.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63791.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63791.1; -; Genomic_DNA. DR RefSeq; WP_002218233.1; NC_002946.2. DR RefSeq; YP_009115489.1; NC_002946.2. DR EnsemblBacteria; AKO63791; AKO63791; NGO_10520. DR GeneID; 22847898; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025234; DUF4177. DR Pfam; PF13783; DUF4177; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 8447 MW; B448DE79BAA2634F CRC64; MKEYKVVIYQ ESLLSSLFFG AAKVNPVNFS AFLNKQTPEG WRVVTMEKDL RRMLLFFKRE AYVVILERDR V // ID A0A0H4IW46_NEIG1 Unreviewed; 356 AA. AC A0A0H4IW46; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Integrase {ECO:0000313|EMBL:AKO63653.1}; GN ORFNames=NGO_03890 {ECO:0000313|EMBL:AKO63653.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63653.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000256|SAAS:SAAS00541913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AKO63653.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63653; AKO63653; NGO_03890. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR025166; DUF4102. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR Pfam; PF13356; DUF4102; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 90 DUF4102. {ECO:0000259|Pfam:PF13356}. FT DOMAIN 211 296 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. SQ SEQUENCE 356 AA; 39731 MW; 9C4C21B78834A124 CRC64; MAAHNKLTQK QIEAAKADGK QSKLADGGGL YLLLHPNGSK YWRMRYRHGG CEKTLALGVY PAVSLKQARE LARAARAQTA AGIDPVAEHH RTRPGSGRSL PEIARAWYGS RQGQRADNTL EGDRRSLAYL TDYYKDNTDI NDITTAGVSK FIEHLNRINI PACARRTVQI LAQIWDYAVQ RGIITDEWRN PATTARPLLN TSKPKPQPHI RPDELPDFYR TLQTAHDLHP YARPLLLLAA LTVPRPSALL SARWQDIDLT ARLWHIPAAD MKTKHPFTVP LSDWAVEILR ELHTQTGDNI HLFPGIRPRR KPAPHPDHIS IKFAHNAIRR LGYDGSTPAN PNTPCTDSAT SSPTSA // ID A0A0H4IS79_NEIG1 Unreviewed; 69 AA. AC A0A0H4IS79; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63771.1}; GN ORFNames=NGO_09385 {ECO:0000313|EMBL:AKO63771.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63771.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63771.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63771; AKO63771; NGO_09385. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 49 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 69 AA; 8144 MW; AFAA43EA1BF760FA CRC64; MEVVIALVPF LRLVKWGANG LQYDLAESVF VTGFLIVINF LNRHFIFLLQ KLWMRLYAKI FVIKTMKLI // ID A0A0H4ISJ9_NEIG1 Unreviewed; 212 AA. AC A0A0H4ISJ9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 8. DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917}; DE Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917}; DE EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917}; DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917}; GN Name=queE {ECO:0000256|HAMAP-Rule:MF_00917}; GN ORFNames=NGO_00720 {ECO:0000313|EMBL:AKO63599.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63599.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00917}. CC -!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7- CC carboxy-7-carbaguanine + NH(3). {ECO:0000256|HAMAP-Rule:MF_00917}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00917}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00917}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- CC deazaguanine synthase family. {ECO:0000256|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; AE004969; AKO63599.1; -; Genomic_DNA. DR RefSeq; WP_025456391.1; NC_002946.2. DR RefSeq; YP_207303.2; NC_002946.2. DR EnsemblBacteria; AKO63599; AKO63599; NGO_00720. DR GeneID; 3281233; -. DR KEGG; ngo:NGO0132; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00917}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00917}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00917}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00917}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00917}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00917}; KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00917}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00917}. FT DOMAIN 38 118 Radical_SAM. {ECO:0000259|Pfam:PF04055}. FT REGION 22 24 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00917}. FT REGION 122 124 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_00917}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00917}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00917}. FT METAL 48 48 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00917}. FT METAL 50 50 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00917}. FT BINDING 37 37 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00917}. FT BINDING 78 78 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00917}. FT BINDING 80 80 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00917}. SQ SEQUENCE 212 AA; 23635 MW; 48C49E14DE002368 CRC64; MKKISVAPEN PQYRIVEIFE SLQGEGWNTG MPAVFVRLGK CNLACGWCDT DYLTFGMMSL SDILGRLKTY AARNIIITGG EPTIQPHLDT LLDALKAEGY FLCLETNGLK PAPPQIDYVA TSPKACYAAK YEKSCIETAD EVRIVADGDA VGFCENMERK IRAHHYYLSP CEQDGAMNIY DTIRQIGILN SRPDAPVHWQ LSVQTHKWAG IE // ID A0A0H4IRV3_NEIG1 Unreviewed; 64 AA. AC A0A0H4IRV3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Baseplate assembly protein {ECO:0000313|EMBL:AKO63651.1}; GN ORFNames=NGO_03860 {ECO:0000313|EMBL:AKO63651.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63651.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63651.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63651; AKO63651; NGO_03860. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 6712 MW; 1990C763DC8560F7 CRC64; MELKAVTSLT IDTPQTTITG HLTVNQTTTA QGLLTYQNGM NGQGGSLSEH THPDDSGGTT EKPQ // ID A0A0H4ISC9_NEIG1 Unreviewed; 81 AA. AC A0A0H4ISC9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63821.1}; GN ORFNames=NGO_11550 {ECO:0000313|EMBL:AKO63821.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63821.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63821.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63821; AKO63821; NGO_11550. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 81 AA; 9334 MW; D640ACB252726F38 CRC64; MLCLKRQAAA NPLFGKGRLK IFSDDLLFIE QTPQTADNPT DKLLQFRVDF LLFPRKANKS RKNIKSVKKL RTNSLISCNH M // ID A0A0H4J5J6_NEIG1 Unreviewed; 157 AA. AC A0A0H4J5J6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63667.1}; GN ORFNames=NGO_04785 {ECO:0000313|EMBL:AKO63667.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63667.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63667.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63667; AKO63667; NGO_04785. DR Proteomes; UP000000535; 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 Pfam; PF02371; Transposase_20; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 157 AA; 17317 MW; 6E5351517057A414 CRC64; MAAITKCLHQ VHETQVESVK QLIARFDRLI DESDKQIDNH TRTHFDGKAQ VAEQIKGIGS ITTATLMAML PELGRLSHKR IAGLVGIAPH PRESGETKFK SRCFGGRSAV RKALYMAAAA ATRFEPLIRD FHQRLLYSEL TKTGTALPRP GSKGTIP // ID A0A0H4IVJ6_NEIG1 Unreviewed; 277 AA. AC A0A0H4IVJ6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=RNA polymerase sigma factor {ECO:0000313|EMBL:AKO63770.1}; GN ORFNames=NGO_09380 {ECO:0000313|EMBL:AKO63770.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63770.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63770.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63770; AKO63770; NGO_09380. DR Proteomes; UP000000535; 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 Pfam; PF00309; Sigma54_AID; 1. DR Pfam; PF04963; Sigma54_CBD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 100 220 Sigma54_CBD. {ECO:0000259|Pfam:PF04963}. SQ SEQUENCE 277 AA; 30979 MW; 202F8E4D7BE61A8C CRC64; MTLCGIFLRR QAENNNFYRI IITLIGIKLK QTQQLDQRLQ QSLRVLQMPG IELEREVENW PSDNPLLERK ETDEFSDAEF SHYTAPARQI GGDEGEDMLS NIAGEEDFKQ YLHAQACEHP LSDQEAACVH ILIDFLDEQG YLTDSIEDIL DHTPLEWMLD EAMLKQALTA LKKFDPAGMA AADVTESLIL QIERSGECAA KPAALHIVRN ALDSIDGNRS QTPARIKNAC PKPTAAHSKP HSASLLRSTP FPPPVLPRPR PSPILTRHSP TCWLSAV // ID Q5F647_NEIG1 Unreviewed; 319 AA. AC Q5F647; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=Alpha/beta hydrolase {ECO:0000313|EMBL:AAW90340.1}; GN ORFNames=NGO_1719 {ECO:0000313|EMBL:AAW90340.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90340.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90340.1; -; Genomic_DNA. DR RefSeq; WP_003705245.1; NC_002946.2. DR RefSeq; YP_208752.1; NC_002946.2. DR ProteinModelPortal; Q5F647; -. DR ESTHER; neime-NMB0276; abh_upf0017. DR EnsemblBacteria; AAW90340; AAW90340; NGO_1719. DR GeneID; 3281305; -. DR KEGG; ngo:NGO1719; -. DR PATRIC; 20337032; VBINeiGon24812_2056. DR HOGENOM; HOG000264007; -. DR OMA; HLQTLWG; -. DR OrthoDB; EOG6C5RKG; -. DR BioCyc; NGON242231:GI2G-1615-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90340.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 319 AA; 34673 MW; E2939AAC19B3AF28 CRC64; MILTPPDTPF FLRNGNADTI AAKFLQHPAP AYRREMLPDS TGKTKTAYDF SAGGISPDAP LVVLFHGLEG SSRSHYAVEL MLAVRNRGWH GAVVHFRSCG GVANTAPVFY HLGDTAEIAF ALDTLTARYR EIYAVGVSLG GNAPAKYLGE QGKKALPHAS AAVSAPVDAE AAGSRFDSGI TRLLYTRYFL RTLIPKARSL QGFQTAFAAG CKTLGEFDDR FTAPLHGFAD RHDYYRQTSC KPLLKHVAKP LLLLNAANDP FLPPEALPRA DEASEAVTLF QPAHGGHAGF VSSTGGRLHL QWLPQTVLSY FDSFRTNRR // ID A0A0H4IRJ9_NEIG1 Unreviewed; 40 AA. AC A0A0H4IRJ9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63586.1}; GN ORFNames=NGO_00300 {ECO:0000313|EMBL:AKO63586.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63586.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63586.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63586; AKO63586; NGO_00300. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 40 AA; 4916 MW; A9539D23C9B17E72 CRC64; MRFIAYCCYM FVLLYNGCIK NYAHRLSRRF ESLIFDNLET // ID Q5F9I2_NEIG1 Unreviewed; 168 AA. AC Q5F9I2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89155.1}; GN ORFNames=NGO_0412 {ECO:0000313|EMBL:AAW89155.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89155.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0307 family. CC {ECO:0000256|SAAS:SAAS00540468}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89155.1; -; Genomic_DNA. DR RefSeq; WP_010357415.1; NC_002946.2. DR RefSeq; YP_207567.1; NC_002946.2. DR ProteinModelPortal; Q5F9I2; -. DR EnsemblBacteria; AAW89155; AAW89155; NGO_0412. DR GeneID; 3282558; -. DR KEGG; ngo:NGO0412; -. DR PATRIC; 20333835; VBINeiGon24812_0495. DR HOGENOM; HOG000013875; -. DR KO; K09889; -. DR OMA; HLIERWR; -. DR OrthoDB; EOG6RJV5H; -. DR BioCyc; NGON242231:GI2G-390-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.10.60.30; -; 2. 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 168 AA; 19105 MW; 050137E84B1450B1 CRC64; MFEQEDEWIS KTQMKKQMNG LQDLGMELTR LSNDTLKKIG LDEDLYEAVV TYKKITSNGA LKRQAQFIGR LMRDTDPAPI EAFLAKLRGD DAAHNAFLQR VEQARVRLLA DEGALTQFMS DFPNAGAGRL RTLVRNTKKE QEQDKPPKNF RALFQELKTV MENGGAEI // ID Q5F5R0_NEIG1 Unreviewed; 178 AA. AC Q5F5R0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000256|HAMAP-Rule:MF_00948, ECO:0000256|SAAS:SAAS00078489}; GN Name=nusG {ECO:0000256|HAMAP-Rule:MF_00948}; GN ORFNames=NGO_1856 {ECO:0000313|EMBL:AAW90477.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90477.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Participates in transcription elongation, termination CC and antitermination. {ECO:0000256|HAMAP-Rule:MF_00948, CC ECO:0000256|RuleBase:RU000538, ECO:0000256|SAAS:SAAS00565765}. CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000256|HAMAP- CC Rule:MF_00948, ECO:0000256|RuleBase:RU000538, CC ECO:0000256|SAAS:SAAS00565689}. CC -!- SIMILARITY: Contains 1 KOW domain. {ECO:0000256|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; AE004969; AAW90477.1; -; Genomic_DNA. DR RefSeq; WP_002215369.1; NC_002946.2. DR RefSeq; YP_208889.1; NC_002946.2. DR ProteinModelPortal; Q5F5R0; -. DR SMR; Q5F5R0; 121-176. DR PRIDE; Q5F5R0; -. DR EnsemblBacteria; AAW90477; AAW90477; NGO_1856. DR GeneID; 3282366; -. DR KEGG; ngo:NGO1856; -. DR PATRIC; 20337392; VBINeiGon24812_2231. DR HOGENOM; HOG000219265; -. DR KO; K02601; -. DR OMA; EDKIFRI; -. DR OrthoDB; EOG6FFS95; -. DR BioCyc; NGON242231:GI2G-1757-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00948, KW ECO:0000256|RuleBase:RU000538, ECO:0000256|SAAS:SAAS00454500, KW ECO:0000256|SAAS:SAAS00454517}; KW Transcription antitermination {ECO:0000256|HAMAP-Rule:MF_00948, KW ECO:0000256|RuleBase:RU000538, ECO:0000256|SAAS:SAAS00454500}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00948, KW ECO:0000256|RuleBase:RU000538, ECO:0000256|SAAS:SAAS00454500, KW ECO:0000256|SAAS:SAAS00454517}; KW Transcription termination {ECO:0000256|HAMAP-Rule:MF_00948, KW ECO:0000256|RuleBase:RU000538, ECO:0000256|SAAS:SAAS00454517}. FT DOMAIN 2 111 NGN. {ECO:0000259|SMART:SM00738}. FT DOMAIN 123 150 KOW. {ECO:0000259|SMART:SM00739}. 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 A0A0H4ISJ3_NEIG1 Unreviewed; 67 AA. AC A0A0H4ISJ3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63594.1}; GN ORFNames=NGO_00570 {ECO:0000313|EMBL:AKO63594.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63594.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63594.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63594; AKO63594; NGO_00570. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7539 MW; 9791989CB60B1330 CRC64; MNIMSTAGNI AKFPYSCHSV EKYSYLNGAL ESLSVRFVQA KKFPHQAGLD CSGEPHRFFN RPPYLSV // ID Q5F924_NEIG1 Unreviewed; 100 AA. AC Q5F924; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Primosomal replication protein n {ECO:0000256|SAAS:SAAS00194886}; GN ORFNames=NGO_0582 {ECO:0000313|EMBL:AAW89313.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89313.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3K8A} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=19906704; DOI=10.1093/nar/gkp1031; RA Dong J., George N.P., Duckett K.L., DeBeer M.A., Lopper M.E.; RT "The crystal structure of Neisseria gonorrhoeae PriB reveals RT mechanistic differences among bacterial DNA replication restart RT pathways."; RL Nucleic Acids Res. 38:499-509(2010). CC -!- FUNCTION: Binds single-stranded DNA at the primosome assembly site CC (PAS). {ECO:0000256|SAAS:SAAS00539216}. CC -!- SIMILARITY: Belongs to the PriB family. CC {ECO:0000256|SAAS:SAAS00539215}. CC -!- SIMILARITY: Contains SSB domain. {ECO:0000256|SAAS:SAAS00522018}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89313.1; -; Genomic_DNA. DR RefSeq; WP_003692950.1; NC_002946.2. DR RefSeq; YP_207725.1; NC_002946.2. DR PDB; 3K8A; X-ray; 2.70 A; A/B=1-100. DR PDBsum; 3K8A; -. DR ProteinModelPortal; Q5F924; -. DR DNASU; 3282384; -. DR EnsemblBacteria; AAW89313; AAW89313; NGO_0582. DR GeneID; 3282384; -. DR KEGG; ngo:NGO0582; -. DR PATRIC; 20334232; VBINeiGon24812_0688. DR HOGENOM; HOG000261222; -. DR KO; K02686; -. DR OMA; HESWQKE; -. DR OrthoDB; EOG654P86; -. DR BioCyc; NGON242231:GI2G-553-MONOMER; -. DR EvolutionaryTrace; Q5F924; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3K8A}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA replication {ECO:0000256|SAAS:SAAS00421442}; KW DNA-binding {ECO:0000256|SAAS:SAAS00522039}; KW Primosome {ECO:0000256|SAAS:SAAS00421430}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 100 AA; 11445 MW; 873F595F5DFCF363 CRC64; MGFTNLVSLA ALIEKAFPIR YTPAGIPVLD IILKHESWQE ENGQQCLVQL EIPARILGRQ AEEWQYRQGD CATVEGFLAQ KSRRSLMPML RIQNIKEYKG // ID A0A0H4IS38_NEIG1 Unreviewed; 192 AA. AC A0A0H4IS38; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Copper ABC transporter substrate-binding protein {ECO:0000313|EMBL:AKO63716.1}; GN ORFNames=NGO_07395 {ECO:0000313|EMBL:AKO63716.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63716.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63716.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63716; AKO63716; NGO_07395. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007742; NosD_dom. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR Pfam; PF05048; NosD; 1. DR SUPFAM; SSF51126; SSF51126; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 118 NosD. {ECO:0000259|Pfam:PF05048}. SQ SEQUENCE 192 AA; 21469 MW; 73E33C52F9814AFA CRC64; MLNYVNYSDI HDNIINKAGK CVFAYNANYD KLSANHFENC QIGMHFTAAI EGTSLHDNSF INNGSQVKYV STRFLDWSEG GHGNYWSDNS PFDLNGDGFG DSAYRPDGII DQIIWRAPVS RLLMNSPAIS IVKWAQAQFP AVLPGGVVDS KPLMKPYAPK IQTRYQAMKD ELLKEAETRQ SERGRAENGS LN // ID A0A0H4J5C0_NEIG1 Unreviewed; 255 AA. AC A0A0H4J5C0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:AKO63597.1}; GN ORFNames=NGO_00680 {ECO:0000313|EMBL:AKO63597.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63597.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63597.1; -; Genomic_DNA. DR RefSeq; WP_003694777.1; NC_002946.2. DR RefSeq; YP_009115478.1; NC_002946.2. DR EnsemblBacteria; AKO63597; AKO63597; NGO_00680. DR GeneID; 22847886; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005074; Peptidase_C39. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF03412; Peptidase_C39; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50990; PEPTIDASE_C39; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 20 139 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 255 AA; 28003 MW; 719DA4B446B3388A CRC64; MDYLQNLSLG LTKKLPVILQ TEVAECGLAC LAAVAGFYGF YTDLRALRSK YCLSLKGENL ADIVRFADDM GLTGRALRLD LDELGSLRLP CILHWDLNHF VVLESVSSDG AAVMDPASGR RKVKTEEISR KFTGIALELW PNTRFEAGEE KQEIRILPML RGISGLGRTL FQLLALAAAM EVFAFLQNVS FKIGRGESLA LIGRSGCGKS TLLDILSGNL PPESGKVMIN GHDIYSLPPR FIRNLSAMVR QDDVL // ID A0A0H4IVH0_NEIG1 Unreviewed; 1201 AA. AC A0A0H4IVH0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197}; GN ORFNames=NGO_08225 {ECO:0000313|EMBL:AKO63740.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63740.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AKO63740.1; -; Genomic_DNA. DR RefSeq; WP_025456515.1; NC_002946.2. DR RefSeq; YP_008914856.1; NC_002946.2. DR EnsemblBacteria; AKO63740; AKO63740; NGO_08225. DR GeneID; 19593002; -. DR KEGG; ngo:NGO1552a; -. DR UniPathway; UPA00261; UER00373. DR UniPathway; UPA00261; UER00374. DR Proteomes; UP000000535; 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:UP000000535}; 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 Proline metabolism {ECO:0000256|PIRNR:PIRNR000197}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 565 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; 129634 MW; 09EB45BAF882EBC3 CRC64; MFHFAFPAQT ALRQAITDAY RRNEIEAVQD MLQRAQMSDE ERNAASELAR RLVTQVRAGR TKAGGVDALM HEFSLSSEEG IALMCLAEAL LRIPDNATRD RLIADKISDG NWKSHLNNSP SLFVNAAAWG LLITGKLTAT NDKQMSSALG RLIGKGGAPL IRQGVNYAMR LLGKQFVTGQ TIEEALQNGK EREKMGYRFS FDMLGEAAYT QADADRYYRD YVEAIHAIGK DAAGQGVYEG NGISVKLSAI HPRYSRAQHG RVMGELLPRL KELFLLGKKY DIGINIDAEE ANRLELSLDL MEALVSDPDL AGYKGIGFVV QAYQKRCPFV IDYLIDLARR NNQKLMIRLV KGAYWDSEIK WAQVDGLNGY PTYTRKVHTD ISYLACACKL LSAQDAVFPQ FATHNAYTLG AIYQMGKGKD FEHQCLHGMG ETLYDQVVGP QNLGRRVRVY APVGTHETLL AYLVRRLLEN GANSSFVNQI VDENISIDRL IKSPFDTIAE QGIHLHNALP LPRDLYGKCR LNSQGVDLSN ENVLQQLQEQ MNKAAAQDFH AASIVNGKAR DVGEAQPIKN PADHGDVVGT VSFADAALAQ EAVGAAVAAF PEWSATPAAE RAACLRRFAD LLEQHTPALM MLAVREAGKT LNNAIAEVRE AVDFCRYYAN EAEHTLPQDA KAVGAIVAIS PWNFPLAIFT GEVVSALAAG NTVIAKPAEQ TSLIAGYAVS LMHEAGIPTS ALQLILGAGD TGAALTNDAS IGGVIFTGST EVARLINKAL AKRGDNPVLI AETGGQNAMI VDSTALAEQV CADVLNSAFD SAGQRCSALR ILCVQEDVAD RMLDMIKGAM DELVVGKPIQ LTTDVGPVID AEAQQNLLNH INKMKGVAKS YHEVKAAADV DSEKSTFVRP ILFELNNLNE LQREVFGPVL HVVRYRADEL DSVIDQINSK GYALTHGVHS RIEGTVRHIR SRIEAGNVYV NRNIVGAVVG VQPFGGHGLS GTGPKAGGSF YLQKLTRIPE WVAPTLSQIG QADEAALKRL EALIHKLPFN AEEKKAAAAA LGHARIRTLR RAETVLTGPT GERNSISWHA PKRVWIHGGS TVQAFAALTG LAASGVQAVV EPDSPLASYT ADLEGLLLVN GKPETAGISH VAALSPLDSA RKQELAAHDG ALIRVLPSEN GLDILQVFEE ISCSINTTAA GGNAGLMAVA D // ID A0A0H4ISQ6_NEIG1 Unreviewed; 105 AA. AC A0A0H4ISQ6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Baseplate protein {ECO:0000313|EMBL:AKO63649.1}; GN ORFNames=NGO_03845 {ECO:0000313|EMBL:AKO63649.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63649.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63649.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63649; AKO63649; NGO_03845. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006949; Baseplate_J-like. DR Pfam; PF04865; Baseplate_J; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 98 Baseplate_J. {ECO:0000259|Pfam:PF04865}. SQ SEQUENCE 105 AA; 11367 MW; C38BCE838AB53F47 CRC64; MRRAAGTVEV YIKTQSGTPD ETILTAAREY LPAETRRPLC DNVQVTAAQP KDTAVEYSAE YHPAANIQAE RQTACEALDN LWRQNAHIGA SVALSKIIGA LDTPA // ID A0A0H4IWF5_NEIG1 Unreviewed; 79 AA. AC A0A0H4IWF5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63763.1}; GN ORFNames=NGO_09000 {ECO:0000313|EMBL:AKO63763.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63763.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63763.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63763; AKO63763; NGO_09000. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 79 AA; 8771 MW; 83EAF0200DF945A9 CRC64; MSGVAVYLRN KNRIAIASQD ANLNSKGRFV SSGLNVGKQL TGSLGVEFDP YYRHRAIRKS AEFVSNTTKT KTDSEKFNE // ID A0A0H4IVL2_NEIG1 Unreviewed; 71 AA. AC A0A0H4IVL2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63790.1}; GN ORFNames=NGO_10515 {ECO:0000313|EMBL:AKO63790.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63790.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63790.1; -; Genomic_DNA. DR RefSeq; WP_002242092.1; NC_002946.2. DR RefSeq; YP_009115488.1; NC_002946.2. DR EnsemblBacteria; AKO63790; AKO63790; NGO_10515. DR GeneID; 22847896; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 8060 MW; 5655C7D408C1F67E CRC64; MFKLGVYACL GLFAGWVLLL IVQLWFSFLE AELFFKITLT MAGLFVIILA ALLVCGQYFS EKKMKDNGFI N // ID Q5F9T0_NEIG1 Unreviewed; 158 AA. AC Q5F9T0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 68. DE SubName: Full=Chorismate--pyruvate lyase {ECO:0000313|EMBL:AAW89057.2}; GN ORFNames=NGO_0310 {ECO:0000313|EMBL:AAW89057.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89057.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89057.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9T0; -. DR EnsemblBacteria; AAW89057; AAW89057; NGO_0310. DR PATRIC; 20333603; VBINeiGon24812_0381. DR HOGENOM; HOG000137785; -. DR OMA; MEHLFEE; -. DR OrthoDB; EOG6Z0QB1; -. DR BioCyc; NGON242231:GI2G-290-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00417425}; KW Lyase {ECO:0000256|SAAS:SAAS00417426, ECO:0000313|EMBL:AAW89057.2}; KW Pyruvate {ECO:0000256|SAAS:SAAS00417424, ECO:0000313|EMBL:AAW89057.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ubiquinone biosynthesis {ECO:0000256|SAAS:SAAS00417423}. SQ SEQUENCE 158 AA; 17609 MW; 8F64678C39AEEEB5 CRC64; MEHLFGKWLP DLPAPVSDGI DLPMSRLLKA RSLTAALCAL PHTFSVELLK LGEAETEYGR RRVRDVLLKL DGTAVVQARS ACSVGSAFWQ NILDCGTRPL GERLFQADLE GARSAFEFAV SSEGCGRYFA ARRSRFSHQG EEMLLTEYFL PELKRFIG // ID A0A0H4J5W3_NEIG1 Unreviewed; 202 AA. AC A0A0H4J5W3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63752.1}; GN ORFNames=NGO_08420 {ECO:0000313|EMBL:AKO63752.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63752.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63752.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63752; AKO63752; NGO_08420. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR028883; tRNA_aden_deaminase. DR Pfam; PF06255; DUF1020; 1. DR Pfam; PF14437; MafB19-deam; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 202 AA; 21386 MW; 6EC7719166156667 CRC64; MSYLSDRENS IREAVDRWIQ ENPNAAETVE AVFNVAAAKV AKLAKAAKPG KAAVSGDFSI SYKNFSTVKP KVIAKGTING KTFRDVNQSA KIGSPDSPTL IAQRVNAKIQ ADGKPRPNAT VANSHAEIGV IQQAYNAGET KGASMTMTVS GKDVCGYCKG DIAAAAQASG LKSLTVNATD NVTGKNKTYY WTPGMKSIKE RK // ID Q5FAJ7_NEIG1 Unreviewed; 257 AA. AC Q5FAJ7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Triosephosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}; DE Short=TIM {ECO:0000256|HAMAP-Rule:MF_00147}; DE Short=TPI {ECO:0000256|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000256|HAMAP-Rule:MF_00147}; GN ORFNames=NGO_0017 {ECO:0000313|EMBL:AAW88786.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88786.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000256|HAMAP- CC Rule:MF_00147}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00525314}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, CC ECO:0000256|SAAS:SAAS00498179}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00147, ECO:0000256|RuleBase:RU363013, CC ECO:0000256|SAAS:SAAS00498183}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498221}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, CC ECO:0000256|RuleBase:RU363013}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000256|HAMAP-Rule:MF_00147, ECO:0000256|RuleBase:RU363013, CC ECO:0000256|SAAS:SAAS00541575}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88786.1; -; Genomic_DNA. DR RefSeq; WP_003687222.1; NC_002946.2. DR RefSeq; YP_207198.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ7; -. DR EnsemblBacteria; AAW88786; AAW88786; NGO_0017. DR GeneID; 3283061; -. DR KEGG; ngo:NGO0017; -. DR PATRIC; 20332864; VBINeiGon24812_0017. DR HOGENOM; HOG000226413; -. DR KO; K01803; -. DR OMA; CEMIRIA; -. DR OrthoDB; EOG66QM23; -. DR BioCyc; NGON242231:GI2G-14-MONOMER; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; 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 {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013}; KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498237}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498222}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498630, KW ECO:0000313|EMBL:AAW88786.1}; KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00147, KW ECO:0000256|RuleBase:RU363013, ECO:0000256|SAAS:SAAS00498169}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 257 AA; 28294 MW; 117114F01B6C0504 CRC64; MYRQIGMWDQ KWVIGNWKMN GRLQNNNALM HRFRILPTAE RVLIGLAAPT VYLLQLHNAM QIVLNNRILT CAQDVSRFPD NGAYTGEVSA EMLADTGTDI VLIGHSERSL YFGEKNEIQR RKMENVLNVG LIPLLCVGES LEERETGKEH EVIAHQLSIL QGLDTKNIAV AYEPVWAIGT GKVATVEQIA DMHAFIYKEI LSLCGSDVKI RVLYGGSVKA DNAADIFAVP YVDGALVGGA SLSYDSFTAI ISAAQNA // ID A0A0H4ISR9_NEIG1 Unreviewed; 123 AA. AC A0A0H4ISR9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63659.1}; GN ORFNames=NGO_04415 {ECO:0000313|EMBL:AKO63659.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63659.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63659.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63659; AKO63659; NGO_04415. DR Proteomes; UP000000535; 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; PF06472; ABC_membrane_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 14 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 114 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 35 122 ABC transmembrane type-1. FT {ECO:0000259|Pfam:PF06472}. SQ SEQUENCE 123 AA; 13904 MW; F15E5D3404D0380C CRC64; MQNRQTELYS TPSWLLQTLL MITAASAVIL FFARNTRLGR EFAYILRLCL TPKSTVKVLL LITAMVTLLL TEVRLNVLST FMSKGLYDSM QDLNASAFWM FAAMNAGVVL IRAFNNVVND FLD // ID Q5F7L8_NEIG1 Unreviewed; 268 AA. AC Q5F7L8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW89819.1}; GN ORFNames=NGO_1152 {ECO:0000313|EMBL:AAW89819.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89819.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89819.1; -; Genomic_DNA. DR RefSeq; WP_003689749.1; NC_002946.2. DR RefSeq; YP_208231.1; NC_002946.2. DR ProteinModelPortal; Q5F7L8; -. DR EnsemblBacteria; AAW89819; AAW89819; NGO_1152. DR GeneID; 3282217; -. DR KEGG; ngo:NGO1152; -. DR PATRIC; 20335566; VBINeiGon24812_1348. DR HOGENOM; HOG000031895; -. DR KO; K02030; -. DR OMA; GYVAKND; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; NGON242231:GI2G-1065-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256057. FT DOMAIN 38 262 PBPb. {ECO:0000259|SMART:SM00062}. SQ SEQUENCE 268 AA; 28859 MW; 9C9ACA23F247CAC0 CRC64; MNMKKWIAAA LACSALALSA CGGQGKDAAA PAANPGKVYR VASNAEFAPF ESLDSKGNVE GFDVDLMNAM AKAGNFKIEF KHQPWDSLFP ALNNGDADVV MSGVTITDDR KQSMDFSDPY FEITQVVLVP KGKKVSSSED LKKMNKVGVV TGHTGDFSVS KLLGNDNPKI ARFENVPLII KELENGGLDS VVSDSAVIAN YVKNNPAKGM DFVTLPDFTT EHYGIAVRKG DEATVKMLND ALEKVRESGE YDKIYAKYFA KEGGQAAK // ID A0A0H4IRM1_NEIG1 Unreviewed; 87 AA. AC A0A0H4IRM1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Myo-inositol transporter permease {ECO:0000313|EMBL:AKO63606.1}; GN ORFNames=NGO_01075 {ECO:0000313|EMBL:AKO63606.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63606.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63606.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63606; AKO63606; NGO_01075. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 67 86 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 87 AA; 10190 MW; 98EB6BBE443A0123 CRC64; MSNPKYVKKE TNPLAYFKRF VPPLSRFYLS GQPLRRLKNS GFRLCSGLKP MAGILFFSGI SFVKQMVLNR LMFYAVFFLF LFFGILF // ID Q5F578_NEIG1 Unreviewed; 109 AA. AC Q5F578; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Alkylphosphonate utilization protein {ECO:0000313|EMBL:AAW90659.1}; GN ORFNames=NGO_2052 {ECO:0000313|EMBL:AAW90659.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90659.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90659.1; -; Genomic_DNA. DR RefSeq; WP_003686995.1; NC_002946.2. DR RefSeq; YP_209071.1; NC_002946.2. DR ProteinModelPortal; Q5F578; -. DR SMR; Q5F578; 2-108. DR EnsemblBacteria; AAW90659; AAW90659; NGO_2052. DR GeneID; 3282733; -. DR KEGG; ngo:NGO2052; -. DR PATRIC; 20337903; VBINeiGon24812_2474. DR HOGENOM; HOG000228486; -. DR KO; K06193; -. DR OMA; SCLYEWN; -. DR OrthoDB; EOG6J752H; -. DR BioCyc; NGON242231:GI2G-1953-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 11732 MW; 0EB45C69F709F092 CRC64; MSLPPCPQCA SEYTYEDGGQ YICPECAHEW NETESAADLA AQVRDANGAA LQNGDTVILI KDLKVKGSSM TIKQGTKVKG IRLQEGDHNI GCKIDGSAMN LKSEFVKKA // ID A0A0H4IVK4_NEIG1 Unreviewed; 126 AA. AC A0A0H4IVK4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63780.1}; GN ORFNames=NGO_09970 {ECO:0000313|EMBL:AKO63780.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63780.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63780.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63780; AKO63780; NGO_09970. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 126 AA; 14036 MW; C62E344A90CE48F0 CRC64; MYDGEAGAGE SYFRKGRRGR SAAGKAAVFG LLKRNGKVCT VTVGHSNRYF IAYYPRTGET RQHCLYGLFV VTMYQIVSGF GRFRINRGTH FAERQNHINA IGNFWNRANV ICASLTAFPK SISGCI // ID A0A0H4IVI1_NEIG1 Unreviewed; 96 AA. AC A0A0H4IVI1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63755.1}; GN ORFNames=NGO_08550 {ECO:0000313|EMBL:AKO63755.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63755.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63755.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63755; AKO63755; NGO_08550. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 10853 MW; 2627BCE2B1BE6691 CRC64; MAKALEIISP DEIYSDLIFK DPVPPHTIYT ELMKLVGRNA GNERIADRAF DFFSPALMDD SATEEQYNAL YDLTLLEEPG MELDKDEITA LINSLK // ID Q5F801_NEIG1 Unreviewed; 166 AA. AC Q5F801; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89686.2}; GN ORFNames=NGO_1003 {ECO:0000313|EMBL:AAW89686.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89686.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89686.2; -; Genomic_DNA. DR DNASU; 3282188; -. DR EnsemblBacteria; AAW89686; AAW89686; NGO_1003. DR PATRIC; 20335206; VBINeiGon24812_1171. DR HOGENOM; HOG000009740; -. DR OMA; VYRVHGF; -. DR OrthoDB; EOG6VMTJ9; -. DR BioCyc; NGON242231:GI2G-929-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006482; Cas7_Csh2/Csh2. DR InterPro; IPR013418; CRISPR-assoc_prot_Csd2. DR Pfam; PF05107; Cas_Cas7; 1. DR TIGRFAMs; TIGR02589; cas_Csd2; 1. DR TIGRFAMs; TIGR01595; cas_CT1132; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 166 AA; 18145 MW; 7EA96A13AF1B990E CRC64; MTTEVNSGQV RGPVQLAFAQ SIDPIVPPEV SITRMAVTNE KDLEKERTMG RKYIVPYVVY RVHGFISANL AAKTGFSDDD LAKLWQALTL MFEHDRSAAR GEMAARKLVV FKHDSALGSQ PAHKLFDAVK VERVNGESGT PASGFGDYKI SVVSDGLNGV SVEEYL // ID A0A0H4IV69_NEIG1 Unreviewed; 80 AA. AC A0A0H4IV69; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63675.1}; GN ORFNames=NGO_05145 {ECO:0000313|EMBL:AKO63675.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63675.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63675.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63675; AKO63675; NGO_05145. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 9238 MW; 1A1A528CA11136CE CRC64; MDLDFFHRTR ARYLELVKDN PKAVVINAEQ TIELVQAEIE SAVKIGGNYT KNDRTFKIIK SAVNFPADFI LLQFNLKRPL // ID A0A0H4IW24_NEIG1 Unreviewed; 149 AA. AC A0A0H4IW24; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63633.1}; GN ORFNames=NGO_03125 {ECO:0000313|EMBL:AKO63633.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63633.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63633.1; -; Genomic_DNA. DR RefSeq; WP_030003511.1; NC_002946.2. DR RefSeq; YP_008914849.1; NC_002946.2. DR EnsemblBacteria; AKO63633; AKO63633; NGO_03125. DR GeneID; 19592993; -. DR KEGG; ngo:NGO0590a; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 51 113 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 149 AA; 17010 MW; 5B28F9AEE0C015F4 CRC64; MSTFFRQTAQ AMTAKHIGRF PLSELDQVID WQPIEQYLIR QKTRYLRDRR GRPAHPLSSM FKAVLPGQWH SLSDPELEHS LITRIGFNLF CRFDGPGIPG CSTLCRYRKF RYARAAYFGL LKVGVQSHLK AMCLNLLKAA NRLSAPAAA // ID Q5F6Y6_NEIG1 Unreviewed; 366 AA. AC Q5F6Y6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Aminomethyltransferase {ECO:0000256|HAMAP-Rule:MF_00259, ECO:0000256|RuleBase:RU003981}; DE EC=2.1.2.10 {ECO:0000256|HAMAP-Rule:MF_00259, ECO:0000256|RuleBase:RU003981}; DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|HAMAP-Rule:MF_00259}; GN Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259}; GN ORFNames=NGO_1406 {ECO:0000313|EMBL:AAW90051.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90051.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of CC glycine. {ECO:0000256|HAMAP-Rule:MF_00259, CC ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00001709}. CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10- CC methylenetetrahydrofolate + NH(3). {ECO:0000256|HAMAP- CC Rule:MF_00259, ECO:0000256|RuleBase:RU003981, CC ECO:0000256|SAAS:SAAS00312915}. CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259, CC ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00001757}. CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|HAMAP- CC Rule:MF_00259, ECO:0000256|RuleBase:RU003980, CC ECO:0000256|SAAS:SAAS00567672}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90051.1; -; Genomic_DNA. DR RefSeq; WP_003693701.1; NC_002946.2. DR RefSeq; YP_208463.1; NC_002946.2. DR ProteinModelPortal; Q5F6Y6; -. DR SMR; Q5F6Y6; 7-364. DR EnsemblBacteria; AAW90051; AAW90051; NGO_1406. DR GeneID; 3281180; -. DR KEGG; ngo:NGO1406; -. DR PATRIC; 20336217; VBINeiGon24812_1657. DR HOGENOM; HOG000239381; -. DR KO; K00605; -. DR OMA; LGWLVHL; -. DR OrthoDB; EOG6T1WS5; -. DR BioCyc; NGON242231:GI2G-1316-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00259, KW ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00416033}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00259, KW ECO:0000256|RuleBase:RU003981, ECO:0000256|SAAS:SAAS00416033}. FT DOMAIN 10 257 GCV_T. {ECO:0000259|Pfam:PF01571}. FT DOMAIN 266 354 GCV_T_C. {ECO:0000259|Pfam:PF08669}. SQ SEQUENCE 366 AA; 39637 MW; C283FAB0AB65BC42 CRC64; MTALKTTPFH QAHQDAGAKP VDFAGWELPI HYGSQIAEHE AVRTDAGMFD VSHMLVTDVV GANAKAFFRK LIANDVAKLA FVGKALYSAL LNDNGGVIDD LIVYRTNEAE TQYRIVSNGA TREKDTAQFH KVGQEFGVAF NPRYDLGMLA VQGPKAIEKL LTVKPEWADV IHGLKPFQGA DLGNDWFVAR TGYTGEDGVE VILPDTEAVA FFKALQTAGV QPCGLGARDT LRMEAGMNLY GNDMDDDTSP LEAGMGRTVD LKDESRDFVG KAALLALKEK GVAVKQVGLL LEKGGILRAH MEVLTDKGKG ETTSGVFSPS LKQSIAIARV PKDFDGDTAK VLIRGKEADV RVLKLPFVRS GQKQFD // ID A0A0H4ISM2_NEIG1 Unreviewed; 207 AA. AC A0A0H4ISM2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Restriction endonuclease subunit S {ECO:0000313|EMBL:AKO63619.1}; GN ORFNames=NGO_02160 {ECO:0000313|EMBL:AKO63619.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63619.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63619.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63619; AKO63619; NGO_02160. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AKO63619.1}; KW Hydrolase {ECO:0000313|EMBL:AKO63619.1}; KW Nuclease {ECO:0000313|EMBL:AKO63619.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 21 186 Methylase_S. {ECO:0000259|Pfam:PF01420}. SQ SEQUENCE 207 AA; 23440 MW; 3B2E5906D1471458 CRC64; MTIKSGGIAD GYQCRLKNVV WKTLGEVAEY SKNRICSDKL NEHNYVGVDN LLQNREGKKL SGYVPSEGKM TEYIVNDILI GNIRPYLKKI WQADCTGGTN GDVLVIRVTD EKVNPKYLYQ VLADDKFFAF NMKHAKGAKM PRGSKAAIMQ YKIPIPPLPE QEKIVAILGK FDTLTHSVSE GLPHEIALRR KQYEYYREQL LAFPKAA // ID A0A0H4IWI5_NEIG1 Unreviewed; 117 AA. AC A0A0H4IWI5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Cytochrome B561 {ECO:0000313|EMBL:AKO63798.1}; GN ORFNames=NGO_10685 {ECO:0000313|EMBL:AKO63798.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63798.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63798.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63798; AKO63798; NGO_10685. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 23 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 103 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 117 AA; 12749 MW; A63A087C901C6A29 CRC64; MIALRIVWAV ANRAKRPQSD SKAAAAGHGI LYLLMLAVPV IGMIRQYGGG RGPLKVFGVE VMQGSPEKIE WMANLGNTFH GNLGWLLFAA VVGHVAMVVV HRVQGKDVLY RMTGRVR // ID Q5F533_NEIG1 Unreviewed; 930 AA. AC Q5F533; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 89. DE SubName: Full=DNA polymerase I {ECO:0000313|EMBL:AAW90704.1}; GN ORFNames=NGO_2103 {ECO:0000313|EMBL:AAW90704.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90704.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90704.1; -; Genomic_DNA. DR RefSeq; WP_003687077.1; NC_002946.2. DR RefSeq; YP_209116.1; NC_002946.2. DR ProteinModelPortal; Q5F533; -. DR SMR; Q5F533; 330-930. DR EnsemblBacteria; AAW90704; AAW90704; NGO_2103. DR GeneID; 3282814; -. DR KEGG; ngo:NGO2103; -. DR PATRIC; 20338043; VBINeiGon24812_2544. DR HOGENOM; HOG000020999; -. DR KO; K02335; -. DR OMA; CFDTETT; -. DR OrthoDB; EOG6SJJH7; -. DR BioCyc; NGON242231:GI2G-1998-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00427491}; KW Nuclease {ECO:0000256|SAAS:SAAS00427491}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 264 53EXOc. {ECO:0000259|SMART:SM00475}. FT DOMAIN 332 518 3'-5' exonuclease. FT {ECO:0000259|SMART:SM00474}. FT DOMAIN 687 892 POLAc. {ECO:0000259|SMART:SM00482}. SQ SEQUENCE 930 AA; 102135 MW; 49A1A7F1C2A54699 CRC64; MSNRPTLLLV DGSSYLYRAY HAMGQNLTAP DGAPTGALYG VLNMLRRLRS EYPHDYCAVV FDAKGKNFRH QMFEEYKATR PPMPDDLRPQ AEALPDLVRL TGWPVLVIGQ VEADDVIGTL AKQGAEHGLR VIVSTGDKDM AQLVDERVTL VNTMSGETLD IEGVKAKFGV RPDQIRDYLA LIGDKVDNVP GVEKCGPKTA VKWLEAYGSL QGVMEHAPEI KGKVGENLQA ALPQLPLSYD LVTIKTDVDL HTELSDGIES LRRTAPKWAQ LAVDFKRWGF RTWLKEAESN MNTGSTDDLF GSDSIGEQAA LNAEIPSEKR AEKATAPEKL DYQAVTTEAQ FAALLDKLAK ADTIGIDTET TSLDAMNAEL VGISIAFQAG EAVYIPVGHS LTAAPEQLDL QDVLGRLKPH LENPALKKIG QNLKYDQHVF ANYGIALNNI AGDAMLASYI IESHLGHGLD ELSGRWLGLE TITYESLCGK GAKQISFADV AIGQATEYAA QDADFALRLE ARLRAQMDDK QLEMYEKMEL PVAQVLFEME CNGVQIDRAE LARQSAELGA ELMKLEQEAY AAAGQPFNLN SPKQLQEILF DKMGIPTKGL KKTAKGGIST NEAVLEQLAP DYPLPKIILQ NRSLAKLKST YTDKLPEMIS PRDNRVHTTY AQAVAITGRL ASNNPNLQNI PIRTAEGRRV RRAFTAPPGS VIVSADYSQI ELRIMAHLSG DKTLIAAFQS GEDVHRRTAA EVFGTAPENV SPEQRRYAKT INFGLIYGMG QYGLAKSLGI DNLSAKNFID RYFARYPGVA EYMQRTKEQA AAQGYVETLF GRRLYLPDIR NKNANARAGA ERAAINAPMQ GTASDLIKRA MINVRNWLSD GIGSKLVMQV HDELVLEVVE TELDFVKEKL PQIMAKVDGG LLDVPLVAEV GVGENWEEAH // ID Q5F9N3_NEIG1 Unreviewed; 444 AA. AC Q5F9N3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 54. DE SubName: Full=Uroporphyrin-III methyltransferase {ECO:0000313|EMBL:AAW89104.2}; GN ORFNames=NGO_0360 {ECO:0000313|EMBL:AAW89104.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89104.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89104.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89104; AAW89104; NGO_0360. DR PATRIC; 20333715; VBINeiGon24812_0435. DR HOGENOM; HOG000218864; -. DR OMA; VSASWWQ; -. DR OrthoDB; EOG6X10V3; -. DR BioCyc; NGON242231:GI2G-339-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000313|EMBL:AAW89104.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89104.2}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 73 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 444 AA; 48355 MW; 3557257F3F943745 CRC64; MGEPENKSSE PVREIQASKE MPSETSSPRK ENETEVHIPA APFIVKQSGS NALAACALVL AALGLGASGF LFVQGQNVLK NQELAFNQKI DKAALGESEN AALLKDNLNR QSAIQSELDR LDSGVKANGE QILMTQKAYR ELTKGRADWL VDETETILNL AAQQLVLTGN IQTAVGVLEH IDSRLSRFDQ AELLPIKQAV SSDLAELKNR PYVDISGTAL RLDRLETAVS GLPLILDGVL KPGVQARNEA VSASWWQNVW EKSLGTLKGL VEIRRLENND AMLISPEQAY FVRENLRLRL LDARTALMQR NGEVYQGDLN NAEAAVRQYF DAKSPATQSW LKELAELKTL DVRMTADDGL KTSLNAVRAY RDGTRMTAAE NQEAEQAASE PANENTASEP AAASDVKAIE APSLPSERKP EQPAKKQPAP EKAGRSPSAK GERA // ID Q5FAJ5_NEIG1 Unreviewed; 218 AA. AC Q5FAJ5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000313|EMBL:AAW88788.1}; GN ORFNames=NGO_0019 {ECO:0000313|EMBL:AAW88788.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88788.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88788.1; -; Genomic_DNA. DR RefSeq; WP_003687226.1; NC_002946.2. DR RefSeq; YP_207200.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ5; -. DR EnsemblBacteria; AAW88788; AAW88788; NGO_0019. DR GeneID; 3283075; -. DR KEGG; ngo:NGO0019; -. DR PATRIC; 20332868; VBINeiGon24812_0019. DR HOGENOM; HOG000257190; -. DR KO; K00573; -. DR OMA; ILRHEFV; -. DR OrthoDB; EOG644ZP2; -. DR BioCyc; NGON242231:GI2G-16-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro. 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW88788.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88788.1}. SQ SEQUENCE 218 AA; 24083 MW; F7416907651B2574 CRC64; MDFEKARFNM VEQQIRPWDV LDFDVLDALE EIPRELFADE SLQGLAYADM ELPLANGHKM LEPKVVARLA QGLKLTKNDT VLEIGTGSGY ATALLAKLAG RVVSDDIDAE RQKRAKAVLD GLSLENIDYV QNNGLTELSA GAPFDAVYVG GAVTLVPEVL KEQLKDGGRM AVIVGRRPVQ RALLITRRGD VFEEKVLFDT LVAHLDDKDA HPFDSFNF // ID A0A0H4IT49_NEIG1 Unreviewed; 296 AA. AC A0A0H4IT49; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Maltose phosphorylase {ECO:0000313|EMBL:AKO63744.1}; GN ORFNames=NGO_08300 {ECO:0000313|EMBL:AKO63744.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63744.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63744.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63744; AKO63744; NGO_08300. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR012341; 6hp_glycosidase. DR InterPro; IPR005194; Glyco_hydro_65_C. DR InterPro; IPR005195; Glyco_hydro_65_M. DR Pfam; PF03633; Glyco_hydro_65C; 1. DR Pfam; PF03632; Glyco_hydro_65m; 1. DR SUPFAM; SSF48208; SSF48208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 188 Glyco_hydro_65m. FT {ECO:0000259|Pfam:PF03632}. FT DOMAIN 192 219 Glyco_hydro_65C. FT {ECO:0000259|Pfam:PF03633}. SQ SEQUENCE 296 AA; 34625 MW; 6E02A79F97ACEC74 CRC64; MGYTREALAK YPRPGSNVSA AELEKWADIS ANMYRPHDEE LGVFVQHDGF LDKDIRPVSA LSPDDLPLNQ KWSWDKILRS PFIKQADVLQ GIYFFGDRFD MDEKRRNFDF YEPMTVHESS LSPCIHSILA AELGKEEKAV EMYRRTARLD LDDYNNDTED GLHITSMTGS WLAIVQGFAQ MKTWGGKLSF APFLPSAWTG YAFHINYRGR LIKVAVGKKR RLHPAQRRSA RIAGVRQRHH AQRQPHRCIG KIRRAQNDFY RSALRSRRRD YRYRRIPLPR MEKACRRIGH RHRPQV // ID A0A0H4IT46_NEIG1 Unreviewed; 48 AA. AC A0A0H4IT46; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Proline dehydrogenase {ECO:0000313|EMBL:AKO63739.1}; GN ORFNames=NGO_08220 {ECO:0000313|EMBL:AKO63739.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63739.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63739.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63739; AKO63739; NGO_08220. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 42 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 48 AA; 5613 MW; 5ACCB1AF06922458 CRC64; MPAYRPYLCF TRFIFKETEA PILPAFEALY FICGFITILP YSDRTDAV // ID Q5F654_NEIG1 Unreviewed; 210 AA. AC Q5F654; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015}; DE EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015}; GN ORFNames=NGO_1712 {ECO:0000313|EMBL:AAW90333.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90333.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90333.1; -; Genomic_DNA. DR RefSeq; WP_003705241.1; NC_002946.2. DR RefSeq; YP_208745.1; NC_002946.2. DR ProteinModelPortal; Q5F654; -. DR EnsemblBacteria; AAW90333; AAW90333; NGO_1712. DR GeneID; 3281343; -. DR KEGG; ngo:NGO1712; -. DR PATRIC; 20337016; VBINeiGon24812_2048. DR HOGENOM; HOG000156897; -. DR KO; K06966; -. DR OMA; DHADYAF; -. DR OrthoDB; EOG6DRPKX; -. DR BioCyc; NGON242231:GI2G-1608-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-EC. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Cytokinin biosynthesis {ECO:0000256|RuleBase:RU363015}; KW Hydrolase {ECO:0000256|RuleBase:RU363015}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90333.1}. SQ SEQUENCE 210 AA; 22726 MW; 48BF4A9A0CF75FE9 CRC64; MENVNRVPEQ ARYDAECRQA DEALADVFPA VSIFGSARTP QDHADYAFAC RLARRLSDSG IAVISGGGPG IMEAANKGAF AGKSVSVGLN IALPHEQKPN PYQDIALRFS RFAERKAVFF RYSQAYVVMP GGFGTLDELF EILTLVQTGK VPPRPVVLVG KAFWSGLAEW INAQLLARGM ISEGAASLFS ISDDEDEIIA YLSEHGLQTA // ID A0A0H4IWA5_NEIG1 Unreviewed; 126 AA. AC A0A0H4IWA5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63713.1}; GN ORFNames=NGO_07165 {ECO:0000313|EMBL:AKO63713.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63713.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63713.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63713; AKO63713; NGO_07165. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0017013; P:protein flavinylation; IEA:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR019546; TAT_signal_bac_arc. DR Pfam; PF02424; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 126 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206264. SQ SEQUENCE 126 AA; 13936 MW; 9BA242E854EB3444 CRC64; MGRHFGRRRF LTAAAVAVAG AAVSFLPNPF AAGGEKRNMD KKRDENVFFW KGVALGSGAE LRLFGVDDRQ AADLVNKVLA EVARLEKMFS LYREDSLISR LNRDGYLTSP PADFLELLSL AAIFTR // ID Q5F7H1_NEIG1 Unreviewed; 949 AA. AC Q5F7H1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=UvrABC system protein A {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00088996}; DE Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205}; DE AltName: Full=Excinuclease ABC subunit A {ECO:0000256|HAMAP-Rule:MF_00205}; GN Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205}; GN ORFNames=NGO_1207 {ECO:0000313|EMBL:AAW89866.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89866.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00571360}. CC -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for CC lesions. {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00571359}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00089096}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA CC family. {ECO:0000256|HAMAP-Rule:MF_00205, CC ECO:0000256|SAAS:SAAS00571366}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000256|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; AE004969; AAW89866.1; -; Genomic_DNA. DR RefSeq; WP_010951215.1; NC_002946.2. DR RefSeq; YP_208278.1; NC_002946.2. DR ProteinModelPortal; Q5F7H1; -. DR SMR; Q5F7H1; 13-949. DR EnsemblBacteria; AAW89866; AAW89866; NGO_1207. DR GeneID; 3282862; -. DR KEGG; ngo:NGO1207; -. DR PATRIC; 20335715; VBINeiGon24812_1416. DR HOGENOM; HOG000050448; -. DR KO; K03701; -. DR OMA; GAIKGWD; -. DR OrthoDB; EOG6QK4PS; -. DR BioCyc; NGON242231:GI2G-1118-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461349}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461486}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461435}; KW DNA excision {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461384}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461435}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461351}; KW Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461435}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461452}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461349}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461462}; KW SOS response {ECO:0000256|HAMAP-Rule:MF_00205}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00205, ECO:0000256|SAAS:SAAS00461452}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00205, KW ECO:0000256|SAAS:SAAS00461452}. FT DOMAIN 319 596 ABC transporter 1. {ECO:0000256|HAMAP- FT Rule:MF_00205}. FT DOMAIN 616 945 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 616 945 ABC transporter 2. {ECO:0000256|HAMAP- FT Rule:MF_00205}. FT NP_BIND 42 49 ATP. {ECO:0000256|HAMAP-Rule:MF_00205}. FT ZN_FING 262 289 C4-type. {ECO:0000256|HAMAP- FT Rule:MF_00205}. FT NP_BIND 649 656 ATP. {ECO:0000256|HAMAP-Rule:MF_00205}. FT ZN_FING 748 774 C4-type. {ECO:0000256|HAMAP- FT Rule:MF_00205}. SQ SEQUENCE 949 AA; 105477 MW; 7FA25B3BA71F8EBB CRC64; MCNHHPRHSH DNDTIRIRGA RTHNLKNIDL DIPRHKLVVV TGLSGSGKSS LAFDTLYAEG QRRYVESLSA YARQFLQMMD KPDVDLIEGL SPAISIEQKS TSHNPRSTVG TVTEIHDYLR LLYARVGTPY CPEHKLPLSS QTVSQMVDAV LKLPEDTRVM ILGPAVRERK GEFVDFFADL QAQGFARVRV DGEVYQLDEV PKLEKNIKHN IDVVIDRVKV KADIKQRLAE SFETALRHGN ERALAMEMDS GEEHWFSARF ACPVCSYSLP ELEPRLFSFN NPMGSCPTCD GLGNTNFFDP EKVVAHPELS LATGAIDGWD KRNQFYFQMI QSLAHHYKFD VNVAWETLPE KVKKVVLHGS GKEVIDFTYL SERGTTFNRS HAFEGIIPNL ERRYRETDSE TVREKLREYQ NHRACPSCGG ARLRKEARYV YVGGEPLHEV SAWPLTKTHR FFETLDLDGN KKQIAEKILK EITERLGFLI NVGLDYLNLS RSAETLSGGE AQRIRLASQI GSGLTGVMYV LDEPSIGLHQ RDNDRLLATL KRLRDLGNSV IVVEHDEDAI READFVVDMG PGAGEHGGNV LIADTPENVA KCEKSVTGQY LGGKKSIAVP SERTPVNPGR MLVLKGARGN NLKNVTLELP LGLITCITGV SGSGKSTLIN DTLAKITARE LNRAQEEPAP YDDIRGLEHL DKVINVDQSP IGRTPRSNPA TYTGLFTPIR ELFAGVPLSR ERGYNVGRFS FNVKGGRCEA CQGDGVIKVE MHFLPDVYVP CEVCHGKRYN RETLEIQYKG KNISQVLDMT VEEAREFFDA VPTVSRKLQT LMDVGLGYIR LGQSATTLSG GEAQRVKLAL ELSKRDTGRT LYILDEPTTG LHFADIALLL EVIGRLKGKG NSIVIIEHNL DVIKTADWIV DLGPEGGDGG GKVIAKGSPE EVAKVKGSYT GKYLKVVLK // ID A0A0H4IS04_NEIG1 Unreviewed; 60 AA. AC A0A0H4IS04; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63706.1}; GN ORFNames=NGO_06845 {ECO:0000313|EMBL:AKO63706.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63706.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63706.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63706; AKO63706; NGO_06845. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 60 AA; 6641 MW; A89D28A47FD459EA CRC64; MQTDYAHPAV GIADIGHLVV FCGYPLLAGN QPRSFPAYQV AHTVRHRRFR SGNGLRAAFM // ID A0A0H4IVK8_NEIG1 Unreviewed; 149 AA. AC A0A0H4IVK8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63785.1}; GN ORFNames=NGO_10180 {ECO:0000313|EMBL:AKO63785.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63785.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63785.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63785; AKO63785; NGO_10180. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008490; Transposase_InsH_N. DR Pfam; PF05598; DUF772; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 51 113 DUF772. {ECO:0000259|Pfam:PF05598}. SQ SEQUENCE 149 AA; 17035 MW; 14D32F05F6B55ED5 CRC64; MSTFFRQTAQ AMTAKHIGRF PLLELDQVID WQPIEQYLNR QKTRYLRDRR GRPAYPLSSM FKAVLPGQWH SLSDPELEHS LITRIGFNLF CRFDGPGIPG CSTLCRYRKF RYARAAYFGL LKVGAQSHLK AMCLNLLKAA NRLSAPAAA // ID Q5F628_NEIG1 Unreviewed; 498 AA. AC Q5F628; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=NADH:ubiquinone oxidoreductase subunit M {ECO:0000313|EMBL:AAW90359.1}; DE EC=1.6.5.11 {ECO:0000313|EMBL:AAW90359.1}; GN ORFNames=NGO_1738 {ECO:0000313|EMBL:AAW90359.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90359.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90359.1; -; Genomic_DNA. DR RefSeq; WP_003691918.1; NC_002946.2. DR RefSeq; YP_208771.1; NC_002946.2. DR EnsemblBacteria; AAW90359; AAW90359; NGO_1738. DR GeneID; 3281183; -. DR KEGG; ngo:NGO1738; -. DR PATRIC; 20337074; VBINeiGon24812_2077. DR HOGENOM; HOG000100683; -. DR KO; K00342; -. DR OMA; AIMLKIG; -. DR OrthoDB; EOG647TZ6; -. DR BioCyc; NGON242231:GI2G-1634-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000313|EMBL:AAW90359.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AAW90359.1}. 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; 54557 MW; 63005AC2B6B4D3E8 CRC64; MFSNYLLSLA IWIPIAAGVL VLATGKDSRA PLARVLAFMG ALAGFLVTLP LFTGFDRLSG GYQFTEFHEW IPLLKINYAL GVDGISVLFI ILNAFITLLV VLAGWEVIQK RPAQYMAAFL MMSGLINGAF AAQDAILFYV FFEGMLIPLY LIIGVWGGPR RVYASVKLFL YTLTGSLLML VAMVYLYYQT GSFSIVDFQN IKQIPLGVQQ LLFVAFFLSF AVKVPMFPVH TWLPDAHVEA PTGGSMVLAA ITLKLGAYGF LRFILPIMPD AARYFAPVII VLSLIAVIYI GMVALVQTDM KKLVAYSSIS HMGFVTLGMF LFVDGQLDDW ALKGAVIQMI SHGFVSAAMF MCIGVMYDRL HTRNIADYGG VVNVMPKFAA FMMLFGMANA GLPATSGFVG EFMVVMGAVK VNFWVGALAA MTLIYGASYT LWMYKRVIFG AIHNPHVAEM KDINCREFAI LAVLAVAVLG MGLYPNAFIE VVHQAANDLI AHVAQSKI // ID Q5F9S4_NEIG1 Unreviewed; 313 AA. AC Q5F9S4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=Ribosome biogenesis GTPase A {ECO:0000256|PIRNR:PIRNR006230}; GN ORFNames=NGO_0316 {ECO:0000313|EMBL:AAW89063.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89063.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for a late step of 50S ribosomal subunit CC assembly. Has GTPase activity. {ECO:0000256|PIRNR:PIRNR006230}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006230}. CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC MTG1 subfamily. {ECO:0000256|PIRNR:PIRNR006230}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89063.1; -; Genomic_DNA. DR RefSeq; WP_003687704.1; NC_002946.2. DR RefSeq; YP_207475.1; NC_002946.2. DR ProteinModelPortal; Q5F9S4; -. DR EnsemblBacteria; AAW89063; AAW89063; NGO_0316. DR GeneID; 3281727; -. DR KEGG; ngo:NGO0316; -. DR PATRIC; 20333615; VBINeiGon24812_0387. DR HOGENOM; HOG000003788; -. DR KO; K14540; -. DR OMA; CDAKAGT; -. DR OrthoDB; EOG6G4VXH; -. DR BioCyc; NGON242231:GI2G-296-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 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; IPR016478; GTPase_MTG1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006230; MG442; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03596; GTPase_YlqF; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006230}; KW GTP-binding {ECO:0000256|PIRNR:PIRNR006230, KW ECO:0000256|PIRSR:PIRSR006230-1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006230, KW ECO:0000256|PIRSR:PIRSR006230-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 116 206 G (guanine nucleotide-binding). FT {ECO:0000259|Pfam:PF01926}. FT NP_BIND 58 61 GTP. {ECO:0000256|PIRSR:PIRSR006230-1}. FT NP_BIND 124 129 GTP. {ECO:0000256|PIRSR:PIRSR006230-1}. FT BINDING 168 168 GTP; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR006230-1}. SQ SEQUENCE 313 AA; 35303 MW; 3F6B4056AC1572F0 CRC64; MAIQWFPGHM NKARKAIAER AKSVDMVIEM LDARMPASSE NPLLAQLSKG KPKLKILNKQ DLADPERTKV WLDHYNSRPD TRAIALDSSE TGAHGKITQA CRAMIPHRQG IDKPLRVLIC GIPNVGKSTL INGMIGKKSA KTGNEPGITK AEQRLFLADD FWLYDTPGML WPKIIVEESG YNLAAGGAVG RNALDEEEVA LELLDYLRRH YLPMLQERYQ ADKDPSSHWD DNSWLEWIAK KRGAVLSGGR VNYQKAAENI LTDFREGKIG RITLETPNQW ETWLKKARQK EAELKAIREA RKAERKGQKP SEA // ID Q5F7W9_NEIG1 Unreviewed; 859 AA. AC Q5F7W9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034}; GN Name=clpB {ECO:0000256|RuleBase:RU362034}; GN ORFNames=NGO_1046 {ECO:0000313|EMBL:AAW89718.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89718.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|RuleBase:RU362034}. CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent. CC {ECO:0000256|SAAS:SAAS00536112}. CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent. CC {ECO:0000256|RuleBase:RU362034}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034, CC ECO:0000256|SAAS:SAAS00433973}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. CC {ECO:0000256|RuleBase:RU004432, ECO:0000256|SAAS:SAAS00548741}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89718.1; -; Genomic_DNA. DR RefSeq; WP_003702540.1; NC_002946.2. DR RefSeq; YP_208130.1; NC_002946.2. DR ProteinModelPortal; Q5F7W9; -. DR SMR; Q5F7W9; 160-351. DR EnsemblBacteria; AAW89718; AAW89718; NGO_1046. DR GeneID; 3282204; -. DR KEGG; ngo:NGO1046; -. DR PATRIC; 20335316; VBINeiGon24812_1224. DR HOGENOM; HOG000218211; -. DR KO; K03695; -. DR OMA; PVERILM; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; NGON242231:GI2G-963-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698}; KW Chaperone {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00480820}; KW Coiled coil {ECO:0000256|RuleBase:RU362034}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|RuleBase:RU362034, KW ECO:0000256|SAAS:SAAS00433964}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repeat {ECO:0000256|SAAS:SAAS00417491}; KW Stress response {ECO:0000256|RuleBase:RU362034}. FT DOMAIN 198 343 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 601 749 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 769 858 ClpB_D2-small. FT {ECO:0000259|SMART:SM01086}. FT COILED 412 461 {ECO:0000256|RuleBase:RU362034}. SQ SEQUENCE 859 AA; 95098 MW; A4E77FEE96825EB9 CRC64; MRYDKLTAKF QQALAEAQSL ALAADSSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV KQRLQQHLNS LPKVSGQGGE ILPSRELQAV LNLMDKAATK RGDAYIASEL FLLALVQQND AAGKILKEAG 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 LELIDEEIDG LQKEYADLDE IWKAEKAISD GAANIKKQID EVKIKIEQAK RQGDLALASK LMYEDLEHLE KQRAAAERAD TDSTKPANKL LRNNVGAEEI AEVVSRMTGI PVSKMMEGER DKLLKMEEVL HRRVVGQNEA VRAVSDAIRR SRSGLADPNK PYGSFLFLGP TGVGKTELCK ALAGFLFDSE DHLIRIDMSE YMEKHAVARL IGAPPGYVGY EEGGYLTEQV RRKPYSVILL DEVEKAHPDV FNILLQVLDD GRLTDGQGRT VDFKNTVIVM TSNIGSQHIQ QMGTQDYEAV KEVVMEDVKE HFRPEMINRI DEVVVFHGLD QANIRSIAKI QLKGLEKRLE KQNLRLTVSD AALDIIAKAG FDPIYGARPL KRAIQSEIEN PLAKALLAGN YAPESEIKVE ADGDRLKFA // ID A0A0H4ISP6_NEIG1 Unreviewed; 148 AA. AC A0A0H4ISP6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Hemagglutinin {ECO:0000313|EMBL:AKO63639.1}; GN ORFNames=NGO_03710 {ECO:0000313|EMBL:AKO63639.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63639.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63639.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63639; AKO63639; NGO_03710. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 23 50 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 148 AA; 15347 MW; D70BFAEF33F99626 CRC64; MQSELDLQRT VSQDFSKNVQ QTNTEINQHL DKLKADKEAA ETAAAEALAN GDMETAKRKA HEAQDAAAKA DNWQQGKVIL NMLASGLAEP TQSGAGIAAA TASPDVSYAI GQHFKDLAGQ NANGKLTASQ ETAHVLAHAV LGAAVAAA // ID A0A0H4IVL7_NEIG1 Unreviewed; 154 AA. AC A0A0H4IVL7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=MAFB alternative {ECO:0000313|EMBL:AKO63795.1}; GN ORFNames=NGO_10575 {ECO:0000313|EMBL:AKO63795.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63795.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63795.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63795; AKO63795; NGO_10575. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 154 AA; 16417 MW; D4B1A617DA14F2D7 CRC64; MHTLDGEMAG GNRPPKSITS KGKANAATYP KLVNQLNEQN LNNIAAQDSR LASAVKDWKT IQPNKKGEIN FGIGSATRQE AEQLGKIWVG DGAKPVSSPS CQGCMLSADG TRLYRPPTTK SNTPESLNPT GVQANFVTRS VDGKTLTNGH LNIK // ID A0A0H4IS66_NEIG1 Unreviewed; 61 AA. AC A0A0H4IS66; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Cro/Cl family transcriptional regulator {ECO:0000313|EMBL:AKO63756.1}; GN ORFNames=NGO_08655 {ECO:0000313|EMBL:AKO63756.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63756.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63756.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63756; AKO63756; NGO_08655. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.30.240.10; -; 1. DR InterPro; IPR000655; Cro. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF09048; Cro; 1. DR PIRSF; PIRSF003217; Cro_protein; 1. DR ProDom; PD054632; HTH_lambda_Cro; 1. DR SUPFAM; SSF47413; SSF47413; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 61 AA; 6759 MW; 654AAA150FD80A37 CRC64; MKKIPLNEYV EQHGQAKTAK EIGVTQGAIS KALRSGRAIF LFSDGKRVKA EEVRAFPSTR L // ID A0A0H4IVK1_NEIG1 Unreviewed; 271 AA. AC A0A0H4IVK1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE RecName: Full=Site-determining protein {ECO:0000256|PIRNR:PIRNR003092}; GN ORFNames=NGO_09675 {ECO:0000313|EMBL:AKO63775.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63775.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ParA family. CC {ECO:0000256|PIRNR:PIRNR003092}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AKO63775.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63775; AKO63775; NGO_09675. DR Proteomes; UP000000535; Chromosome. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR003092, KW ECO:0000256|PIRSR:PIRSR003092-1}; KW Cell cycle {ECO:0000313|EMBL:AKO63775.1}; KW Cell division {ECO:0000313|EMBL:AKO63775.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003092, KW ECO:0000256|PIRSR:PIRSR003092-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 218 CbiA. {ECO:0000259|Pfam:PF01656}. FT NP_BIND 10 17 ATP. {ECO:0000256|PIRSR:PIRSR003092-1}. SQ SEQUENCE 271 AA; 29627 MW; 87EC6FE30DD16E32 CRC64; MAKIIVVTSG KGGVGKTTTS ASIATGLALR GYKTAVIDFD VGLRNLDLIM GCERRVVYDL INVIQGEATL NQALIKDKNC ENLFILPASQ TRDKDALTRE GVEKVMQELS GKKMGFEYII CDSPAGIEQG ALMALYFADE AIVTTNPEVS SVRDSDRILG ILQSKSRKAE QGGSVKEHLL ITRYSPERVA KGEMLSVQDI CDILRIPLLG VIPESQNVLQ ASNSGEPVIH QDSVTASEAY KDVIARLLGE NREMRFLEAE KKSFFKRLFG G // ID A0A0H4IRK4_NEIG1 Unreviewed; 84 AA. AC A0A0H4IRK4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63591.1}; GN ORFNames=NGO_00430 {ECO:0000313|EMBL:AKO63591.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63591.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63591.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63591; AKO63591; NGO_00430. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 84 AA; 9495 MW; 7BE3C93B6298A073 CRC64; MGCYVVVNEG RDVSMLSDSV AAAVILKNRC MANAKEKPLC RHSRAGENPD FDLLEMFKVN RYFKLPDSCF RGNGDMNVFN FNLL // ID Q5F771_NEIG1 Unreviewed; 451 AA. AC Q5F771; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 50. DE SubName: Full=Protease {ECO:0000313|EMBL:AAW89966.1}; GN ORFNames=NGO_1314 {ECO:0000313|EMBL:AAW89966.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89966.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89966.1; -; Genomic_DNA. DR RefSeq; WP_003691638.1; NC_002946.2. DR RefSeq; YP_208378.1; NC_002946.2. DR EnsemblBacteria; AAW89966; AAW89966; NGO_1314. DR GeneID; 3281920; -. DR KEGG; ngo:NGO1314; -. DR PATRIC; 20335987; VBINeiGon24812_1544. DR HOGENOM; HOG000275241; -. DR KO; K08303; -. DR OMA; DFQVNGE; -. DR OrthoDB; EOG6GJBTC; -. DR BioCyc; NGON242231:GI2G-1229-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89966.1}; KW Protease {ECO:0000313|EMBL:AAW89966.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 369 445 Peptidase_U32_C. FT {ECO:0000259|Pfam:PF16325}. SQ SEQUENCE 451 AA; 50809 MW; BCA7750564B44B00 CRC64; MKAPELLLPA GGLERMRAAY DYGADAVYAG SPRYSLRARN NEFAKLDVLE QGIKEAHERN KKFFLTVNTL PHNSKLKTFV ADMEPLIAMK PDALIMADPG LIMTVREKWP EMPIHLSVQA NTTNYWGVKF WQNIGVERII LSRELGMEEI AEIRQECPDI ELEVFIHGAL CIAYSGRCLL SGYFNHRDPN QGTCTNSCRW DYKVHNATES EAGDAQLLQG FNFEKAQEEA NQNFEGINGQ KRHPYADKVF LIEESNRPGE MMPIMEDEHG TYIMNSKDLR GIEVVEKLAK IGVDSLKVEG RTKSLYYVAR VAQSYRKAIH DAVAGRPFDY SLLSELEGLA NRGYTSGFLE RHQTQDYQNY LSGHSTAKQS QYVGHVTEID ENGWATIEVK NRFAVGDSLE IIHPSGNQTI KLEQMTRKGQ PVDVAPGNGI QVKIPNMQGK EKALIARVLN P // ID Q5F9X3_NEIG1 Unreviewed; 514 AA. AC Q5F9X3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 89. 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 ORFNames=NGO_0263 {ECO:0000313|EMBL:AAW89014.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89014.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89014.1; -; Genomic_DNA. DR RefSeq; WP_003690741.1; NC_002946.2. DR RefSeq; YP_207426.1; NC_002946.2. DR ProteinModelPortal; Q5F9X3; -. DR SMR; Q5F9X3; 2-485. DR EnsemblBacteria; AAW89014; AAW89014; NGO_0263. DR GeneID; 3281534; -. DR KEGG; ngo:NGO0263; -. DR PATRIC; 20333493; VBINeiGon24812_0327. DR HOGENOM; HOG000033687; -. DR KO; K00764; -. DR OMA; AARVHMG; -. DR OrthoDB; EOG6KT2Q1; -. DR BioCyc; NGON242231:GI2G-246-MONOMER; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW89014.1}; 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:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01931, KW ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:AAW89014.1}. 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; 55989 MW; AFCA0B25922914A5 CRC64; MCGVLGLVSH EPVNQLLYDG LQMLQHRGQD AAGIATAEGG TFHMHKGKGM VSEVFRTRNM RDLTGNAGIA HVRYPTAGNA GSSAEAQPFY VSSPFGIVLA HNGNLTNTAE LYENVCNKHL RHINTGSDSE VLLNVFAHEL RREVSKNADP HRLNADNIFN AVAEVHRLVR GAYGVVAMIA GYGMLAFRDP YGIRPLALGS QTDSEGRKSY AVASESVAFN ALAYDLERDI RPGEAVFVGF NGTIIARQCS DRAKLSPCLF EYVYFARPDS VIDGVSVYQS RLDMGVSLAE KIKRELPVDG IDVVMPIPDT SRPSAMELAV HLNKPYREGL IKNRYIGRTF IMPGQSTRKK SVRQKLSPME TEFAGKSVLL VDDSIVRGTT SREIVEMVRA AGARKVYIAS AAPEVRYPNV YGIDMPTREE LIANGRSAAE IAAEIGADGI VFQDLGDLEA VVKALNPKIE SFDSSCFNGI YRTGDIDDAY LDRLSAEKSG CAGLKIHPSR MEHSISISDA GDEE // ID A0A0H4ISQ2_NEIG1 Unreviewed; 64 AA. AC A0A0H4ISQ2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63644.1}; GN ORFNames=NGO_03805 {ECO:0000313|EMBL:AKO63644.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63644.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63644.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63644; AKO63644; NGO_03805. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 7289 MW; 6A64195E3EBEC70B CRC64; MIYYPAVLFQ NPDQSNWGVI IPDLPGCILS AIRLPTRLPM PKPPQCSISK GFCRKTCRFP RRKA // ID Q5F6M7_NEIG1 Unreviewed; 262 AA. AC Q5F6M7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90160.1}; GN ORFNames=NGO_1524 {ECO:0000313|EMBL:AAW90160.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90160.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90160.1; -; Genomic_DNA. DR RefSeq; WP_003693564.1; NC_002946.2. DR RefSeq; YP_208572.1; NC_002946.2. DR EnsemblBacteria; AAW90160; AAW90160; NGO_1524. DR GeneID; 3281527; -. DR KEGG; ngo:NGO1524; -. DR PATRIC; 20336540; VBINeiGon24812_1818. DR HOGENOM; HOG000114880; -. DR KO; K07090; -. DR OMA; GTNKGQS; -. DR OrthoDB; EOG61VZ6K; -. DR BioCyc; NGON242231:GI2G-1426-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363041}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 27264 MW; 294FBD18FEE616C9 CRC64; MEDLYIILAL GLVAMIAGFI DAIAGGGGLI TLPALLLAGI PPVSAIATNK LQAAAATFSA TVSFARKGLI DWKKGLPIAA ASFAGGVVGA LSVSLVSKDI LLAVVPVLLI FVALYFVFSP KLDGSKEGKA RMSFFLFGLT VAPLLGFYDG VFGPGVGSFF LIAFIVLLGC KLLNAMSYTK LANVACNLGS LSVFLLHGSI IFPIVATMAV GAFVGANLGA RFAVRFGSKL IKPLLIVISI SMAVKLLIDE RNPLYQMIVS MF // ID A0A0H4ITA9_NEIG1 Unreviewed; 92 AA. AC A0A0H4ITA9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63809.1}; GN ORFNames=NGO_11125 {ECO:0000313|EMBL:AKO63809.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63809.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63809.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63809; AKO63809; NGO_11125. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 92 AA; 9991 MW; 3FB97E5750ADA026 CRC64; MASASTIKGK YVQKVEVAKG VVTAQMASTG VNKEIQDKKL SLWAKRQDGS VKWFCGQPVT RTGDNDDTVA DANNAIDTKH LPSTCRDKHD AK // ID Q5F9R2_NEIG1 Unreviewed; 291 AA. AC Q5F9R2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Tyrosine recombinase XerD {ECO:0000256|HAMAP-Rule:MF_01807}; GN Name=xerD {ECO:0000256|HAMAP-Rule:MF_01807, GN ECO:0000313|EMBL:AAW89075.1}; GN ORFNames=NGO_0329 {ECO:0000313|EMBL:AAW89075.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89075.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two CC molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP- CC Rule:MF_01807}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01807, CC ECO:0000256|SAAS:SAAS00019473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89075.1; -; Genomic_DNA. DR RefSeq; WP_003690783.1; NC_002946.2. DR RefSeq; YP_207487.1; NC_002946.2. DR ProteinModelPortal; Q5F9R2; -. DR EnsemblBacteria; AAW89075; AAW89075; NGO_0329. DR GeneID; 3283041; -. DR KEGG; ngo:NGO0329; -. DR PATRIC; 20333649; VBINeiGon24812_0402. DR HOGENOM; HOG000045296; -. DR KO; K04763; -. DR OMA; AIWQMIK; -. DR OrthoDB; EOG6PZXFP; -. DR BioCyc; NGON242231:GI2G-310-MONOMER; -. DR Proteomes; UP000000535; 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; 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 {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00444057}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00444057}; KW Chromosome partition {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00444068}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00424238}; KW DNA integration {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00424142}; KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00424218}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01807, KW ECO:0000256|SAAS:SAAS00424103}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 85 Integrase_SAM-like_N. FT {ECO:0000259|Pfam:PF02899}. FT DOMAIN 108 276 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. FT ACT_SITE 143 143 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 167 167 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 237 237 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 240 240 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 263 263 {ECO:0000256|HAMAP-Rule:MF_01807}. FT ACT_SITE 272 272 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01807}. SQ SEQUENCE 291 AA; 33002 MW; 5BB57FB50CC6FBF0 CRC64; MENGLIDRLL ETLWLDRRLS RNTLDSYRRD LEKIARRLSL CGRTLKDADE ADLAAAVYVD GEQRSSQARA LSACKRLYVW MEREGMRADN PTRLLKPPKI DRNIPTLITE QQISRLLAAP DTDTPHGLRD KALLELMYAT GLRVSEAVGL NFGNVDLDRG CITTLGKGDK QRMVPMGQES AYWVERYYTE ARPLLLKGRS CDALFVSQKK TGISRQLAWM IVKEYAGRAG IGHISPHSLR HAFATHLVRH GLDLRVVQDM LGHADLNTTQ IYTHVANVRL HSVVKEHHSR N // ID Q5F9E3_NEIG1 Unreviewed; 203 AA. AC Q5F9E3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 49. DE SubName: Full=Pilus assembly protein PilX {ECO:0000313|EMBL:AAW89194.1}; GN ORFNames=NGO_0455 {ECO:0000313|EMBL:AAW89194.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89194.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89194.1; -; Genomic_DNA. DR RefSeq; WP_010951047.1; NC_002946.2. DR RefSeq; YP_207606.1; NC_002946.2. DR EnsemblBacteria; AAW89194; AAW89194; NGO_0455. DR GeneID; 3282989; -. DR KEGG; ngo:NGO0455; -. DR PATRIC; 20333942; VBINeiGon24812_0545. DR HOGENOM; HOG000218896; -. DR KO; K02673; -. DR OMA; DNKGMEY; -. DR OrthoDB; EOG6JX7J7; -. DR BioCyc; NGON242231:GI2G-432-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 92 198 PilX. {ECO:0000259|Pfam:PF13681}. SQ SEQUENCE 203 AA; 21967 MW; 9EEF8192FA7B7FF0 CRC64; MRKQNTLTGI PTSDGQRGSA LFIVLMVMIV VAFLVVTAAQ SYNTEQRISA NESDRKLALS LAEAALREGE FQVLDLEYAA DSKVTFSENC EKGLCTAVNV RTNNNGSEEA FGNIVVQGKP AVEAVKRSCP AKSGKNSTDL CIDNKGMEYN KGAAGVSKMP RYIIEYLGVK NGQNVYRVTA KAWGKNANTV VVLQSYVGNN DEQ // ID A0A0H4IT26_NEIG1 Unreviewed; 533 AA. AC A0A0H4IT26; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Nitrous-oxide reductase {ECO:0000313|EMBL:AKO63719.1}; DE EC=1.7.2.4 {ECO:0000313|EMBL:AKO63719.1}; GN ORFNames=NGO_07410 {ECO:0000313|EMBL:AKO63719.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63719.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63719.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63719; AKO63719; NGO_07410. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-EC. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR011045; N2O_reductase_N. DR InterPro; IPR023644; NO_Rdtase. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR SUPFAM; SSF50974; SSF50974; 1. DR TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AKO63719.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 533 AA; 58112 MW; 3D2CEEDFB0AE1B72 CRC64; MSDEKLEQNG LSRRSFLGTA AASGAGIAGA GLLGLAGCSK DGEQAAANAS GAAPVAKAQG ESKPGQLSSE VGPGELDQYY GFLSGGQSGE MRLIGLPSMR ELMRIPVFNM DSATGWGRTN ESLKVLNGNI TEETRKFLKD SGLRCYPNGD LHHPHLSFTD QTYDGRYAYA NDKANNRVCR VRLDVMKADK IIDIPNDSGI HGLRPQRYPK TGYVFANGEH ITPVSGVGKL DDAKTWNAVY TAIDGETMEI AWQVLVDGNL DNGDADYQGK YSFATCYNSE RALTVQGASS NEQDWCVVFD LKAIEEGIKA GDFKEVNGVK MLDGRAEAKS KYTRYIPVPN SPHGCNASPD GKYIMPNGKL PPTVTVLDVS KLDDLFAGKI KERDVVVAEP QLGLGPLHTA FDGRGNAYTT LFIDSQMVKW NIDDAIKAYK GEKIDPIKQK LDVHYQPGHN HTTMGETKEA DGQWLVSLNK FSKDRFLNAG PLKPECDQLI GISGDEMRLV HDNPTFAEPH DLCLVAASKL NPGKTWDRKD PWF // ID A0A0H4IV81_NEIG1 Unreviewed; 229 AA. AC A0A0H4IV81; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63685.1}; GN ORFNames=NGO_05620 {ECO:0000313|EMBL:AKO63685.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63685.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63685.1; -; Genomic_DNA. DR RefSeq; WP_030003514.1; NC_002946.2. DR RefSeq; YP_008914853.1; NC_002946.2. DR EnsemblBacteria; AKO63685; AKO63685; NGO_05620. DR GeneID; 19593000; -. DR KEGG; ngo:NGO1073a; -. DR Proteomes; UP000000535; 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; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 229 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 229 AA; 25856 MW; 4E8872492700BB0C CRC64; MQADLAYAAE RITHDYPEPT GTKKDKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWNNS KYSVNTKKVN ENKGEKINVT QYLKAENQEN GTFHAVSSLG LSAVYDFKLN DKFKPYIGAR VAYGHVRHSI DSTKKTTEFL TAAGQDGGAP TVYNNGSTQD AHQESDSIRR VGLGVIAGVG FDITPNLTLD AGYRYHNWGR LENTRFKTHE ASLGMRYRF // ID Q5F5Q9_NEIG1 Unreviewed; 92 AA. AC Q5F5Q9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Preprotein translocase subunit SecE {ECO:0000313|EMBL:AAW90478.1}; GN ORFNames=NGO_1857 {ECO:0000313|EMBL:AAW90478.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90478.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90478.1; -; Genomic_DNA. DR RefSeq; WP_003690113.1; NC_002946.2. DR RefSeq; YP_208890.1; NC_002946.2. DR EnsemblBacteria; AAW90478; AAW90478; NGO_1857. DR GeneID; 3282374; -. DR KEGG; ngo:NGO1857; -. DR PATRIC; 20337394; VBINeiGon24812_2232. DR HOGENOM; HOG000218664; -. DR KO; K03073; -. DR OMA; FQQGIVQ; -. DR OrthoDB; EOG6DRPR4; -. DR BioCyc; NGON242231:GI2G-1758-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00458914, ECO:0000256|SAM:Phobius}; KW Protein transport {ECO:0000256|SAAS:SAAS00458899}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 10625 MW; F503C2A5AE4EF14D CRC64; MTEHTPEKKN VKVNQLVVQD KESASNSGKE GFFAYFSNSW SEFKKVVWPK REDAVRMTVF VIVFVAVLSI FIYAADTAIS WLFFDVLLRR EG // ID Q5F527_NEIG1 Unreviewed; 809 AA. AC Q5F527; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Ligand-gated channel protein {ECO:0000313|EMBL:AAW90710.1}; GN ORFNames=NGO_2109 {ECO:0000313|EMBL:AAW90710.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90710.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90710.1; -; Genomic_DNA. DR RefSeq; WP_003705045.1; NC_002946.2. DR RefSeq; YP_209122.1; NC_002946.2. DR ProteinModelPortal; Q5F527; -. DR EnsemblBacteria; AAW90710; AAW90710; NGO_2109. DR GeneID; 3282808; -. DR KEGG; ngo:NGO2109; -. DR PATRIC; 20338059; VBINeiGon24812_2552. DR HOGENOM; HOG000220769; -. DR KO; K16087; -. DR OMA; YAEGFRT; -. DR OrthoDB; EOG6HB9KP; -. DR BioCyc; NGON242231:GI2G-2004-MONOMER; -. DR Proteomes; UP000000535; 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; -; 1. DR InterPro; IPR012910; Plug_dom. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010949; TonB_Hb/transfer/lactofer_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 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00444644, KW ECO:0000256|SAAS:SAAS00447760}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357, KW ECO:0000256|SAAS:SAAS00444615}; KW Transmembrane {ECO:0000256|SAAS:SAAS00447760}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00447760}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 809 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256180. FT DOMAIN 52 160 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 514 807 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 809 AA; 90481 MW; 1A6F7920A5C561F8 CRC64; MPIPFKPVLA AAAIAQAFPA FAADPAPQSA QTLNEITVTG THKTQKLGEE KIRRKTLDKL LANDEHGLVR YDPGISVVEG GRAGSNGFTI RGVDKDRVAI NVDGLAQAES RSSEAFQELF GAYGNFNANR NTSEPENFSE VTITKGADSL KSGSGALGGA VNYQTKSASD YVSEDKPYHL GIKGGSVGKN SQKFSSITAA GRLFGLDALL VYTRRFGKET KNRSTEGDVE IKNDGYVFDP ANPSPSRYLT YKATGVARSQ PDPQEWVNKS TLFKLGYNFN DRNRIGWIFE DSRTDRFTNE LSNLWTGTTT SAATGDYRHR QDVSYRRRTG VEYKNELEHG PWDSLKLRYD KQRIDMNTWT WDIPKNYDTN GINGEVYHSF RHIRQNTAQW TADFEKQLDF SKAVWAAQYG LGGGRGDNAN SDYSYFAKLY DPKILASNQA KITMLIENRS KYKFAYWNNV FHLGGNDRFR LNAGIRYDKN SSSAKDDPKY TTAIRGQIPH LGSERAHAGF SYGTGFDWRF TKHLHLLAKY STGFRAPTSD ETWLLFPHPD FYLKTNPELK AEKAKNWELG LAGSGKAGSF KLSGFKTKYR DFIELTYMGV SSDDKNNPRY APLSDGTALV SSPVWQNQNR TAAWVKGIEF NGTWNLDSIG LPKGLHTGLN VSYIKGKATQ NNGKETPINA LSPWTAVYSL GYDAPSKRWG VNAYAARTAA KKPSDTVHSN DDLNKPWPYA KHSKAYTLFD LSAYLNIGKQ VTLRAAAYNI TNKQYYTWES LRSIREFGTV NRVNNKTHAG IQRFTSPGRS YNFTIEAKF // ID A0A0H4J5I6_NEIG1 Unreviewed; 115 AA. AC A0A0H4J5I6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63657.1}; GN ORFNames=NGO_04345 {ECO:0000313|EMBL:AKO63657.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63657.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63657.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63657; AKO63657; NGO_04345. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 115 AA; 13307 MW; C1B8AB8AE90AE3A9 CRC64; MNNMFAAKLS ELVYTASDHP DSLSEMEEFD RLILLIRKLY QILDGQHTLY RVTVCLNYRS RRGLIALDKA AVGCDAAMLR ARRWRICMQI AERLSESVGR LHGCGRKRVR RLPRA // ID Q5FAE7_NEIG1 Unreviewed; 77 AA. AC Q5FAE7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=RNA-binding protein {ECO:0000313|EMBL:AAW88840.1}; GN ORFNames=NGO_0079 {ECO:0000313|EMBL:AAW88840.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88840.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88840.1; -; Genomic_DNA. DR RefSeq; WP_010950990.1; NC_002946.2. DR RefSeq; YP_207252.1; NC_002946.2. DR ProteinModelPortal; Q5FAE7; -. DR EnsemblBacteria; AAW88840; AAW88840; NGO_0079. DR GeneID; 3283048; -. DR KEGG; ngo:NGO0079; -. DR PATRIC; 20333043; VBINeiGon24812_0105. DR HOGENOM; HOG000074028; -. DR KO; K14761; -. DR OMA; GWADCGG; -. DR OrthoDB; EOG6VB6ZH; -. DR BioCyc; NGON242231:GI2G-69-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 13 73 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 77 AA; 8231 MW; 152A80EF20EE5526 CRC64; MEATVYLEDN EYIALCDLLK LAGLAESGGQ AKAFIAEGLV LRNGGTEIRK TAKIRGGEVI EFDGARLEIA DGYDPEA // ID Q5F6I1_NEIG1 Unreviewed; 236 AA. AC Q5F6I1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90206.1}; GN ORFNames=NGO_1577 {ECO:0000313|EMBL:AAW90206.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90206.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ompA family. CC {ECO:0000256|RuleBase:RU003859}. CC -!- SIMILARITY: Contains OmpA-like domain. CC {ECO:0000256|SAAS:SAAS00509386}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90206.1; -; Genomic_DNA. DR RefSeq; WP_003689500.1; NC_002946.2. DR RefSeq; YP_208618.1; NC_002946.2. DR ProteinModelPortal; Q5F6I1; -. DR SMR; Q5F6I1; 84-223. DR EnsemblBacteria; AAW90206; AAW90206; NGO_1577. DR GeneID; 3281426; -. DR KEGG; ngo:NGO1577; -. DR PATRIC; 20336678; VBINeiGon24812_1885. DR HOGENOM; HOG000189913; -. DR OMA; CWRTGYW; -. DR OrthoDB; EOG6PP9QB; -. DR BioCyc; NGON242231:GI2G-1474-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003859}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 236 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255488. FT DOMAIN 86 223 OmpA-like. {ECO:0000259|PROSITE:PS51123}. SQ SEQUENCE 236 AA; 25540 MW; DAE9AAECA66FB199 CRC64; MTKQLKLSAL FVALLASGTA VAGEASVQGY TVSGQSNEIV RNNYGECWKN AYFDKASQGR VECGDAVAVP EPEPAPVAVV EQAPQYVDET ISLSAKTLFG FDKDSLRAEA QDNLKVLAQR LSRTNVQSVR VEGHTDFMGS EKYNQALSER RAYVVANNLV SNGVPASRIS AVGLGESQAQ MTQVCQAEVA KLGAKASKAK KREALIACIE PDRRVDVKIR SIVTRQVVPA RNHHQH // ID Q5F9V1_NEIG1 Unreviewed; 290 AA. AC Q5F9V1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 76. 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 ORFNames=NGO_0288 {ECO:0000313|EMBL:AAW89036.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89036.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89036.1; -; Genomic_DNA. DR RefSeq; WP_003687661.1; NC_002946.2. DR RefSeq; YP_207448.1; NC_002946.2. DR ProteinModelPortal; Q5F9V1; -. DR EnsemblBacteria; AAW89036; AAW89036; NGO_0288. DR GeneID; 3281630; -. DR KEGG; ngo:NGO0288; -. DR PATRIC; 20333555; VBINeiGon24812_0358. DR HOGENOM; HOG000270269; -. DR KO; K03089; -. DR OMA; EIHEYIV; -. DR OrthoDB; EOG6D5G0W; -. DR BioCyc; NGON242231:GI2G-268-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 32829 MW; 6FAFAC9A2D967B25 CRC64; MPQMNNAFAL PAIQSGNGSL EQYIHTVNSI PMLSQEEETR LAERRIKGDL NAAKQLILSH LRVVVSIARG YDGYGLNQAD LIQEGNIGLM KAVKRYEPGR GARLFSFAVH WIKAEIHEFI LRNWRLVRVA TTKPQRKLFF NLRSMRKNLN VLSPKEAQDI ADDLGVKLSE VLEMEQRMTG HDIAIMADNS DDEDSFAPID WLADHDSEPS RQLSKQAHYA LQTEGLQNAL AQLDDRSRRI VESRWLQDDG GLTLHQLAAE YGVSAERIRQ IEAKAMQKLR GFLTEEAEAV // ID A0A0H4IV64_NEIG1 Unreviewed; 177 AA. AC A0A0H4IV64; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63670.1}; GN ORFNames=NGO_04910 {ECO:0000313|EMBL:AKO63670.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63670.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63670.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63670; AKO63670; NGO_04910. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 177 AA; 20593 MW; EED0E9310370C848 CRC64; MLAIEDLRYG TRTISRQAQD AIMEQERRLR EATLMLTQGS QKTRGQGEEP KRARYFEVSA TSAYLNRHNN GLGGNFQYIG QLPGYLKMHG EMLENQSLFR LSNRERNPDK PFLDIHFDEN GKITRIVVYE KNIYSGLNLN QDKATKPKTV QIVRQGEATL YWFKFNPLYF NPNTGRI // ID Q5F8A1_NEIG1 Unreviewed; 182 AA. AC Q5F8A1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN ORFNames=NGO_0887 {ECO:0000313|EMBL:AAW89586.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89586.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89586.1; -; Genomic_DNA. DR RefSeq; WP_003706302.1; NC_002946.2. DR RefSeq; YP_207998.1; NC_002946.2. DR ProteinModelPortal; Q5F8A1; -. DR EnsemblBacteria; AAW89586; AAW89586; NGO_0887. DR GeneID; 3281121; -. DR KEGG; ngo:NGO0887; -. DR PATRIC; 20334949; VBINeiGon24812_1044. DR HOGENOM; HOG000218410; -. DR OMA; INVEHAC; -. DR OrthoDB; EOG6P5ZKB; -. DR BioCyc; NGON242231:GI2G-828-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00461175}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00461184, KW ECO:0000313|EMBL:AAW89586.1}; KW Peroxidase {ECO:0000256|SAAS:SAAS00461184, KW ECO:0000313|EMBL:AAW89586.1}; KW Redox-active center {ECO:0000256|SAAS:SAAS00461089}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 41 121 CMD. {ECO:0000259|Pfam:PF02627}. SQ SEQUENCE 182 AA; 19151 MW; 008F85E17E01B8C7 CRC64; MARLTVHTLE TAPEAAKPRV EAVPKNNGFI PNLIGVLANA PEALAFYQEV GKLNAANSLT AGEVEVIRII AVRTNQCSFC VAGHTKLATL KKLLSEQSLN AARALAAGKS DDAKLGALAA FTQAVMAKKG AVSDDELNAF LEAGYNRQQA VEVVMGVALA TLCNYANNLA QTEINPKLQA YA // ID Q5F5Z6_NEIG1 Unreviewed; 796 AA. AC Q5F5Z6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 97. 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:AAW90391.1}; GN ORFNames=NGO_1772 {ECO:0000313|EMBL:AAW90391.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90391.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90391.1; -; Genomic_DNA. DR RefSeq; WP_003689984.1; NC_002946.2. DR RefSeq; YP_208803.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z6; -. DR SMR; Q5F5Z6; 14-380. DR EnsemblBacteria; AAW90391; AAW90391; NGO_1772. DR GeneID; 3281137; -. DR KEGG; ngo:NGO1772; -. DR PATRIC; 20337176; VBINeiGon24812_2128. DR HOGENOM; HOG000075155; -. DR KO; K02470; -. DR OMA; IKNMITA; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; NGON242231:GI2G-1666-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 88209 MW; A39E518CACB144E3 CRC64; MTEQKHEEYG ADSIQVLEGL EAVRKRPGMY IGDTQDGSGL HHMVFEVLDN AIDEALAGHC DKITVTIHAD HSVSVADNGR GMPTGIHPKE GRSAAEVIMT VLHAGGKFDN NSYKISGGLH GVGVSVVNAL SDWVTLTIYR DGKEHFVRFV RGETEEPLKI VGDSDKKGTT VRFLAGTETF GNIEYSFDIL AKRIRELSFL NNGVDIELTD ERDGKHESFA LSGGVAGFVQ YMNRKKTPLH EKIFYAFGEK DGMSVECAMQ WNDSYQESVQ CFTNNIPQRD GGTHLTALRQ VMTRTINSYI EANEVAKKAK VETAGDDMRE GLTCVLSVKL PDPKFSSQTK DKLVSGEIGP VVNEVINQAL TDFLEENPNE AKIITGKIVD AARAREAARK AREITRRKGV MDGLGLPGKL ADCQEKDPAL SELYLVEGDS AGGSAMQGRD RKFQAILPLK GKILNVEKAR FEKMLASQEV ATLITALGAG IGKEEFNPEK LRYHRIIIMT DADVDGAHIR TLLLTFFYRQ MPELVERGYI YIAQPPLYKA KYGKQERYLK DELEKDQWLL GLALEKAKIV SDGRTIEGAE LADTAKQFLL AKTVIEQESR FVDELVLRAM LHASPIDLTS SENADKAVAE LSGLLDEKEA ALERIEGHEG HRFIKITRKL HGNVMVSYIE PKFLNSKAYQ TLTQTAAALK GLVGEGAKLY KGENEYDADS FETALDILMS VAQKGMSIQR YKGLGEMNPE QLWETTMDPA VRRLLKVRIE DAIAADEVFV TLMGDEVEPR RAFIENNALI AQNIDA // ID A0A0H4ITB4_NEIG1 Unreviewed; 247 AA. AC A0A0H4ITB4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Large pilS cassette {ECO:0000313|EMBL:AKO63814.1}; GN ORFNames=NGO_11155 {ECO:0000313|EMBL:AKO63814.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63814.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63814.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63814; AKO63814; NGO_11155. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 247 AA; 26955 MW; 4EE0AA6C98612F84 CRC64; MKGKYVKEVE VKNGVVTATM LSSGVNNEIK GKKLSLWARR ENGSVKWFCG QPVTRAKADA DADAAGKDTT NIDTKHLPST CRDESSAVCT KHHAPISNTS KKSAVTGYCP NHGKWPKDNT SAGVASPAEI KGKYVKSVTV AKGVVTAQMN PSGVNNEIKD KKLSLWAKRE NGSVKWFCGQ PVTRNDAKAD AKDDTVTAIE TKHLPSTCRD ESSAGCIKTP RADFKHFQKI SRCRVLPESR HMAERQR // ID A0A0H4IWK7_NEIG1 Unreviewed; 219 AA. AC A0A0H4IWK7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:AKO63823.1}; GN ORFNames=NGO_11620 {ECO:0000313|EMBL:AKO63823.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63823.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63823.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63823; AKO63823; NGO_11620. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR002495; Glyco_trans_8. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01501; Glyco_transf_8; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63823.1}. SQ SEQUENCE 219 AA; 25454 MW; 9E87B43546F59F80 CRC64; MGEYIADCDK VLYLDTDVLV RDGLKPLWDT DLGGNWVGAC IDLFVERQEG YKQKIGMADG EYYFNAGVLL INLKKWRRHD IFKMSCEWVE QYKDVMQYQD QDILNGLFKG GVCYANSRFN FMPTNYAFMA NGFASRHTDP LYLDRTNTAM PVAVSHYCGS AKPWHRDCTV WGAERFTELA GSLTTVPEEW RGKLAVPPTK RMLQRWRKKL SARFLRKIY // ID Q5F5P8_NEIG1 Unreviewed; 419 AA. AC Q5F5P8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 76. DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|SAAS:SAAS00013752}; DE EC=2.1.1.- {ECO:0000256|SAAS:SAAS00500186}; GN ORFNames=NGO_1869 {ECO:0000313|EMBL:AAW90489.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90489.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90489.1; -; Genomic_DNA. DR RefSeq; WP_010951361.1; NC_002946.2. DR RefSeq; YP_208901.1; NC_002946.2. DR ProteinModelPortal; Q5F5P8; -. DR EnsemblBacteria; AAW90489; AAW90489; NGO_1869. DR GeneID; 3282371; -. DR KEGG; ngo:NGO1869; -. DR PATRIC; 20337432; VBINeiGon24812_2247. DR HOGENOM; HOG000037300; -. DR KO; K03500; -. DR OMA; LRVNRQH; -. DR OrthoDB; EOG6091D0; -. DR BioCyc; NGON242231:GI2G-1773-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00423093}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00500183, KW ECO:0000313|EMBL:AAW90489.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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:AAW90489.1}. FT DOMAIN 164 419 SAM_MT_RSMB_NOP. FT {ECO:0000259|PROSITE:PS51686}. SQ SEQUENCE 419 AA; 46316 MW; 4894F2385DD951F6 CRC64; MSMALAQKLA ADSIAAVAEG RNLQDVLAHI RAAHPQLTAQ ENGALQDIAY GCQRYLGSLK HMLAQMLKKP IDNPQLESLL LAALYQLHYT RNAPHAVVNE AVESIAKIGR GQYRSFANAV LRRFLREREK LAASCKKDDV AKHNLPLWWV AYLKNHYPKH WHNIAAALQS HPPMTLRVNR RHGNAESYLE KLVAEGIAAK ALDEYAVTLE EAVPVNRLPG FAEGLVSVQD FGAQQAAYLL NPKDGERILD ACAAPGGKTG HILELADCRV TALDIDAGRL KRVEDNIARL GFQTASAACA DARDLAAWYD GKPFDAILAD VPCTASGVAR RNPDVKWLRR PTDALKTARQ QEALLDALWQ ALKQGGRMLL ATCSVFVEEN DGQLQKFLNR HADAEPIESR VLLPNKHQDG FYYALIQKH // ID A0A0H4IVG2_NEIG1 Unreviewed; 98 AA. AC A0A0H4IVG2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63730.1}; GN ORFNames=NGO_07815 {ECO:0000313|EMBL:AKO63730.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63730.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63730.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63730; AKO63730; NGO_07815. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 98 AA; 10994 MW; 11F39E677FE3D04A CRC64; MRGKKDVSGI SQEKIGAIAG LVRADQGAKI LKDKVSYETA SKQYDRAIQT SEKPANLIID ALKLDYQHAD IDRFAGHLWK LYQTLGNYGR QVKERMLG // ID A0A0H4IT38_NEIG1 Unreviewed; 129 AA. AC A0A0H4IT38; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63729.1}; GN ORFNames=NGO_07810 {ECO:0000313|EMBL:AKO63729.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63729.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63729.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63729; AKO63729; NGO_07810. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 129 AA; 15169 MW; 87527F2E44E97B7C CRC64; MRHGYLPKNI QKFKAQHRDL VLQDSSLINT GSSPADDAVK EVESLLMYGQ IEAAMDVLEQ AVLKYPDESQ LYITLIDIYE RTEDWDRLGQ FLRVLRERAD RLPEEVVMLM SRLLQRMNQN IKKIKRYGK // ID Q5F709_NEIG1 Unreviewed; 212 AA. AC Q5F709; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 54. DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:AAW90028.1}; GN ORFNames=NGO_1380 {ECO:0000313|EMBL:AAW90028.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90028.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90028.1; -; Genomic_DNA. DR RefSeq; WP_003693735.1; NC_002946.2. DR RefSeq; YP_208440.1; NC_002946.2. DR ProteinModelPortal; Q5F709; -. DR EnsemblBacteria; AAW90028; AAW90028; NGO_1380. DR GeneID; 3281799; -. DR KEGG; ngo:NGO1380; -. DR PATRIC; 20336149; VBINeiGon24812_1623. DR HOGENOM; HOG000077737; -. DR OMA; VEPYGFF; -. DR OrthoDB; EOG6WHNQN; -. DR BioCyc; NGON242231:GI2G-1293-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 23582 MW; 6155F9D9D9620EAD CRC64; MFQNFDLGVF LLAVLPVLLA ITVREVARGY TARYWGDNTA EQYGRLTLNP LPHIDLVGTI IVPLLTLMFT PFLFGWARPI PIDSRNFRNP RLAWRCIAAS GPLSNLAMAV LWGVVLVLTP YAGGAYQMPL AQMANYGILI NAILFALNII PILPWDGGIF IDTFLPAKYS QAFRKIEPYG TWIILLLMLT GVLGAFIAPI VRLVIAFVQM FV // ID Q5F9F7_NEIG1 Unreviewed; 193 AA. AC Q5F9F7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Outer-membrane lipoprotein LolB {ECO:0000256|SAAS:SAAS00002103}; GN ORFNames=NGO_0439 {ECO:0000313|EMBL:AAW89180.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89180.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|SAAS:SAAS00002106}. CC -!- SUBUNIT: Monomer. {ECO:0000256|SAAS:SAAS00088648}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|SAAS:SAAS00002105}; Lipid-anchor CC {ECO:0000256|SAAS:SAAS00002105}. CC -!- SIMILARITY: Belongs to the LolB family. CC {ECO:0000256|SAAS:SAAS00535102}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89180.1; -; Genomic_DNA. DR RefSeq; WP_010357457.1; NC_002946.2. DR RefSeq; YP_207592.1; NC_002946.2. DR ProteinModelPortal; Q5F9F7; -. DR EnsemblBacteria; AAW89180; AAW89180; NGO_0439. DR GeneID; 3282511; -. DR KEGG; ngo:NGO0439; -. DR PATRIC; 20333900; VBINeiGon24812_0526. DR HOGENOM; HOG000220712; -. DR KO; K02494; -. DR OMA; EILMKHT; -. DR OrthoDB; EOG6R5C6M; -. DR BioCyc; NGON242231:GI2G-416-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR029046; LolA/LolB/LppX. DR InterPro; IPR004565; OM_lipoprot_LolB. DR Pfam; PF03550; LolB; 1. DR SUPFAM; SSF89392; SSF89392; 1. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00416116}; KW Chaperone {ECO:0000256|SAAS:SAAS00416147}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00416116}; KW Protein transport {ECO:0000256|SAAS:SAAS00416139}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transport {ECO:0000256|SAAS:SAAS00416139}. SQ SEQUENCE 193 AA; 21188 MW; 489168489DEF93C2 CRC64; MKHTVSASVI LLLTACAQLP QNNENLWQPS EHISSFAAEG RLAVKAEGKG SYANFDWTYQ PPVETININT PLGSTLGQLC QDRDGALAVD GKGNVYQAEG TEDLSRQLVG FKLPIQYLHI WAEGRRVAGA PYRIRSDGIL EQYGWTIGRT ADSGGQVRTL QLNNGNLNIR LVFTEIGMPS ETETPERCAA RTR // ID Q5F9M0_NEIG1 Unreviewed; 238 AA. AC Q5F9M0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=Cysteine ABC transporter permease {ECO:0000313|EMBL:AAW89117.1}; GN ORFNames=NGO_0373 {ECO:0000313|EMBL:AAW89117.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89117.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89117.1; -; Genomic_DNA. DR RefSeq; WP_003687787.1; NC_002946.2. DR RefSeq; YP_207529.1; NC_002946.2. DR ProteinModelPortal; Q5F9M0; -. DR EnsemblBacteria; AAW89117; AAW89117; NGO_0373. DR GeneID; 3282174; -. DR KEGG; ngo:NGO0373; -. DR PATRIC; 20333749; VBINeiGon24812_0452. DR HOGENOM; HOG000267552; -. DR KO; K10009; -. DR OMA; IYWCFCW; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NGON242231:GI2G-352-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450258, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 33 55 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 75 96 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 204 224 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 32 225 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 238 AA; 26389 MW; 16E2C2050215DDE7 CRC64; MFNNFLASLP FMTETRADML ISAFWPMVKA GFTVSLPLAI ASFVIGMIIA VAVALVRIMP SGGIFQKCLL KLVEFYISVV RGTPLLVQLV IVFYGLPSVG IYINPIPAAI IGFSLNVGAY ASETIRAAIL SVPKGQWEAG FSIGMTYMQT FRRIVAPQAF RVAVPPLSNE FIGLFKNTSL AAVVTVTELF RVAQETANRT YDFLPVYIEA ALVYWCFCKV LFLIQARLEK RFDRYVAK // ID A0A0H4IRN3_NEIG1 Unreviewed; 66 AA. AC A0A0H4IRN3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Bacterioferritin {ECO:0000313|EMBL:AKO63616.1}; GN ORFNames=NGO_01775 {ECO:0000313|EMBL:AKO63616.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63616.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63616.1; -; Genomic_DNA. DR RefSeq; WP_002214037.1; NC_002946.2. DR RefSeq; YP_009115480.1; NC_002946.2. DR EnsemblBacteria; AKO63616; AKO63616; NGO_01775. DR GeneID; 22847888; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom. DR Pfam; PF04324; Fer2_BFD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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 A0A0H4J621_NEIG1 Unreviewed; 30 AA. AC A0A0H4J621; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63817.1}; GN ORFNames=NGO_11320 {ECO:0000313|EMBL:AKO63817.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63817.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63817.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63817; AKO63817; NGO_11320. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR031596; MaAIMP_sms. DR Pfam; PF16951; MaAIMP_sms; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 25 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 30 AA; 3186 MW; A88065F99009EE29 CRC64; MSTSAIVMMV AAIAVIWGGL LLSLLRLPEE // ID Q5F8L6_NEIG1 Unreviewed; 287 AA. AC Q5F8L6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:AAW89471.1}; GN ORFNames=NGO_0756 {ECO:0000313|EMBL:AAW89471.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89471.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89471.1; -; Genomic_DNA. DR RefSeq; WP_003688678.1; NC_002946.2. DR RefSeq; YP_207883.1; NC_002946.2. DR ProteinModelPortal; Q5F8L6; -. DR DNASU; 3282484; -. DR EnsemblBacteria; AAW89471; AAW89471; NGO_0756. DR GeneID; 3282484; -. DR KEGG; ngo:NGO0756; -. DR PATRIC; 20334660; VBINeiGon24812_0902. DR HOGENOM; HOG000255906; -. DR KO; K06923; -. DR OMA; YPFTQEH; -. DR OrthoDB; EOG6XQ3HX; -. DR BioCyc; NGON242231:GI2G-711-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 32 280 DUF815. {ECO:0000259|Pfam:PF05673}. SQ SEQUENCE 287 AA; 32348 MW; A62C8284AAFED41E CRC64; MELNEFLDKA YAVLRRLDAV LPPEPGHTDW NALAFRWQSA GKKGFLEHLP DPHVFPLSRL AGVGRQTELL VRNTEQFIAG RPANNVLMSG ARGTGKSSLV KALLHEYADK GLRLIEVDKS DLIGLPYLLA LLKERPEKFI VFCDDLSFES GDETYKALKT ALDGGLSQRC ANVMVYATSN RRHLMPEYLD ENAGTTGVRG EIHQKEAVEE KVSLSDRFGL WLSFYPFDQN DYLAAVRSWL EDFDVPYDEA ARTAALQWAQ MRGNRSGRSA WQFACDWAGR LPEQRAP // ID A0A0H4IRP5_NEIG1 Unreviewed; 69 AA. AC A0A0H4IRP5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63626.1}; GN ORFNames=NGO_02840 {ECO:0000313|EMBL:AKO63626.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63626.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63626.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63626; AKO63626; NGO_02840. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 69 AA; 7707 MW; 6B59748E669254E4 CRC64; MQRAKAAFFF LFGIFCLSEG TIARKFNQFI LPVQLNQMPS EGAERASDGI GETQRLQTAF LPLYFNAAS // ID A0A0H4IRY7_NEIG1 Unreviewed; 67 AA. AC A0A0H4IRY7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Serine/arginine repetitive matrix 2 {ECO:0000313|EMBL:AKO63686.1}; GN ORFNames=NGO_05650 {ECO:0000313|EMBL:AKO63686.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63686.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63686.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63686; AKO63686; NGO_05650. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7849 MW; 4CEAC4E9B0F541F8 CRC64; MPNIKINFTE NVPPHIRHNA ADAAAKRGKA ISPFLSRRRV ISPFLSRRRV QTRQDRTKRE QSRQNMP // ID Q5F8V9_NEIG1 Unreviewed; 315 AA. AC Q5F8V9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 68. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW89378.2}; GN ORFNames=NGO_0651 {ECO:0000313|EMBL:AAW89378.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89378.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|SAAS:SAAS00182971}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00026557}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000256|SAAS:SAAS00545020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89378.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8V9; -. DR EnsemblBacteria; AAW89378; AAW89378; NGO_0651. DR PATRIC; 20334390; VBINeiGon24812_0767. DR HOGENOM; HOG000218999; -. DR OMA; LMKWAKR; -. DR OrthoDB; EOG6HJ238; -. DR BioCyc; NGON242231:GI2G-618-MONOMER; -. DR Proteomes; UP000000535; 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; 3.40.50.150; -; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00428966}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00429068}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW rRNA processing {ECO:0000256|SAAS:SAAS00429013}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00429032}; KW Transferase {ECO:0000256|SAAS:SAAS00429068}. FT DOMAIN 105 291 Methyltrans_SAM. FT {ECO:0000259|Pfam:PF10672}. SQ SEQUENCE 315 AA; 36489 MW; 8C0F23D6E71AE112 CRC64; MTDITPFANR LGKNIKHLMK WAKRNGIEAW RIYDRDIPQF PFAADVYGDR IHLQEYDTGW LMRPGEYEAW LAEVLEAVAF VTGFEPEQIR LKRRERQKGL QQYEKTGKAG DDFVIAENGR KFWVNLDKYL DTGFFLDHRN TRKKVGETAA GKRFLNLFSY TGSFTVYAAT GGAASSETVD LSNTYLDWAR RNFELNGIDM ERHKIVRADV FQYLQTAYGE GRQFDLIVMD PPSFSNSKKM PGILDIQRDH QKLIDGAVNL LASDGILYFS NNLRSFVLDD SVSEQYAVKD ISKQSVPEDF RNKKIHRCWE IRHKS // ID Q5F9K4_NEIG1 Unreviewed; 252 AA. AC Q5F9K4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Pseudouridylate synthase {ECO:0000313|EMBL:AAW89133.1}; GN ORFNames=NGO_0389 {ECO:0000313|EMBL:AAW89133.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89133.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89133.1; -; Genomic_DNA. DR RefSeq; WP_003687817.1; NC_002946.2. DR RefSeq; YP_207545.1; NC_002946.2. DR ProteinModelPortal; Q5F9K4; -. DR EnsemblBacteria; AAW89133; AAW89133; NGO_0389. DR GeneID; 3283021; -. DR KEGG; ngo:NGO0389; -. DR PATRIC; 20333785; VBINeiGon24812_0470. DR HOGENOM; HOG000044956; -. DR KO; K06182; -. DR OMA; HKERIFP; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; NGON242231:GI2G-368-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|SAAS:SAAS00485707}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 14 80 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 252 AA; 28063 MW; FB4F8D53CB8C3CE1 CRC64; MNSKISSDHT EDTIRLSKRM AQLGLCSRRE ADGHIEQGWV TVNGKTAVLG QKVSPADRIE LNKKAHEQQA ARITILLNKP VGYVSAQAEK GYKSAAELIT PENCWEGDTS RISFDPKHKI GLAPAGRLDI DSVGLLVLTQ DGRIAKQLIG ENSGSEKEYL VRVRGKLDEK GLALLNHGLS LDGDKLRPAK VEWQNEDQLR FVLKQGKKRQ IRRMCELVGL RVVGLKRIRM GKVKLGRLPP GKWRYLAPGE SF // ID A0A0H4IVM2_NEIG1 Unreviewed; 73 AA. AC A0A0H4IVM2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63800.1}; GN ORFNames=NGO_10970 {ECO:0000313|EMBL:AKO63800.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63800.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63800.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63800; AKO63800; NGO_10970. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 73 AA; 8341 MW; A2649A05F42A4C42 CRC64; MFGKWGGGLR ACQIKTVFKR VAMRYMQGLE AQSIYYFHRN GRPRPPCKPL KDKPPGLIRA AVGNHLPLDL FKI // ID A0A0H4IV06_NEIG1 Unreviewed; 90 AA. AC A0A0H4IV06; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63620.1}; GN ORFNames=NGO_02280 {ECO:0000313|EMBL:AKO63620.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63620.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63620.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63620; AKO63620; NGO_02280. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F8Q9_NEIG1 Unreviewed; 445 AA. AC Q5F8Q9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 80. DE SubName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000313|EMBL:AAW89428.2}; DE EC=4.1.99.12 {ECO:0000313|EMBL:AAW89428.2}; GN ORFNames=NGO_0704 {ECO:0000313|EMBL:AAW89428.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89428.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000256|SAAS:SAAS00357067}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000256|SAAS:SAAS00317988}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. {ECO:0000256|SAAS:SAAS00317950}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000256|SAAS:SAAS00534513}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89428.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8Q9; -. DR EnsemblBacteria; AAW89428; AAW89428; NGO_0704. DR PATRIC; 20334520; VBINeiGon24812_0832. DR HOGENOM; HOG000115440; -. DR OMA; ECKLPTE; -. DR OrthoDB; EOG679TK8; -. DR BioCyc; NGON242231:GI2G-668-MONOMER; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. 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 {ECO:0000313|Proteomes:UP000000535}; KW Lyase {ECO:0000313|EMBL:AAW89428.2}; KW Magnesium {ECO:0000256|SAAS:SAAS00434334}; KW Metal-binding {ECO:0000256|SAAS:SAAS00434439}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Riboflavin biosynthesis {ECO:0000256|SAAS:SAAS00434473}. FT DOMAIN 293 439 GTP_cyclohydro2. FT {ECO:0000259|Pfam:PF00925}. SQ SEQUENCE 445 AA; 48425 MW; 50368D3CEA4168FE CRC64; MTDTAGLRRR NLRQWIAEHY GGLQNRFAEA VALNTGELSA LLKNKSFGEK KARKIEQAAK MPAFWLDTEH TGRPPGHTGK HTMSHISPIP EILADIKAGK MVIITDAEDR ENEGDLLMAA QFVTPEAVNF MIKHARGLVC LPMEGAMVEK LGLPMMTQKN GAQYGTNFTV SIEAAHGITT GISAADRALT IQTAVSPTAK PADIVQPGHI FPLRAQKGGV LVRAGHTEAG VDLAQMNGLI PAAVICEIIN DDGTMARMPE LMKFAEEHKL KIGTIADLIE YRSRTESLLE DMGDAPVQTP WGEFQQHVYV DKLSGETHLA LVKGTPSADT ETLVRVHEPF SVMDFIQANP RHSWSLPKAL ERVQQAESGV VILLHHTEDG ASLLDRTLPK GANQAYKWDS KSYGIGAQIL AGLHVKKLRV LGQPSSFTGL TGFGLEVVGF EEAEK // ID A0A0H4IVZ5_NEIG1 Unreviewed; 93 AA. AC A0A0H4IVZ5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AKO63598.1}; GN ORFNames=NGO_00685 {ECO:0000313|EMBL:AKO63598.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63598.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63598.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63598; AKO63598; NGO_00685. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 51 ABC transporter. FT {ECO:0000259|Pfam:PF00005}. SQ SEQUENCE 93 AA; 10118 MW; 5CBB270F14ABE15C CRC64; MIREEISAMP MGYETLIGDM GSALSGGQKQ RIVLARALYC EPKILFLDEA ASHLDIANEK AVNANLNGLS IIKIMAAHRK ETVESADRKM SLG // ID Q5F7L4_NEIG1 Unreviewed; 217 AA. AC Q5F7L4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 42. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89823.1}; GN ORFNames=NGO_1157 {ECO:0000313|EMBL:AAW89823.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89823.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89823.1; -; Genomic_DNA. DR RefSeq; WP_010951203.1; NC_002946.2. DR RefSeq; YP_208235.1; NC_002946.2. DR EnsemblBacteria; AAW89823; AAW89823; NGO_1157. DR GeneID; 3282205; -. DR KEGG; ngo:NGO1157; -. DR PATRIC; 20335583; VBINeiGon24812_1356. DR HOGENOM; HOG000218644; -. DR OMA; GWEFRLN; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-1069-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24123 MW; 51837E7F642ADE96 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFERPAGPG GSCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADNA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP FLKGWEFRLN FGTPPRQLKI LRDRCGI // ID Q5FA33_NEIG1 Unreviewed; 217 AA. AC Q5FA33; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 47. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW88954.1}; GN ORFNames=NGO_0201 {ECO:0000313|EMBL:AAW88954.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88954.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88954.1; -; Genomic_DNA. DR RefSeq; WP_010951010.1; NC_002946.2. DR RefSeq; YP_207366.1; NC_002946.2. DR EnsemblBacteria; AAW88954; AAW88954; NGO_0201. DR GeneID; 3281705; -. DR KEGG; ngo:NGO0201; -. DR PATRIC; 20333335; VBINeiGon24812_0250. DR HOGENOM; HOG000218644; -. DR OMA; MLGIHPN; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-184-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24058 MW; 290A7F3375670FF4 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV ANHRLALAAD EVFEGPAGPG ASCFGVRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADDA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP FLRECEFRLN FGTPSRQLKI LRDRCGI // ID Q5F8K3_NEIG1 Unreviewed; 415 AA. AC Q5F8K3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=Permease {ECO:0000313|EMBL:AAW89484.1}; GN ORFNames=NGO_0769 {ECO:0000313|EMBL:AAW89484.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89484.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000256|SAAS:SAAS00573676}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89484.1; -; Genomic_DNA. DR RefSeq; WP_003706248.1; NC_002946.2. DR RefSeq; YP_207896.1; NC_002946.2. DR EnsemblBacteria; AAW89484; AAW89484; NGO_0769. DR GeneID; 3282005; -. DR KEGG; ngo:NGO0769; -. DR PATRIC; 20334686; VBINeiGon24812_0915. DR HOGENOM; HOG000218040; -. DR KO; K09808; -. DR OMA; YVKHVTF; -. DR OrthoDB; EOG68SVTW; -. DR BioCyc; NGON242231:GI2G-724-MONOMER; -. DR Proteomes; UP000000535; 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: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 membrane {ECO:0000256|SAAS:SAAS00573687}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00573687, KW ECO:0000256|SAAS:SAAS00573714, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 20 47 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 316 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 398 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 26 241 MacB_PCD. {ECO:0000259|Pfam:PF12704}. FT DOMAIN 275 408 FtsX. {ECO:0000259|Pfam:PF02687}. SQ SEQUENCE 415 AA; 45407 MW; 490164F9F6057CA7 CRC64; MFSLEAWIGL RYLRAKKRNG FMSFITMVSI AGIALGVTAL IVVLSVMNGF QKEIRGQLLN VAPHAEIGYI DNTDTDWRNL LRFAENRKGI LAAAPYVSNQ ALLANAGEIR GVQIRGILPS EERKVVEYGD KMPAGKFEDL IPGEFDIILG IGLAEALGAE VGDKVTVITP EGNVTPAGIV PRLKQFTVVG LVKTGVYEVD NSLAMTHIQD ARVLYRLDKE VAGLRLKLAD PQNAPALTAT LIPEAQRDTV WVRDWTYSNR SYFEAVELEK RMMFIILTLI IAVAAFNLVS SLVMAVTEKQ ADIAILRTLG LSPAGVMKIF MVQGAFSGFF GTLAGVVCGV LWGWNVGRVV AFFENLLGVH LINSQVYFID YLPSDVDMGD VALIACISLG LSFVATLYPS WRASKTQPAE ALRYE // ID A0A0H4J5C8_NEIG1 Unreviewed; 63 AA. AC A0A0H4J5C8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63607.1}; GN ORFNames=NGO_01225 {ECO:0000313|EMBL:AKO63607.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63607.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63607.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63607; AKO63607; NGO_01225. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR032869; WHH_dom_containing. DR Pfam; PF14414; WHH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 7450 MW; 70AB26690A7AFD54 CRC64; MRLSDGIFDI KRITKEMFDG KGTSEIPNYT WHHHQDTGRM QLIREDSHHD TDHIGWRAMS KGK // ID Q5F7D5_NEIG1 Unreviewed; 289 AA. AC Q5F7D5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=3-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AAW89902.1}; GN ORFNames=NGO_1243 {ECO:0000313|EMBL:AAW89902.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89902.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89902.1; -; Genomic_DNA. DR RefSeq; WP_003692220.1; NC_002946.2. DR RefSeq; YP_208314.1; NC_002946.2. DR ProteinModelPortal; Q5F7D5; -. DR EnsemblBacteria; AAW89902; AAW89902; NGO_1243. DR GeneID; 3282154; -. DR KEGG; ngo:NGO1243; -. DR PATRIC; 20335805; VBINeiGon24812_1462. DR HOGENOM; HOG000219608; -. DR KO; K00020; -. DR OMA; VPVETFM; -. DR OrthoDB; EOG62RS92; -. DR BioCyc; NGON242231:GI2G-1155-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 30250 MW; 8CA1C52FD8C06A27 CRC64; MSAETYTQIG WVGLGQMGLP MVTRLLDGGI EVGVYNRSPD KTAPISAKGA KVYGSTAELV RACPVIFLMV SDYAAVCDIL NGVRDGLAGK IIVNMSTISP TENLAVKALV EAAGGQFAEA PVSGSVGPAT NGTLLILFGG SEAVLNPLQK IFSLVGKKTF HFGDVGKGSG AKLVLNSLLG IFGEAYSEAM LMARQFGIDT DTIVEAIGGS AMDSPMFQTK KSLWANREFP PAFALKHASK DLNLAVKELE QAGNTLPAVE TVAASYRKAV EAGYGEQDVS GVYLKLAEH // ID A0A0H4IRL6_NEIG1 Unreviewed; 162 AA. AC A0A0H4IRL6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63601.1}; GN ORFNames=NGO_00795 {ECO:0000313|EMBL:AKO63601.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63601.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63601.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63601; AKO63601; NGO_00795. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 162 AA; 18500 MW; B634A07B36D305F3 CRC64; MTRPAGFSDC QRVCPDETGF DRRLFRPYAR SLKGQMAKAR IRVKRYRRLS LVSAQVGNRP IAPMVCQNTV AGVFFEARFQ QCLLPALAQK SVIISDNARF RRMGALRGTA EKLGHKVLPP APYSPEPNPI EKVWANIKRY LRTVLSDYAR FDDALLSYFD FN // ID Q5F9S3_NEIG1 Unreviewed; 200 AA. AC Q5F9S3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=Chromosome segregation protein ScpB {ECO:0000313|EMBL:AAW89064.1}; GN ORFNames=NGO_0317 {ECO:0000313|EMBL:AAW89064.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89064.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89064.1; -; Genomic_DNA. DR RefSeq; WP_002235622.1; NC_002946.2. DR RefSeq; YP_207476.1; NC_002946.2. DR ProteinModelPortal; Q5F9S3; -. DR EnsemblBacteria; AAW89064; AAW89064; NGO_0317. DR GeneID; 3281739; -. DR KEGG; ngo:NGO0317; -. DR PATRIC; 20333617; VBINeiGon24812_0388. DR HOGENOM; HOG000242838; -. DR KO; K06024; -. DR OMA; WATTPHF; -. DR OrthoDB; EOG6CZQQQ; -. DR BioCyc; NGON242231:GI2G-297-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0051304; P:chromosome separation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 2. DR InterPro; IPR005234; ScpB_csome_segregation. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF04079; SMC_ScpB; 1. DR PIRSF; PIRSF019345; ScpB; 1. DR SUPFAM; SSF46785; SSF46785; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 200 AA; 22477 MW; 5CB5BED6600D2856 CRC64; MTDKISPDAL IEAALLTQTE PLTEKSMREL CVPPLSQDKL IDVLAQLKTR WQDRALQLVH TQEGWRFQIV QTAFERLGSL QEQRAPRYSR AVMETLAIIA YQQPVTRGDI EGIRGVAVSQ NVMQTLQDRG WIEVIGHRDT LGKPALWATT ATFLSDLRLD GLEELPPLTE LGELVLPDLI EMPPTDEEEP ETVPSDTLPN // ID A0A0H4J5C4_NEIG1 Unreviewed; 58 AA. AC A0A0H4J5C4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63602.1}; GN ORFNames=NGO_00870 {ECO:0000313|EMBL:AKO63602.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63602.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63602.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63602; AKO63602; NGO_00870. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 58 AA; 6854 MW; C2423381523D6882 CRC64; MGEYLEFEES GTKITVEIGS AWHFNETIRN INTHLRGTKL PGSNWRVQDK GHFHLWKR // ID A0A0H4J5G8_NEIG1 Unreviewed; 314 AA. AC A0A0H4J5G8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63642.1}; GN ORFNames=NGO_03725 {ECO:0000313|EMBL:AKO63642.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63642.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63642.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63642; AKO63642; NGO_03725. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 314 AA; 35684 MW; 150FBC1407FFD397 CRC64; MFYVNYGRSI GGTPDEENFD GHRKEGGSNN YAVHYSAPFG KWTWAFNHNG YRYHQAVSGL SEVYDYNGKS YNTDFGFNRL LYRDAKRKTY LSVKLWTRET KSYIDDAELT VQRRKTTGWL AELSHKGYIG RSTADFKLKY KHGTGMKDAL RAPEEAFGEG TSRMKIWTAS ADVNTPFQIG KQLFAYDTSV HAQWNKTPLT SQDKLAIGGH HTVRGFDGEM SLPAERGWYW RNDLSWQFKP GHQLYLGADV GHVSGQSAKW LSGQTLAGTA IGIRGQIKLG GNLHYDIFTG RALKKPEYFQ TKKWVTGFQV GYSF // ID Q5F6R8_NEIG1 Unreviewed; 260 AA. AC Q5F6R8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 70. 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 ORFNames=NGO_1481 {ECO:0000313|EMBL:AAW90119.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90119.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90119.1; -; Genomic_DNA. DR RefSeq; WP_003689357.1; NC_002946.2. DR RefSeq; YP_208531.1; NC_002946.2. DR ProteinModelPortal; Q5F6R8; -. DR DNASU; 3281631; -. DR EnsemblBacteria; AAW90119; AAW90119; NGO_1481. DR GeneID; 3281631; -. DR KEGG; ngo:NGO1481; -. DR PATRIC; 20336411; VBINeiGon24812_1753. DR HOGENOM; HOG000003262; -. DR KO; K02169; -. DR OMA; SADYWLF; -. DR OrthoDB; EOG6GXTQ5; -. DR BioCyc; NGON242231:GI2G-1385-MONOMER; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00835, KW ECO:0000256|SAAS:SAAS00444274, ECO:0000313|EMBL:AAW90119.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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, ECO:0000313|EMBL:AAW90119.1}. FT DOMAIN 54 146 Methyltransf_11. FT {ECO:0000259|Pfam:PF08241}. SQ SEQUENCE 260 AA; 29670 MW; 8B0798E30193970B CRC64; MESLTAINKP RIRQAFQKAL SDYDRHALIQ QKMTINLIAH LQDYLPDMPL ENVLELGCGS GMLSALLQKQ ISANYWLFND LCDVRSRLAE KLPQSFDFYC GDAENFPFQR QFDLIASASA VQWFHQPDAF IAHCKTGLKT NGLLAVATFG KDNLKEVRQI TNIGLNYPTL SQWQAWLAKD FELLWCEDFK VILDFDTPLD VLKHLKYTGV TATNQKNWTR KNLNGFIGDY LSAFGMPSGK VRLTYHPLFF IARHSAAGRQ // ID Q5F6R2_NEIG1 Unreviewed; 630 AA. AC Q5F6R2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Arginine decarboxylase {ECO:0000256|RuleBase:RU003740, ECO:0000256|SAAS:SAAS00212226}; DE EC=4.1.1.19 {ECO:0000256|RuleBase:RU003740, ECO:0000256|SAAS:SAAS00212226}; GN ORFNames=NGO_1487 {ECO:0000313|EMBL:AAW90125.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90125.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2). CC {ECO:0000256|RuleBase:RU003740, ECO:0000256|SAAS:SAAS00212228}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU003740}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|PIRSR:PIRSR001336-50}; CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. {ECO:0000256|RuleBase:RU003737}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90125.1; -; Genomic_DNA. DR RefSeq; WP_003689369.1; NC_002946.2. DR RefSeq; YP_208537.1; NC_002946.2. DR ProteinModelPortal; Q5F6R2; -. DR EnsemblBacteria; AAW90125; AAW90125; NGO_1487. DR GeneID; 3281576; -. DR KEGG; ngo:NGO1487; -. DR PATRIC; 20336425; VBINeiGon24812_1760. DR HOGENOM; HOG000029191; -. DR KO; K01585; -. DR OMA; DQLFPIM; -. DR OrthoDB; EOG676Z0R; -. DR BioCyc; NGON242231:GI2G-1391-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 2.40.37.10; -; 2. DR Gene3D; 3.20.20.10; -; 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 {ECO:0000313|Proteomes:UP000000535}; KW Decarboxylase {ECO:0000256|RuleBase:RU003740, KW ECO:0000256|SAAS:SAAS00467027}; KW Lyase {ECO:0000256|RuleBase:RU003740, ECO:0000256|SAAS:SAAS00467027}; KW Magnesium {ECO:0000256|SAAS:SAAS00417966}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001336-50, KW ECO:0000256|SAAS:SAAS00418093}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Spermidine biosynthesis {ECO:0000256|RuleBase:RU003740, KW ECO:0000256|SAAS:SAAS00417951}. FT DOMAIN 71 340 Orn_Arg_deC_N. FT {ECO:0000259|Pfam:PF02784}. FT DOMAIN 366 555 Orn_DAP_Arg_deC. FT {ECO:0000259|Pfam:PF00278}. FT MOD_RES 99 99 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001336-50}. SQ SEQUENCE 630 AA; 71053 MW; A9B941A04B6D707F CRC64; MPILTIREVC NINHWSIGYY DVDDSGEIIV RPNPSQHNQT VSLQKLTEAV QQKHQARLPV LFCFPQILEH RLRDINRAFQ TAREECGYKG GYCLVYPIKV NQHRRVIESL MSSGQPHGLE AGSKAELMAV LAHAGTRQTL 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 FLGFFMVGAY QEILGNMHNL FGDTATADVV VREDGQFTVI DYDEGNTVAD MLEYVYQDPK ELMKRYREQI EHSDLPASQA MSFLKELEAG LNGYTYLEDE // ID Q5F4X7_NEIG1 Unreviewed; 308 AA. AC Q5F4X7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE RecName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000256|PIRNR:PIRNR000446}; DE EC=2.3.1.39 {ECO:0000256|PIRNR:PIRNR000446}; GN ORFNames=NGO_2166 {ECO:0000313|EMBL:AAW90760.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90760.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90760.1; -; Genomic_DNA. DR RefSeq; WP_010951418.1; NC_002946.2. DR RefSeq; YP_209172.1; NC_002946.2. DR ProteinModelPortal; Q5F4X7; -. DR SMR; Q5F4X7; 3-299. DR EnsemblBacteria; AAW90760; AAW90760; NGO_2166. DR GeneID; 3282758; -. DR KEGG; ngo:NGO2166; -. DR PATRIC; 20338188; VBINeiGon24812_2616. DR HOGENOM; HOG000036503; -. DR KO; K00645; -. DR OMA; FHCALMQ; -. DR OrthoDB; EOG6W19KW; -. DR BioCyc; NGON242231:GI2G-2054-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR000446}. FT ACT_SITE 90 90 {ECO:0000256|PIRSR:PIRSR000446-1}. FT ACT_SITE 199 199 {ECO:0000256|PIRSR:PIRSR000446-1}. SQ SEQUENCE 308 AA; 32030 MW; D0C0936BCFFA2988 CRC64; MSFAFFFPGQ GSQSLGMMNG FAEHVIVKNT FDEASAILGQ DLWAMINGSD AEIIGQTVNT QPIMLAAGVA VYRAYLEVGG KTPAAVAGHS LGEYTALVAA EALDFADAVK LVRLRAELMQ SAVPQGVGAM AAILGLEDEQ VRQICAESAQ GEVVEAVNFN SPGQVVIAGN AAAVGRTMAA AKEAGAKRAL PLPVSVPSHC SLMKPAADKL AETLKTVEIK QPQIRVIHNA DVAAYDDAGK IKDALVRQLY SPVRWTETVN ALVSDGIAES AECSPGKVLA GLAKRINKAA ACSALTDAGQ ITAFIEAH // ID A0A0H4IWE9_NEIG1 Unreviewed; 86 AA. AC A0A0H4IWE9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63753.1}; GN ORFNames=NGO_08465 {ECO:0000313|EMBL:AKO63753.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63753.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63753.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63753; AKO63753; NGO_08465. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 9915 MW; 9018E7522FD8D0F1 CRC64; MLLPRQHLGQ NGRRLKSKHR PSCCRLRMST GQPQCRRNRR SRLQHCHRQS REVGKNGKTG EIKADGRKVN VRIDSTEADL LYPAGQ // ID A0A0H4IRW3_NEIG1 Unreviewed; 77 AA. AC A0A0H4IRW3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63661.1}; GN ORFNames=NGO_04470 {ECO:0000313|EMBL:AKO63661.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63661.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63661.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63661; AKO63661; NGO_04470. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 77 AA; 9033 MW; EA2B6E59A5D2521B CRC64; MFPSLLVCPV SLPPCTAEFA LFCRNCQQSR RICNKIDKMY KINKIYSNLL RFFQINIAVL SKMRIILSIF LLRADLF // ID Q5FA85_NEIG1 Unreviewed; 274 AA. AC Q5FA85; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Cation transporter {ECO:0000313|EMBL:AAW88902.1}; GN ORFNames=NGO_0144 {ECO:0000313|EMBL:AAW88902.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88902.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88902.1; -; Genomic_DNA. DR RefSeq; WP_003687434.1; NC_002946.2. DR RefSeq; YP_207314.1; NC_002946.2. DR ProteinModelPortal; Q5FA85; -. DR SMR; Q5FA85; 191-274. DR DNASU; 3281301; -. DR EnsemblBacteria; AAW88902; AAW88902; NGO_0144. DR GeneID; 3281301; -. DR KEGG; ngo:NGO0144; -. DR PATRIC; 20333201; VBINeiGon24812_0183. DR HOGENOM; HOG000062294; -. DR KO; K06189; -. DR OMA; QMISIKA; -. DR OrthoDB; EOG60W7V4; -. DR BioCyc; NGON242231:GI2G-132-MONOMER; -. DR Proteomes; UP000000535; 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; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 64 123 CBS. {ECO:0000259|PROSITE:PS51371}. FT DOMAIN 128 185 CBS. {ECO:0000259|PROSITE:PS51371}. SQ SEQUENCE 274 AA; 31062 MW; 385919800B9361F5 CRC64; MDGAQPKTNF FERLIARLAR EPDSAEDVLN LLRQAHEQEV FDADTLTRLE KVLDFAELEV RDAMITRSRM NVLKENDSIE RITAYVIDTA HSRFPVIGED KDEVLGILHA KDLLKYMFNP EQFHLKSVLR PAVFVPEGKS LTALLKEFRE QRNHMAIVID EYGGTSGLVT FEDIIEQIVG DIEDEFDEDE SADNIHSVSA ERWRIHAATE IEDINAFFGT EYGSEEADTI GGLVIQELGH LPVRGEKVLI GGLQFTVARA DNRRLHTLMA TRVK // ID A0A0H4J5P6_NEIG1 Unreviewed; 67 AA. AC A0A0H4J5P6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63707.1}; GN ORFNames=NGO_06850 {ECO:0000313|EMBL:AKO63707.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63707.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63707.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63707; AKO63707; NGO_06850. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7785 MW; 1D8D10DB88A48D82 CRC64; MVALDKVLMN AKYEGSFPNK LGRDHIIAVH KYSTGVRFGN KVLKIRIIAR EKFDGIKHYD HFILKDK // ID A0A0H4IVM8_NEIG1 Unreviewed; 252 AA. AC A0A0H4IVM8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Large pilS cassette {ECO:0000313|EMBL:AKO63810.1}; GN ORFNames=NGO_11130 {ECO:0000313|EMBL:AKO63810.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63810.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63810.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63810; AKO63810; NGO_11130. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 252 AA; 27178 MW; E2A048D4BFE4210B CRC64; MAEGQKSAVT EYYLNHGIWP ENNDKAGVAS SSSIKGKYVK EVKVENGVVT ATMNSSNVNK EIKDKRLSLW AKRENGSVKW FCGQPVKRAN VAAANDDDVT DDKNNNGIDT KHLPSTCRDK SSAVCTKHHA PISNTSKKSA VTEYCPNHGE WPKDNDKAGV ASPPSNIKGK YVESVTVTNG VVTATMLSSG VNNEIKGKKL SLWAKRQAGS VKWFCGQPVQ RAKADDAVTA DANNAIDTKH LPSTCRDTSS AK // ID A0A0H4IWE5_NEIG1 Unreviewed; 227 AA. AC A0A0H4IWE5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63748.1}; GN ORFNames=NGO_08325 {ECO:0000313|EMBL:AKO63748.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63748.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63748.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63748; AKO63748; NGO_08325. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 82 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 135 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 227 AA; 24830 MW; BFBFB585427A39CD CRC64; MGGRRLPYLL YGTLIAVIVM ILMPNSGSFG FGYASLAALS FGALMIALLD VSSNMAMQPF KMMVGDMVNE EQKSYAYGIQ SFLANTDAVV AAILPFVFAY IGLANTAEKG VVPQTVVVAF YVGAALLIIT SAFTISKVKE YDPETYARYH GIDVAANQEK ANWFELLKTA PKVFWTVTPV QFFCWFAFRY MWTYSAGAIA ENVWHTTDAS SVGHQEAGNR YGVLAAV // ID Q5F5H1_NEIG1 Unreviewed; 1389 AA. AC Q5F5H1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90566.1}; GN ORFNames=NGO_1955 {ECO:0000313|EMBL:AAW90566.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90566.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90566.1; -; Genomic_DNA. DR RefSeq; WP_003705164.1; NC_002946.2. DR RefSeq; YP_208978.1; NC_002946.2. DR EnsemblBacteria; AAW90566; AAW90566; NGO_1955. DR GeneID; 3282666; -. DR KEGG; ngo:NGO1955; -. DR PATRIC; 20337653; VBINeiGon24812_2353. DR HOGENOM; HOG000218696; -. DR KO; K09800; -. DR OMA; DTPWSSS; -. DR OrthoDB; EOG6Z3KF9; -. DR BioCyc; NGON242231:GI2G-1856-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 57 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 1389 AA; 147240 MW; 56ABA42926418313 CRC64; MTDTTPTDTD PTENGTRKMP SEHRPAPPAK KRRPLLKLSA ALLSVLILAV CFLGWIAGTE AGLRFGLYQI PSWFGVNISS QNLKGTLLDG FDGDNWSIET EGADLKISRF RFAWKPSELM RRSLHITDIS AGDIAIVTKP TPPKEERPPQ GLPDSIDLPA AVYLDRFETG KISMGKTFDK QTVYLERLNA AYRYDRKGHR LDLKAADTPW SSSSGSASVG LKKPFALDTA IYTKGGFEGE TIHSTARLSG SLKDVRAELT IDGGNIRLSG KSVIHPFAES LDKTLEEVLV KGFNINPSAF VPSLPDAGLN FDLTAIPSFS DGIALEGSLD LENTKAGFAD RNGIPVRQVL GGFVIRQDGT VHIGNTSAAL LGRGGIRLSG KIDTEKDILD LNIGINSVGA EDVLQTAFKG RLDGSIGIGG TTASPKISWQ LGTGTARTDG SLAIASDPAN EQRKLVFDTV NISAGEGSLT AQGYLELFKD RLLKLDIRSR AFDPSRIDPQ FPAGNINGSI HLAGELAKEK FTGKMRFLPG TFNGVPIAGS ADIVYESRHL PRAAVDLRLG RNIVKTDGGF GKKGDRLNLN ITAPDLSRFG FGLAGSLNVR GHLSGDLDGG IRTFETDLSG TARNLHIGKA ADIRSLDFTL KGSPGTSRPM RADIKGGRLS LSGGAAVVDT AGLTLEGTGA QHRIRTHAAM TLDGKPFKLD LDASGGINRE LTRWKGSIGI LDIGGAFNLK LQNRMTLEAG AEHVAASAAN WQAMGGSLNL QHFSWDRKTG ISAKGGARGL HIAELHNFFK PPFEHNLVLN GDWDVAYGHN ARGYLNISRQ SGDAVLPGGQ ALGLNAFSLK TRFQNDRIGI LLDGGARFGR INADLGIGNA FGGNMANTPL GGRITASLPD LGALKPFLPA AAQNITGSLN ASAQIGGRVG SPSVNAAVNG SSNYGKINGN ITVGQSRSFD TAPLGGRLNL TVADAEAFRN FLPVGQTVKG SLNAAVTLGG SIADPHLGGS INGDKLYYRN QTQGIILDNG SLRSHIAGRK WVIDSLKFRH EGTAELSGTV SMENSVPDVD IGAVFDKYRI LSRPNRRLTV SGNTRLRYSP QKGISVTGMI KTDQGLFGSQ KSSMPSVGDD VVVLGEVKKE AAASLPVNMN LTLDLNDGIR FSGYGADVTI GGKLTLTAQP GGNVRGVGTV RVIKGRYKAY GQDLDITKGT VSFVGPLNDP NLNIRAERRL SPVGAGVEIL GSLNSPRITL TANEPMSEKD KLSWLILNRA GSGSSGDNAA LSAAAGALLA GQINDRIGLV DDLGFTSKRS RNAQTGELNP AEQVLTVGKQ LTGKLYIGYE YGISSAEQSV KLIYRLTRAI QAVARIGSRS SGGELTYTIR FDRLFGSDKK DSAGNGKGK // ID A0A0H4J600_NEIG1 Unreviewed; 290 AA. AC A0A0H4J600; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=MAFB alternative {ECO:0000313|EMBL:AKO63797.1}; GN ORFNames=NGO_10585 {ECO:0000313|EMBL:AKO63797.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63797.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63797.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63797; AKO63797; NGO_10585. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 290 AA; 31153 MW; 7DDF7DAA90E3253A CRC64; MGINANPNCA DEAGKLIWED DPDKNWRANR MDDIRGIVQG AVNPFLTGFQ GVGIGAITDS AVSPVTDTAA QQTLQGINDL GKLSPEAQLA AASLLQDSAF AVKDGINSAK QWADAHPNIT ATAQTALAVA EAAGTVWGGK KVELNPAKWD WVKNTGYKTP AVRTMHTLDG EMAGGNRPPK SITSNSKADA STQPSLQAQL IGEQISSGHA YNKHVIRQQE FTDLNINSPA DFARHIENIV SHPTNMKELP RGRTAYWDDK TGTIVIRDKN SDDGGTAFRP TSGKKYYDDL // ID Q5F8V3_NEIG1 Unreviewed; 349 AA. AC Q5F8V3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 80. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887}; GN ORFNames=NGO_0657 {ECO:0000313|EMBL:AAW89384.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89384.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89384.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8V3; -. DR EnsemblBacteria; AAW89384; AAW89384; NGO_0657. DR PATRIC; 20334406; VBINeiGon24812_0775. DR HOGENOM; HOG000044954; -. DR OMA; MEEWINN; -. DR OrthoDB; EOG6130DV; -. DR BioCyc; NGON242231:GI2G-624-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 97 158 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 349 AA; 39476 MW; C8F0B29AE7E6E36E CRC64; MSKQPTSKRQ WRDGAAPSAK KTAKPFKSKA RPKDETRKTA AQAYGQKASD GIKLQNAPKQ RAAKAKKLVV RNPNQKIMEH ARDLKERRSD LSRMEPERLQ KVLAASGVGS RREMEEWINN GWVTVNGKTA QLGDKVTPDD HVTVKGSIIK LKWADRLPRI ILYYKQEGEI VSRDDPQGRV SIFDRLPQAA SSRWVAIGRL DINTSGLLIL TTSGELVQRF AHPSFEVERE YAVRVLGGLT TEQMRSLTEE GVMLEDGLAK VERIYEQGGE GANKWYNIVI KEGRNREVRR IFESQGLTVS RLVRVAFGPI GLPNRLKRGQ FYELNPAEVA NILKWADMLL PGERRRKKA // ID A0A0H4IS76_NEIG1 Unreviewed; 140 AA. AC A0A0H4IS76; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63766.1}; GN ORFNames=NGO_09325 {ECO:0000313|EMBL:AKO63766.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63766.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63766.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63766; AKO63766; NGO_09325. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 15490 MW; 1C0F3487EFFA26D3 CRC64; MPDNLILISV LAKPSPTHAR KTLIGGYHIA AFQTDLDGRI DRMRADLPSL TMVKLGKPLP RKGGIRIGFD IALSVGENIS VCRLNIGITA FQFANNRNRT DCSDTAKNKC RLKPGLSGFR RHFLFRRLPL PPRTLPATIS // ID Q5F9M3_NEIG1 Unreviewed; 1200 AA. AC Q5F9M3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 85. 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 ORFNames=NGO_0370 {ECO:0000313|EMBL:AAW89114.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89114.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89114.1; -; Genomic_DNA. DR RefSeq; WP_010951035.1; NC_002946.2. DR RefSeq; YP_207526.1; NC_002946.2. DR ProteinModelPortal; Q5F9M3; -. DR EnsemblBacteria; AAW89114; AAW89114; NGO_0370. DR GeneID; 3282190; -. DR KEGG; ngo:NGO0370; -. DR PATRIC; 20333741; VBINeiGon24812_0448. DR HOGENOM; HOG000258330; -. DR KO; K03582; -. DR OMA; IMIGDPK; -. DR OrthoDB; EOG6677M1; -. DR BioCyc; NGON242231:GI2G-349-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. 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 1200 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 1200 AA; 134269 MW; 572B55C3174DDECB CRC64; MSAPIRAFDP LTAPISGTNL IEASAGTGKT YGIAALFTRL IVLEQKSVER VLVVTFTKAA TAELKTRLRA RLDDVLQVLE SKEIAELGDD TLSDGIAAYC AEHHEGDTFL PALLEQALQK ESRTRLIVRL KAAIGQFDNA AIYTIHGFCQ RILRDYAFLC QAPFDVELTE EDGDRLLVPA QDFWRERVSG DPVLAALAFK RKAVPQTVLA QIRAYLSRPY LNFRRPQADL KQAQRDAETS WQTVCRLLPE LEAGFWRIHP DLNGNSYRKN SFGNLFKELA QKSAAGQLPC LDKDTHERLL KLSSDKLEAG LKKGKTPDAA VFAELQKLAD FGRDLNALEE AEETTMIRLQ LDLIEYLNSS LAEMKKSRRE RGFDDLLLDV HTALTDNPHA ETPARAVAEN WEIALIDEFQ DTDPLQYEIF QKIFIARNRP LFLVGDPKQA IYSFRGADIY AYLQAAEDAR HRYTLATNYR SHAALIGSIG ALFRLKERPF VLENIGYSEV GAARAESRLS PKRPAVQLRW LHENDNEKAN KDVLRRRAAD YCADEIARAL NEASGGRLNF KDRPLQSGDI AVLVRTHNEA VMISAALKKR QVQSVLLSRE SVFASPEAAA LSALIGFWLE PRRAGTLRFV LTSGIFGYDA QQLHDFNQNE SEILHWAESA RTALDIWQKY GIFAAMQQFS QTHGIETRLL SRNNGRSLTN YFQLLELLAA EDAQNRNPAA LHKWLRDQIS LAGNNGGDNR AIRLESDEDL VKIVTMHASK GLQYPLVYCP FAWDAQDTGP SDWQILHQGA NRAELLAKAQ LSESEQKQYA DEEMAERLRL LYVALTRAEE QLNIYAAYSS DTADNPLAYL IEGLPQDSRE TVRRTYACEK DGITMLKRNW RRVADNAPAG TDFTFTEDAP PPAAYRGNAD QAAEFAANSI PERGFRFVRH TSFTALSRHT QTPDGGEEDA CPSLDAAETS VPAMPSETPT ASDGISIHDF PKGTQAGLCL HEILEDFKFG QAAAEQETLI ADKLKKYGFE EIWLPAVAEM AEACRKTPLT GAYGLSDIPP GCRRPEMGFT LHTEDFGLKR LRDWLARDDI RLPEVCRAAA ETLDFHTVNG FLNGFIDMVC QDPDGNICII DYKSNHLSAY TRQAMDEAVA HQHYYLQALI YAVAAARYFK LRGQPPAAVS VRYLFLRGLD GKGGGVWRWD IDAAALEQIK // ID Q5F902_NEIG1 Unreviewed; 230 AA. AC Q5F902; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, 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 ORFNames=NGO_0607 {ECO:0000313|EMBL:AAW89335.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89335.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89335.1; -; Genomic_DNA. DR RefSeq; WP_003688930.1; NC_002946.2. DR RefSeq; YP_207747.1; NC_002946.2. DR ProteinModelPortal; Q5F902; -. DR EnsemblBacteria; AAW89335; AAW89335; NGO_0607. DR GeneID; 3281619; -. DR KEGG; ngo:NGO0607; -. DR PATRIC; 20334294; VBINeiGon24812_0719. DR HOGENOM; HOG000044954; -. DR KO; K06183; -. DR OMA; TVIYLTI; -. DR OrthoDB; EOG6TFCPK; -. DR BioCyc; NGON242231:GI2G-575-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU003887, KW ECO:0000256|SAAS:SAAS00429931}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW RNA-binding {ECO:0000256|SAAS:SAAS00568463}. FT DOMAIN 1 69 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 230 AA; 26150 MW; 85B10E5D5EAED7D9 CRC64; MKLIKYLQYQ GIGSRKQCQW LIRGGYVSIN GTCMDDTDAD IDSSYVETLD IDGEAVTVVP EPYFYILLNK PEDYETSHKP KHYRSVFSLF PDNMRNIDMQ AVGRLDADTT GVLLITNDGK LNHNLTSPSR KIPKLYEVTL KHPTGETLCE TLKNGVPLHD ENETVCAADA VLENPTTLLL TITEGKYHQV KRMVAAAGNR VQHLHRRRFA HLETENLKPG EWKFIECPKF // ID A0A0H4IVH3_NEIG1 Unreviewed; 109 AA. AC A0A0H4IVH3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63745.1}; GN ORFNames=NGO_08305 {ECO:0000313|EMBL:AKO63745.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63745.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63745.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63745; AKO63745; NGO_08305. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR012341; 6hp_glycosidase. DR InterPro; IPR005195; Glyco_hydro_65_M. DR Pfam; PF03632; Glyco_hydro_65m; 1. DR SUPFAM; SSF48208; SSF48208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 109 Glyco_hydro_65m. FT {ECO:0000259|Pfam:PF03632}. SQ SEQUENCE 109 AA; 12620 MW; 5AFC6704527E9E83 CRC64; MPQAQHNARE QGLAGALYPM VTFTGIECHN EWEITFEEIH RNGAIPYAIY NYTNYTGDEC YLAKEGLEVL VEVSRFRADR VHFSKRNGKY MIQGVTGPNE YENNINNNW // ID Q5F670_NEIG1 Unreviewed; 158 AA. AC Q5F670; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:AAW90317.1}; GN ORFNames=NGO_1693 {ECO:0000313|EMBL:AAW90317.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90317.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90317.1; -; Genomic_DNA. DR RefSeq; WP_003689851.1; NC_002946.2. DR RefSeq; YP_208729.1; NC_002946.2. DR ProteinModelPortal; Q5F670; -. DR EnsemblBacteria; AAW90317; AAW90317; NGO_1693. DR GeneID; 3281185; -. DR KEGG; ngo:NGO1693; -. DR PATRIC; 20336950; VBINeiGon24812_2019. DR HOGENOM; HOG000004483; -. DR OMA; VWEVDVF; -. DR OrthoDB; EOG6DC6QR; -. DR BioCyc; NGON242231:GI2G-1587-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 18586 MW; FF771D5DA869AE5A CRC64; MPIEIERRFL IENDKWRQYA DEPLLLKQGY LSVEKERTIR IRIAGKRAWL TLKGYISEIS RSEFEYEIPL ADAEKMMETM CPFKMEKRRY PVRWGGSLFE VDVFLGENSP LVVAEIELPA ENADFDRPDW LGREITSDGM FTNAYLSKHP FSSWKNAV // ID Q5F6V5_NEIG1 Unreviewed; 392 AA. AC Q5F6V5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW90082.1}; GN ORFNames=NGO_1440 {ECO:0000313|EMBL:AAW90082.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90082.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90082.1; -; Genomic_DNA. DR RefSeq; WP_010951265.1; NC_002946.2. DR RefSeq; YP_208494.1; NC_002946.2. DR ProteinModelPortal; Q5F6V5; -. DR EnsemblBacteria; AAW90082; AAW90082; NGO_1440. DR GeneID; 3281712; -. DR KEGG; ngo:NGO1440; -. DR PATRIC; 20336299; VBINeiGon24812_1698. DR HOGENOM; HOG000216993; -. DR KO; K13888; -. DR OMA; EINVDSA; -. DR OrthoDB; EOG6DNT5K; -. DR BioCyc; NGON242231:GI2G-1347-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 43 265 HlyD_D23. {ECO:0000259|Pfam:PF16576}. FT COILED 143 170 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 392 AA; 41726 MW; 69DA16E148702616 CRC64; MAKMMKWAAV AAVAAAAVWG GWSYLKPEPQ AAYITETVRR GDISRTVSAT GEISPSNLVS VGAQASGQIK KLYVKLGQQV KKGDLIAEIN STTQTNTIDM EKSKLETYQA KLVSAQIALG SAEKKYKRQA ALWKDDATSK EDLESAQDAL AAAKANVAEL KALIRQSKIS INTAESDLGY TRITATMDGT VVAIPVEEGQ TVNAAQSTPT IVQLANLDMM LNKMQIAEGD ITKVKAGQDI SFTILSEPDT PIKAKLDSVD PGLTTMSSGG YNSSTDTASN AVYYYARSFV PNPDGKLATG MTTQNTVEID GVKNVLLIPS LTVKNRGGKA FVRVLGADGK AVEREIRTGM KDSMNTEVKS GLKEGDKVVI SEITAAEQQE SGERALGGPP RR // ID A0A0H4IVZ1_NEIG1 Unreviewed; 67 AA. AC A0A0H4IVZ1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63593.1}; GN ORFNames=NGO_00545 {ECO:0000313|EMBL:AKO63593.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63593.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63593.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63593; AKO63593; NGO_00545. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7780 MW; 9F08133394BCF4AC CRC64; MELKKANHGR ERSVGDIRDL LIVCLFRHQE YGKAELGRQK TTSRFYCLDA FYFKTMKTAC IDSNGCD // ID Q5F560_NEIG1 Unreviewed; 172 AA. AC Q5F560; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE RecName: Full=Gluconokinase {ECO:0000256|RuleBase:RU363066}; DE EC=2.7.1.12 {ECO:0000256|RuleBase:RU363066}; GN ORFNames=NGO_2076 {ECO:0000313|EMBL:AAW90677.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90677.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90677.1; -; Genomic_DNA. DR RefSeq; WP_003705071.1; NC_002946.2. DR RefSeq; YP_209089.1; NC_002946.2. DR ProteinModelPortal; Q5F560; -. DR EnsemblBacteria; AAW90677; AAW90677; NGO_2076. DR GeneID; 3282841; -. DR KEGG; ngo:NGO2076; -. DR PATRIC; 20337983; VBINeiGon24812_2514. DR HOGENOM; HOG000032567; -. DR KO; K00851; -. DR OMA; MGVCASG; -. DR OrthoDB; EOG6XHC8K; -. DR BioCyc; NGON242231:GI2G-1971-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Kinase {ECO:0000256|RuleBase:RU363066, ECO:0000313|EMBL:AAW90677.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363066}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU363066, KW ECO:0000313|EMBL:AAW90677.1}. SQ SEQUENCE 172 AA; 18869 MW; 304A0CD0A6C46707 CRC64; MTTHFVVTGV CGCGKTTAAP SLQKHLGQCP YAEGDEFHTQ ANRDKMGAGI PLTDEDRYPW LGNLRDWMTQ QAQNGADHTI VTCSALKRGY RDILRGAEGK AAFIHLSPPQ DINLERMMSR KGHYMKAGVL DSQLEILEEL GEGEYGVKIA NPGTPEAVEA DILNWVASEN LL // ID Q5F8K0_NEIG1 Unreviewed; 320 AA. AC Q5F8K0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 54. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89487.2}; GN ORFNames=NGO_0773 {ECO:0000313|EMBL:AAW89487.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89487.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89487.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89487; AAW89487; NGO_0773. DR HOGENOM; HOG000130878; -. DR OMA; CFGVLKT; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NGON242231:GI2G-727-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 152 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 320 AA; 36283 MW; D5ACB89B1F86C47D CRC64; MRNAVGLDIS KLTFDATAIV GNAEYSAKFD NDSKGLDQFS DRLKSLGCQN LHICMEATGN YYEEVADYFA QYYSVYVVNP LKISKYAESR FKRTKTDKQD AKLIAQYCRS AQESELVKRQ KPTDEQYRLS RMTAAYAQIK SECAAMKNRH HAAKDEEAAK AYAEIIKAMN EQLEVLKEKI KEQTEKPNCK EGVKRLETIP AIGRMTAAVL FHHLTSSKFE TSNKFAAFAG LSPQQKESGT SVRGKGKLTK FGNRKLRAVL FMPAMVAYRI RAFPDFIKRL EEKKKPKKVI IAALMRKLAV IAYHVHKKGG DYDPSRYKSA // ID Q5FA90_NEIG1 Unreviewed; 209 AA. AC Q5FA90; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 79. 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 ORFNames=NGO_0139 {ECO:0000313|EMBL:AAW88897.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88897.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88897.1; -; Genomic_DNA. DR RefSeq; WP_010951000.1; NC_002946.2. DR RefSeq; YP_207309.1; NC_002946.2. DR ProteinModelPortal; Q5FA90; -. DR SMR; Q5FA90; 1-208. DR EnsemblBacteria; AAW88897; AAW88897; NGO_0139. DR GeneID; 3281300; -. DR KEGG; ngo:NGO0139; -. DR PATRIC; 20333189; VBINeiGon24812_0177. DR HOGENOM; HOG000252206; -. DR KO; K10773; -. DR OMA; HHALILF; -. DR OrthoDB; EOG6H4KC5; -. DR BioCyc; NGON242231:GI2G-127-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW88897.1}; 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:AAW88897.1}; 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}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942, KW ECO:0000256|PIRNR:PIRNR001435}; KW Nuclease {ECO:0000313|EMBL:AAW88897.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 38 185 ENDO3c. {ECO:0000259|SMART:SM00478}. FT DOMAIN 99 127 HhH. {ECO:0000256|HAMAP-Rule:MF_00942}. 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; 23622 MW; 1B0B9DCD0A0ABA7B CRC64; MNRQIRQEIF ERFRAANPHP TTELNFNSPF ELLIAVLLSA QATDVGVNKA TAKLFPVADT PQAMLDLGLD GVMEYTKTIG LYKTKSKHIM QTCRIVLEKY NGQVPEDREA LESLPGVGRK TANVVLNTAF GHPVMAVDTH IFRVSNRTKI APGKDVREVE DKLMRFIPKE FLMDAHHWLI LHGRYTCKAL KPQCQTCIIN DLCEYPAKS // ID Q5F7X0_NEIG1 Unreviewed; 336 AA. AC Q5F7X0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140, ECO:0000256|SAAS:SAAS00009965}; DE EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140, ECO:0000256|SAAS:SAAS00009965}; DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140}; GN Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140}; GN ORFNames=NGO_1045 {ECO:0000313|EMBL:AAW89717.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89717.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + CC diphosphate + L-tryptophyl-tRNA(Trp). {ECO:0000256|HAMAP- CC Rule:MF_00140, ECO:0000256|SAAS:SAAS00009937}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_00140, CC ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00538757}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89717.1; -; Genomic_DNA. DR RefSeq; WP_003690986.1; NC_002946.2. DR RefSeq; YP_208129.1; NC_002946.2. DR ProteinModelPortal; Q5F7X0; -. DR EnsemblBacteria; AAW89717; AAW89717; NGO_1045. DR GeneID; 3282584; -. DR KEGG; ngo:NGO1045; -. DR PATRIC; 20335314; VBINeiGon24812_1223. DR HOGENOM; HOG000059939; -. DR KO; K01867; -. DR OMA; WYLSCFF; -. DR OrthoDB; EOG686NJQ; -. DR BioCyc; NGON242231:GI2G-962-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00140, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00420549}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00420551}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00140, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00420549}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00140, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00420551}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00140, KW ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00420554}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT MOTIF 12 20 "HIGH" region. {ECO:0000256|HAMAP- FT Rule:MF_00140}. FT MOTIF 203 207 "KMSKS" region. {ECO:0000256|HAMAP- FT Rule:MF_00140}. FT BINDING 206 206 ATP. {ECO:0000256|HAMAP-Rule:MF_00140}. SQ SEQUENCE 336 AA; 37579 MW; AA7C8CB83888EE90 CRC64; MSKKRVLTGV TTTGTPHLGN YVGAIRPAVR AAQNPDTESF LFLADYHGII KCHEQEMIHQ STQAVAATWL ACGLDPERTT FYRQSDIPEV MELNWILTCI TAKGLMNRAH AYKAAVQANA ENGQEDPDFG VEMGLFSYPI LMTADILMFN ANEVPVGRDQ IQHVEMARDI AGRFNHRFQE LFTLPEVKID ENVELLVGLD GRKMSKSYGN TIPLWENDKK TQKSVNKIIT NMKEPGEPKQ PDESPLFEIY KAFSTPSETA EFTQMLADGL AWGEAKKLSA AKINAELAEL RERYNALTSN PSQIEEILQA GAQKARKEAR ELLDKVRDAV GIRPLK // ID Q5F7W1_NEIG1 Unreviewed; 160 AA. AC Q5F7W1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Acyl-CoA thioester hydrolase {ECO:0000313|EMBL:AAW89726.1}; GN ORFNames=NGO_1055 {ECO:0000313|EMBL:AAW89726.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89726.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89726.1; -; Genomic_DNA. DR RefSeq; WP_003688183.1; NC_002946.2. DR RefSeq; YP_208138.1; NC_002946.2. DR ProteinModelPortal; Q5F7W1; -. DR EnsemblBacteria; AAW89726; AAW89726; NGO_1055. DR GeneID; 3281122; -. DR KEGG; ngo:NGO1055; -. DR PATRIC; 20335342; VBINeiGon24812_1237. DR HOGENOM; HOG000044842; -. DR OMA; SMDEMVF; -. DR OrthoDB; EOG65XN1H; -. DR BioCyc; NGON242231:GI2G-971-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89726.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 120 HotDog ACOT-type. FT {ECO:0000259|PROSITE:PS51770}. SQ SEQUENCE 160 AA; 17892 MW; 9EA969FF5D52841E CRC64; MTQQRQLPSH ELIMSELMMP DTANFSGNVH GGELLLLLDQ VAYSCASRYS GNYCVTLSVD KVLFKEPIHI GDLVTFYAAV NYTGRTSMEI GIRVEAQNIR TGEIRHTNSC YFTMVAVKDG KPVPVPPLEI LTDRQRCRYE KAKKRREISL QASGDVSCGC // ID Q5F7R8_NEIG1 Unreviewed; 172 AA. AC Q5F7R8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89769.1}; GN ORFNames=NGO_1102 {ECO:0000313|EMBL:AAW89769.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89769.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89769.1; -; Genomic_DNA. DR RefSeq; WP_010951187.1; NC_002946.2. DR RefSeq; YP_208181.1; NC_002946.2. DR ProteinModelPortal; Q5F7R8; -. DR EnsemblBacteria; AAW89769; AAW89769; NGO_1102. DR GeneID; 3282526; -. DR KEGG; ngo:NGO1102; -. DR HOGENOM; HOG000219507; -. DR OMA; KPAGHIF; -. DR OrthoDB; EOG6FRD2Z; -. DR BioCyc; NGON242231:GI2G-1014-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR InterPro; IPR016177; DNA-bd_dom. DR InterPro; IPR003615; HNH_nuc. DR Pfam; PF13392; HNH_3; 1. DR SUPFAM; SSF54171; SSF54171; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 69 111 HNHc. {ECO:0000259|Pfam:PF13392}. SQ SEQUENCE 172 AA; 20185 MW; B5FB5C8CB8222270 CRC64; MGLTQEVLKE LLRYDDNTGK LYWAERPRKY FNSGLHYKSW NTGFSGKEVF LYKGRLGYLK LKIFKKQYNA HRLIWLFVYG KHASSIGHIN RDKTDNRISN LRDVTHAENM KNRGKFKNNT SGHTGVYFHK PSKKWQARIM VNRKNKILGL FEHIEDAAKA REAASKDFGF VV // ID Q5F9E6_NEIG1 Unreviewed; 221 AA. AC Q5F9E6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Ferrous iron transporter B {ECO:0000313|EMBL:AAW89191.1}; GN ORFNames=NGO_0452 {ECO:0000313|EMBL:AAW89191.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89191.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89191.1; -; Genomic_DNA. DR RefSeq; WP_010951044.1; NC_002946.2. DR RefSeq; YP_207603.1; NC_002946.2. DR ProteinModelPortal; Q5F9E6; -. DR EnsemblBacteria; AAW89191; AAW89191; NGO_0452. DR GeneID; 3282992; -. DR KEGG; ngo:NGO0452; -. DR PATRIC; 20333936; VBINeiGon24812_0542. DR HOGENOM; HOG000218893; -. DR KO; K08084; -. DR OMA; AFNHIAF; -. DR OrthoDB; EOG6Z3KHV; -. DR BioCyc; NGON242231:GI2G-429-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 14 37 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 44 162 GspH. {ECO:0000259|Pfam:PF12019}. SQ SEQUENCE 221 AA; 24687 MW; 012246C5B9B1A894 CRC64; MCTRKQQGFT LTELLIVMAI AAIMATIALP NMSGWIASRR IASHAEQVAN LLRFSRGEAV RLNLPVYICP VQVKKDGASN NRCDFSKKGW GMLAFGDKNG NKEYDGDVAD VFLRSVVLND DINDKRIDYA FNHIAFGSSQ PTADRVVWTF NQNGTFGYTT DQHLTERSSF FYSDGYIQIV LTDARAVSDA DRKFRSAVVL IDSSGRVEVC RKNDTRAVCK H // ID Q5F5L0_NEIG1 Unreviewed; 482 AA. AC Q5F5L0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485}; DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485}; GN ORFNames=NGO_1914 {ECO:0000313|EMBL:AAW90527.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90527.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90527.1; -; Genomic_DNA. DR RefSeq; WP_003688061.1; NC_002946.2. DR RefSeq; YP_208939.1; NC_002946.2. DR ProteinModelPortal; Q5F5L0; -. DR SMR; Q5F5L0; 2-473. DR EnsemblBacteria; AAW90527; AAW90527; NGO_1914. DR GeneID; 3282280; -. DR KEGG; ngo:NGO1914; -. DR PATRIC; 20337562; VBINeiGon24812_2309. DR HOGENOM; HOG000255147; -. DR KO; K00033; -. DR OMA; EGEPCVT; -. DR OrthoDB; EOG6MSS4W; -. DR BioCyc; NGON242231:GI2G-1816-MONOMER; -. DR UniPathway; UPA00115; UER00410. DR Proteomes; UP000000535; 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:UP000000535}; KW Gluconate utilization {ECO:0000256|RuleBase:RU000486}; KW NADP {ECO:0000256|RuleBase:RU000485}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000485, KW ECO:0000313|EMBL:AAW90527.1}; KW Pentose shunt {ECO:0000256|RuleBase:RU000485}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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 REGION 128 130 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT REGION 186 187 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000109-2}. 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 102 102 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 191 191 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 260 260 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 287 287 Substrate. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 445 445 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. FT BINDING 451 451 Substrate; shared with dimeric partner. FT {ECO:0000256|PIRSR:PIRSR000109-2}. SQ SEQUENCE 482 AA; 52711 MW; 42BDD104E1E167F7 CRC64; MKGDIGVIGL AVMGQNLILN MNDCGFKVVA YNRTIGKVDE FLNGAAKETG IIGAYSLQDL VDKLAKPRKI MMMVRAGSVV DDFVEQLLPL LEEGDIIIDG GNANYPDTTR RTHYLAGKGI LFVGAGVSGG EEGARRGPSI MPGGDKRAWE AVKPIFQAIA AKTPQGEPCC DWVGKDGAGH FVKMVHNGIE YGDMQLICEA YQFMKDGLGL SYDEMHRVFA EWNKTELDSY LIEITAAILG YKDEGGEPLA EKILDTAGQK GTGKWTGINA LDLGIPLTLI SEAVFARCVS SFKEQRVQTG KLFARTATPV EGGKQEWVEA LRQALLASKI ISYAQGFMLI REAGESYGWG LDYGNTALLW REGCIIRSAF LGNIRDAYEA NPDLVFLGAD PYFKNILENC LPAWRKVVAK AVECGIPMPC MASAITFLDG YTTERLPANL LQAQRDYFGA HTYERTDKPR GEFFHTNWTG KGGDTASTTY DI // ID Q5F591_NEIG1 Unreviewed; 591 AA. AC Q5F591; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. 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 ORFNames=NGO_2038 {ECO:0000313|EMBL:AAW90646.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90646.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90646.1; -; Genomic_DNA. DR RefSeq; WP_003686967.1; NC_002946.2. DR RefSeq; YP_209058.1; NC_002946.2. DR ProteinModelPortal; Q5F591; -. DR EnsemblBacteria; AAW90646; AAW90646; NGO_2038. DR GeneID; 3282709; -. DR KEGG; ngo:NGO2038; -. DR PATRIC; 20337859; VBINeiGon24812_2453. DR HOGENOM; HOG000278513; -. DR KO; K08483; -. DR OMA; RSFSMHP; -. DR OrthoDB; EOG657JBQ; -. DR BioCyc; NGON242231:GI2G-1939-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW90646.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 64979 MW; E5F03345634A5B8D CRC64; MSIVLHGVAA GKGIAVGCAH LIARGTEEVP QYDVAQADTD AEAERFDAAV KATRKELEQL RSAIPENAPT ELGAFISLHL MLLTDVTLSR EPVDILREQK INAEWALKQQ SDKLAAQFDN MDDAYLRERK QDMLQVVRRI HNNLIGQGNE LEVADNLFDE TVLIANDLSP ADTVLFKEQR IAAFVTDAGG PTGHTAILGR SLDIPSVVGL HNARKLITEG ETVIVDGING VLIISPDESV LNEYRRRARE YRSHKRDLNK LKKTAAATAD GVCIELVGNI ESAEDVKPLH NLGADGIGLF RSEFLYLNRD TMPSEDEQYE VYSAIVKKMK GKSVTIRTVD LGVDKNPRWF GKNSTPNGSL NPALGMTGIR LCLAEPVMFR TQMRAILRAA VHGPVRMMWP MITSVSEVRQ CLIHLDTAQR QLAERGDAFG EVGIGCMIEI PSAALTVGSI LKLVDFISVG TNDLIQYILS VDRGDDSVSH LYQPGHPSVL KMLQHVIRTA NRMDKDVSVC GEMAGDTAFT RVLLGMGLRR FSMNPNNILP VKNIILHSNA GQLEGDIAKV IRCEDEEKSE KLIKQINSVS VAEEAEVKGR K // ID Q5F7N3_NEIG1 Unreviewed; 320 AA. AC Q5F7N3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89804.1}; GN ORFNames=NGO_1137 {ECO:0000313|EMBL:AAW89804.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89804.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89804.1; -; Genomic_DNA. DR RefSeq; WP_010951198.1; NC_002946.2. DR RefSeq; YP_208216.1; NC_002946.2. DR EnsemblBacteria; AAW89804; AAW89804; NGO_1137. DR GeneID; 3282236; -. DR KEGG; ngo:NGO1137; -. DR PATRIC; 20335532; VBINeiGon24812_1331. DR HOGENOM; HOG000130878; -. DR OMA; VILVMQK; -. DR OrthoDB; EOG647V4C; -. DR BioCyc; NGON242231:GI2G-1050-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 152 DEDD_Tnp_IS110. FT {ECO:0000259|Pfam:PF01548}. FT COILED 159 186 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 320 AA; 36337 MW; FB539F44E17CB471 CRC64; MRNAVGLDIS KLTFDASAMV GKTEHSAKFD NDSKGLDQFS DRLKSLGYQN LHICMEATGS YYEEVADYFA QYYSVYVVNP LKISKYAESR FKRTKTDKQD AKLIAQYCRS AKESELVKRQ KPTDEQYRLS RMTAAYAQIK SECAAMKNRH HAAKDEEAAK AYAQIIKAMN EQLEVLKEKI KEQTEKPNCK EGVKRLETIP AIGRMTAAVL FHHLTSSKFE TSNKFAAFAG LSPQQKESGT SVRGKGKLTK FGNRKLRAVL FMPAMVAYRI RAFPDFIKRL EEKKKPKKVI IAALMRKLAV IAYHVHKKGG DYDPSRYKSA // ID Q5F6L0_NEIG1 Unreviewed; 492 AA. AC Q5F6L0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|SAAS:SAAS00085409}; DE EC=6.3.2.- {ECO:0000256|SAAS:SAAS00276926}; GN ORFNames=NGO_1541 {ECO:0000313|EMBL:AAW90177.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90177.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00085391}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004135, CC ECO:0000256|SAAS:SAAS00085486}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000256|SAAS:SAAS00569976}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90177.1; -; Genomic_DNA. DR RefSeq; WP_003705692.1; NC_002946.2. DR RefSeq; YP_208589.1; NC_002946.2. DR ProteinModelPortal; Q5F6L0; -. DR EnsemblBacteria; AAW90177; AAW90177; NGO_1541. DR GeneID; 3281489; -. DR KEGG; ngo:NGO1541; -. DR PATRIC; 20336580; VBINeiGon24812_1838. DR HOGENOM; HOG000268118; -. DR KO; K01928; -. DR OMA; MAFYDYP; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NGON242231:GI2G-1443-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP 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: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 {ECO:0000256|SAAS:SAAS00459289}; KW Cell cycle {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459379}; KW Cell division {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459379}; KW Cell shape {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459442}; KW Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459257}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00459408}; KW Ligase {ECO:0000256|SAAS:SAAS00459363, ECO:0000313|EMBL:AAW90177.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00459289}; KW Peptidoglycan synthesis {ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00459442}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 28 96 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 112 315 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 337 423 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. SQ SEQUENCE 492 AA; 53010 MW; 9ED0CF2865C86A20 CRC64; MFSKLSPLAE TGIPTLSCAN AAGRLLHSDS RQIKQGDIFV ACPGEYADGR SYIPAAVANG AAFVFWDDDG RFAWNPEWKV PNQGIKDLKH RAGILAAQVY GNVSDGLKVW GVTGTNGKTS ITQWLAQAAD LLGEKTAIIG TVGNGFWGAL EETAHTTPAP VDVQTLLYRF RQQGATAAAM EVSSHGLDQS RVNGVPFRSA IFTNLTRDHL DYHGTMEAYG AIKSRLFYWH GLKHAVINTD DGYGAELAGR LKKDCPDLAV YSYGFSEHAD IRITDFTASS DGMEAVFQTP WGEGKCRTRL LGRFNAQNLA ACIALLCANG YPLDKVLDVL AKIRPASGRM DCIMNSGKPL VVVDYAHTPD ALEKALSTLQ EIKPQGAALW CVFGCGGNRD CGKRPLMGAA AVQGADKVVV TSDNPRLENP HDIINDILPA VPAPECVEAD RAAAIRYAVE QAAANDIILI AGKGHENYQD VQGVKHRFSD LEIVGQALLT RK // ID Q5FA55_NEIG1 Unreviewed; 225 AA. AC Q5FA55; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Chemotaxis protein CheY {ECO:0000313|EMBL:AAW88932.1}; GN ORFNames=NGO_0177 {ECO:0000313|EMBL:AAW88932.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88932.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88932.1; -; Genomic_DNA. DR RefSeq; WP_002214312.1; NC_002946.2. DR RefSeq; YP_207344.1; NC_002946.2. DR ProteinModelPortal; Q5FA55; -. DR EnsemblBacteria; AAW88932; AAW88932; NGO_0177. DR GeneID; 3281311; -. DR KEGG; ngo:NGO0177; -. DR PATRIC; 20333281; VBINeiGon24812_0223. DR HOGENOM; HOG000034819; -. DR KO; K02483; -. DR OMA; HAINIET; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NGON242231:GI2G-162-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00582919}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 A0A0H4J5I0_NEIG1 Unreviewed; 82 AA. AC A0A0H4J5I0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Integrase {ECO:0000313|EMBL:AKO63652.1}; GN ORFNames=NGO_03885 {ECO:0000313|EMBL:AKO63652.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63652.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63652.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63652; AKO63652; NGO_03885. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 9381 MW; F69ABC9A24918990 CRC64; MHGFRDLFTN ISLTAGKDTL TTDLALGHIS RAALQRAGFS SLHHYLTADS YRLQERRELA EWYGRRHRQA YEAAAQNTCN KT // ID A0A0H4IVG5_NEIG1 Unreviewed; 128 AA. AC A0A0H4IVG5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63735.1}; GN ORFNames=NGO_07995 {ECO:0000313|EMBL:AKO63735.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63735.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63735.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63735; AKO63735; NGO_07995. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 128 AA; 13649 MW; F44C9B0185009C70 CRC64; MAEGQKSAVT EYYLNHGTWP ENNTSAGVAS SATDIKGKYV QSVTVANGVV TAEMKSDGVN KEIQGKRLSL WARREAGSVK WFCGQPVTRA KAKDADDVTD DAGTDNGGKG KIDTKHLPST CRDKSTAK // ID Q5F789_NEIG1 Unreviewed; 154 AA. AC Q5F789; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89948.1}; GN ORFNames=NGO_1294 {ECO:0000313|EMBL:AAW89948.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89948.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89948.1; -; Genomic_DNA. DR RefSeq; WP_003702910.1; NC_002946.2. DR RefSeq; YP_208360.1; NC_002946.2. DR ProteinModelPortal; Q5F789; -. DR SMR; Q5F789; 4-153. DR EnsemblBacteria; AAW89948; AAW89948; NGO_1294. DR GeneID; 3282118; -. DR KEGG; ngo:NGO1294; -. DR PATRIC; 20335933; VBINeiGon24812_1521. DR HOGENOM; HOG000115327; -. DR KO; K03719; -. DR OMA; LVFVEIK; -. DR OrthoDB; EOG6F29D2; -. DR BioCyc; NGON242231:GI2G-1206-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000704}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 17777 MW; B0367022AD14690E CRC64; MKELDKIDFR ILKILQQNAR IPMTELAEKV GLSSTPVTER VCRLEREHYI SGYHVHLNPH LLGKPPLVFV ELKLQSKSGN IFEDFKKEVL KIPQIMECHL VSGEYDYLIK VRLPDMSAYR DMLGNILLQL PAASESRSYV VMEEVKENPV LDLD // ID Q5F5I1_NEIG1 Unreviewed; 195 AA. AC Q5F5I1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=RNA polymerase sigma factor {ECO:0000256|RuleBase:RU000716}; GN ORFNames=NGO_1944 {ECO:0000313|EMBL:AAW90556.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90556.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90556.1; -; Genomic_DNA. DR RefSeq; WP_003688115.1; NC_002946.2. DR RefSeq; YP_208968.1; NC_002946.2. DR ProteinModelPortal; Q5F5I1; -. DR DNASU; 3282676; -. DR EnsemblBacteria; AAW90556; AAW90556; NGO_1944. DR GeneID; 3282676; -. DR KEGG; ngo:NGO1944; -. DR PATRIC; 20337633; VBINeiGon24812_2343. DR HOGENOM; HOG000220918; -. DR KO; K03088; -. DR OMA; PEEMMEQ; -. DR OrthoDB; EOG6F299N; -. DR BioCyc; NGON242231:GI2G-1846-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000716, KW ECO:0000256|SAAS:SAAS00457605}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 22566 MW; CCB513C511709725 CRC64; MPLPDLTDAE LMESRKLLLH FARLQLPDHP DLAEDLVQET LLSAYSAGDS FQGRALVNSW LFAILKNKII DALRQIGRQR KVFTALDDEL LDEAFESHFS QNGHWTPEGQ PQHWNTPEKS LNNNEFQKIL QSCLYNLPEN TARVFTLKEI LGFSSNEIQQ MCGISTSNYH TIMHRARESL RQCLQIKWFN QENPK // ID Q5F8D2_NEIG1 Unreviewed; 1014 AA. AC Q5F8D2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AAW89555.1}; GN ORFNames=NGO_0851 {ECO:0000313|EMBL:AAW89555.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89555.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. CC {ECO:0000256|SAAS:SAAS00545451}. CC -!- SIMILARITY: Contains FtsK domain. {ECO:0000256|SAAS:SAAS00514329}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89555.1; -; Genomic_DNA. DR RefSeq; WP_003695161.1; NC_002946.2. DR RefSeq; YP_207967.1; NC_002946.2. DR ProteinModelPortal; Q5F8D2; -. DR SMR; Q5F8D2; 533-932, 946-1010. DR EnsemblBacteria; AAW89555; AAW89555; NGO_0851. DR GeneID; 3282193; -. DR KEGG; ngo:NGO0851; -. DR PATRIC; 20334872; VBINeiGon24812_1006. DR HOGENOM; HOG000220743; -. DR KO; K03466; -. DR OMA; WIVMIVI; -. DR OrthoDB; EOG6S52GD; -. DR BioCyc; NGON242231:GI2G-797-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; 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 {ECO:0000256|SAAS:SAAS00514327}; KW Cell cycle {ECO:0000313|EMBL:AAW89555.1}; KW Cell division {ECO:0000313|EMBL:AAW89555.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00429514}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00514327}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 662 871 FtsK. {ECO:0000259|PROSITE:PS50901}. SQ SEQUENCE 1014 AA; 110840 MW; AA5BFBF755D5CEBB CRC64; MFWIVLIVIL LLALAGLFFV RAQSEREWMR EVSAWQEKKG EKQAELPEIK DGMPDFPEFS LMLFHAVKTA VYWLFVGVVR FCRNYLAHES EPDRPVPPAS ANRADVPTAS DGYSDSGNGT EEAETEAAEA AEEEAADTED IATAVIDNRR IPFDRSIAEG LMQSESKTSP VRPVFKEITL EEATRALSSA ALRETKKRYI DAFEKNGTAV PKVRVSDTPM EGLQIIGLDD PVLQRTYSRM FDADKEAFSE SADYGFEPYF EKQHPSAFSA VKAENARNAP FRRHAGQEKG QAEAKSPDVS QGQSVSDGTA VRDARRRVSV NLKEPNKATV SAEARISRLI PESRTVVGKR DVEMPSETEN VFTETVSSVG YGGPVYDEAA DIHIEEPAAP DAWVVEPPEV PEVAVPEIDI LPPPPVSEIY NRTYEPPAGF EQAQRSRIAE TDHLAADVLN GGWQEETAAI ADDGSEGAAE RSSGQYLSET EAFGHDSQAV CPFEDVPSER PSCRVSDTEA DEGAFQSEET GAVSEHLPTT DLLLPPLFNP EATQTEEELL ENSITIEEKL AEFKVKVKVV DSYSGPVITR YEIEPDVGVR GNSVLNLEKD LARSLGVASI RVVETIPGKT CMGLELPNPK RQMIRLSEIF NSPEFAESKS KLTLALGQDI TGQPVVTDLG KAPHLLVAGT TGSGKSVGVN AMILSMLFKA APEDVRMIMI DPKMLELSIY EGITHLLAPV VTDMKLAANA LNWCVNEMEK RYRLMSFMGV RNLAGFNQKI AEAAARGEKI GNPFSLTPDD PEPLEKLPFI VVVVDEFADL MMTAGKKIEE LIARLAQKAR AAGIHLILAT QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE NLLGQGDMLF LPPGTAYPQR VHGAFASDEE VHRVVEYLKQ FGEPDYVDDI LSGGGSEELP GIGRSGDGET DPMYDEAVSV VLKTRKASIS GVQRALRIGY NRAARLIDQM EAEGIVSAPE HNGNRTILVP LDNA // ID Q5F714_NEIG1 Unreviewed; 582 AA. AC Q5F714; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW90023.1}; GN ORFNames=NGO_1375 {ECO:0000313|EMBL:AAW90023.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90023.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90023.1; -; Genomic_DNA. DR RefSeq; WP_010951253.1; NC_002946.2. DR RefSeq; YP_208435.1; NC_002946.2. DR ProteinModelPortal; Q5F714; -. DR DNASU; 3281495; -. DR EnsemblBacteria; AAW90023; AAW90023; NGO_1375. DR GeneID; 3281495; -. DR KEGG; ngo:NGO1375; -. DR PATRIC; 20336139; VBINeiGon24812_1618. DR HOGENOM; HOG000255783; -. DR OMA; PYDRYLF; -. DR OrthoDB; EOG6V4G82; -. DR BioCyc; NGON242231:GI2G-1288-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 262 377 Peptidase_M61. FT {ECO:0000259|Pfam:PF05299}. SQ SEQUENCE 582 AA; 66154 MW; F471E5020C33901E CRC64; MIHYKIAPSP LDHEWHILLK FTQDNDFPIE ISLPNWVPGS YLIRDFSRHI TSIHASCNGT SMPLEQIAKN RWHTAAVRGE WQIRYTVYAF DLSVRGSFLT TERGFFDGSC LFLKVEGTET LPHRLELTGI PPEWRIATTL PETGRLVFQT ASYDELIDRP VEMGLIEFLD FEAAGIPHTI ALNGIYPDFD RDRLVSDIKK ICETELAMFS SPAPFEKYLF LLHVGDHIYG GLEHTDSTAL LADRHSLPPY GMTDADDAYT TLLGLFSHEY FHAWNVKSIK PAAFAPYDLD KENYTEQLWA FEGITSYYDD LFLARSRTIS PEFYLNLLAQ GITRVQQTRG RLRQTLAESS FTAWNKFYKP DENSPNAIVS YYQKGALAAL CLDLIIRNRS NGRHSLDTVM DKLYREWRDT HSGIPEKHWQ IRCQEITGLD LTDFFQTALY STEDLPLAEC LATTGVKLTF LPLPRQHGGG YAEHIFPIPP TGDFGARFKQ NADHIVLTHV FNGGSAESAA LCPQDKIIAL DGYACTDFAA QWARYHVRAK INIHFFRAGI LRQTVLTVQA TAADTAILHI TDRNLLENWL FG // ID Q5FAB6_NEIG1 Unreviewed; 437 AA. AC Q5FAB6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=Citrate transporter {ECO:0000313|EMBL:AAW88871.1}; GN ORFNames=NGO_0110 {ECO:0000313|EMBL:AAW88871.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88871.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88871.1; -; Genomic_DNA. DR RefSeq; WP_003687374.1; NC_002946.2. DR RefSeq; YP_207283.1; NC_002946.2. DR EnsemblBacteria; AAW88871; AAW88871; NGO_0110. DR GeneID; 3282426; -. DR KEGG; ngo:NGO0110; -. DR PATRIC; 20333121; VBINeiGon24812_0144. DR HOGENOM; HOG000241948; -. DR KO; K03300; -. DR OMA; MVDAMAQ; -. DR OrthoDB; EOG65TRSJ; -. DR BioCyc; NGON242231:GI2G-100-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 46705 MW; FC5F49CD06C75D80 CRC64; MLTFIGLLII GVIVWLLLTE KVSPIIALIL VPLIGALLAG FDVSQLKEFY SGGTKSVTQI VIMFMFSILF FGIMNDVGLF RPMIGGLIKL TRGNIVAVSV GTVLVSVVAQ LDGAGATTFL SVVPALLPLY KRLHMNPYLL FLLLTSSAGL INLLPRGGPI GRVASVLGAD VGELYKPLLT VQIIGVVFIL VLSLFLGVRE KRRIVRELGA LPAVADLIKP APLSEEEQKL ARPKLFWWNV LLFLAAMSLL FSGIFPPGYV FMLAATAALL LNYRSPQEQM ERIYAHAGGA VMMASIILAA GTFLGILKGA GMLDAISKDL VHILPDALLP YLHIAIGVLG IPLELVLSTD AYYFGLFPIV EQITSQAGVA PEAAGYAMLI GSIVGTFVTP LSPALWMGLG LAKLSMGKHI RYSFFWAWGL SLAILVSSIA AGIVPLP // ID Q5F763_NEIG1 Unreviewed; 213 AA. AC Q5F763; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=GDSL family lipase {ECO:0000313|EMBL:AAW89974.1}; GN ORFNames=NGO_1323 {ECO:0000313|EMBL:AAW89974.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89974.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89974.1; -; Genomic_DNA. DR RefSeq; WP_003691652.1; NC_002946.2. DR RefSeq; YP_208386.1; NC_002946.2. DR ProteinModelPortal; Q5F763; -. DR EnsemblBacteria; AAW89974; AAW89974; NGO_1323. DR GeneID; 3281844; -. DR KEGG; ngo:NGO1323; -. DR PATRIC; 20336011; VBINeiGon24812_1556. DR HOGENOM; HOG000261382; -. DR OMA; KPMNRRI; -. DR OrthoDB; EOG6PGK4B; -. DR BioCyc; NGON242231:GI2G-1237-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 43 198 SGNH_hydro. {ECO:0000259|Pfam:PF13472}. SQ SEQUENCE 213 AA; 22963 MW; 7473036E0A8D22D5 CRC64; MPSEKPMNRR TFLLGAGALL LTACGRKSAR THAKIPEGST VLALGDSLTF GYGANPGESY PAQLQKLTGW NIVNGGVSGD TSAQALSRLP ALLARKPKLV IVGIGGNDFL RKVPEEQTRA NIAKIIETVQ KENIPAVLVG VPHITLGALF GHLSDHPLYE DLSEEYGIPL FGGAWAEILG NNNLKSDQIH ANGKGYRKFA ENLNQFLRKH GFR // ID A0A0H4IT71_NEIG1 Unreviewed; 106 AA. AC A0A0H4IT71; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transporter {ECO:0000313|EMBL:AKO63769.1}; GN ORFNames=NGO_09370 {ECO:0000313|EMBL:AKO63769.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63769.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63769.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63769; AKO63769; NGO_09370. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 15 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 99 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 106 AA; 11428 MW; CBE871FFB0ED92C1 CRC64; MVLIYIFSPK TDLNFYIFAA ALGFTWLATV APTAAVTGKL FGTRYLATLF GLVMLTHQIG GFLGSYIGGI VITQFGDYGW MWYADAVLAG TAALLVLPVR EPRTAA // ID A0A0H4ITA0_NEIG1 Unreviewed; 82 AA. AC A0A0H4ITA0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Histidinol phosphate phosphatase {ECO:0000313|EMBL:AKO63799.1}; GN ORFNames=NGO_10775 {ECO:0000313|EMBL:AKO63799.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63799.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63799.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63799; AKO63799; NGO_10775. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 8710 MW; 4BCC6E7EC211ACF5 CRC64; MAFGGILKKA AKMPSEGFRR HRGPKRANRH SPASRLCREE QGNRPENLAA RPDTATNETP GLPGAQAAAQ ALSTAIEGSF VV // ID Q5F674_NEIG1 Unreviewed; 489 AA. AC Q5F674; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 64. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90313.1}; GN ORFNames=NGO_1688 {ECO:0000313|EMBL:AAW90313.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90313.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90313.1; -; Genomic_DNA. DR RefSeq; WP_010951324.1; NC_002946.2. DR RefSeq; YP_208725.1; NC_002946.2. DR ProteinModelPortal; Q5F674; -. DR TCDB; 9.B.24.1.2; the duf805 or pf05656 (duf805) family. DR EnsemblBacteria; AAW90313; AAW90313; NGO_1688. DR GeneID; 3281210; -. DR KEGG; ngo:NGO1688; -. DR PATRIC; 20336934; VBINeiGon24812_2011. DR HOGENOM; HOG000219118; -. DR KO; K07280; -. DR OMA; FMPARNR; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NGON242231:GI2G-1583-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 489 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255482. FT DOMAIN 119 186 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 489 AA; 56499 MW; BA161FBFA2C66E12 CRC64; MVIFYFYFCG KTFMPARNRW MLLPLLASAA YAEETPCEPD LRSRPEFRLH EAEVKPIDRE KVPGQVREKG KVLQVDGETL LKNPELLSRA MYSAVVSNNI AGIRVILPIY LQQARQDKML ALYAQGILAQ AEGRVKEAVS HYRELIAAQP DAPAVRMRLA AALFEDRQNE AAADQFDRLK TEDLPPQLME QVELYRKALR ERDAWKVNGG FSVTREHNIN QAPKQQQYGN WTFPKQVDGT AVNYRFGAEK KWSLKNGWYT TAGGDVSGRV YPGNKKFNDM TAGVSGGIGF ADRRKDVGLA VFHERRTYGN DAYSYANGAR LYFNRWQTPR WQTLSSAEWG RLKNTRRARS DNTHLQISNS LVFYRNARQY WTGGLDFYRE RNPADRGDNF NRYGLRFAWG QEWGGSGLSS LFRLGVAKRH YEKPGFFSSF KGERRRDKES DTSLSLWHRA LHFKGITPRL TLSHRETWSN DVFNEYEKNR AFVEFNKTF // ID Q5F5Y1_NEIG1 Unreviewed; 475 AA. AC Q5F5Y1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE SubName: Full=Sodium:alanine symporter {ECO:0000313|EMBL:AAW90406.1}; GN ORFNames=NGO_1787 {ECO:0000313|EMBL:AAW90406.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90406.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90406.1; -; Genomic_DNA. DR RefSeq; WP_003690336.1; NC_002946.2. DR RefSeq; YP_208818.1; NC_002946.2. DR EnsemblBacteria; AAW90406; AAW90406; NGO_1787. DR GeneID; 3282464; -. DR KEGG; ngo:NGO1787; -. DR PATRIC; 20337218; VBINeiGon24812_2145. DR HOGENOM; HOG000255107; -. DR KO; K03310; -. DR OMA; AQLFKVK; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NGON242231:GI2G-1685-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 51741 MW; C9B6729B9875F62E CRC64; MNENFTEWLH GWVGAINDPM WSYLVYMLLG TGLFFTVTTG FVQFRLFGRS IKEMLGGRKQ GDDPHGITPF QAFVTGLASR VGVGNIAGVA IAIKVGGPGA VFWMWVTALI GMSSAFVESS LAQLFKVRDC DNHHFRGGPA YYITHGLGQK 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 A0A0H4J5D6_NEIG1 Unreviewed; 68 AA. AC A0A0H4J5D6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Dioxygenase {ECO:0000313|EMBL:AKO63617.1}; GN ORFNames=NGO_02015 {ECO:0000313|EMBL:AKO63617.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63617.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63617.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63617; AKO63617; NGO_02015. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Dioxygenase {ECO:0000313|EMBL:AKO63617.1}; KW Oxidoreductase {ECO:0000313|EMBL:AKO63617.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 68 AA; 7743 MW; 00AB0A7A704D0264 CRC64; MTELKQLIQT ESIPVIEETL DFLLYECSID DAPSAEEVAQ WRDILAARGG KFLRLSKICQ TWLDEEAA // ID Q5F842_NEIG1 Unreviewed; 405 AA. AC Q5F842; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448}; DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448}; GN ORFNames=NGO_0956 {ECO:0000313|EMBL:AAW89645.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89645.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89645.1; -; Genomic_DNA. DR RefSeq; WP_003688344.1; NC_002946.2. DR RefSeq; YP_208057.1; NC_002946.2. DR ProteinModelPortal; Q5F842; -. DR SMR; Q5F842; 246-404. DR EnsemblBacteria; AAW89645; AAW89645; NGO_0956. DR GeneID; 3282184; -. DR KEGG; ngo:NGO0956; -. DR PATRIC; 20335097; VBINeiGon24812_1118. DR HOGENOM; HOG000293093; -. DR KO; K00928; -. DR OMA; INIMMIS; -. DR OrthoDB; EOG6NSGHC; -. DR BioCyc; NGON242231:GI2G-887-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AAW89645.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003448, KW ECO:0000313|EMBL:AAW89645.1}. FT DOMAIN 266 340 ACT. {ECO:0000259|PROSITE:PS51671}. FT DOMAIN 346 405 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 405 AA; 43398 MW; 0C1743D30FFC2872 CRC64; MALIVHKYGG TSVGSPERIK NVAKRVAKAR AEGHDIVVVV SAMSGETNRL VALAHEMQEH PDPRELDVVL ATGEQVTIGL LAMALKDIGV DAKSYTGWQV SLKTDTAHTK ARIESIDDEK MRADLAAGKV VIVAGFQGIS SEGNISTLGR GGSDTSAVAL AAALKADECQ IYTDVDGVYT TDPRVVPEAR RMDTVTFEEM IELASLGSKV LQIRSVEFAG KYKVRLRVLS SLQDGGNGTL ITFEEDDNME RAAVTGIAFD KNQARINVRG VPDKPGVAYQ ILGAVADANI EVDMIIQNVG SEGTTDFSFT VPRGDYKQTL EILSERKDSI GAASIDGDDT VCKVSAVGLG MRSHVGVAAK IFRTLAEEGI NIQMISTSEI KVSVLIDEKY MELATRVLHK AFDLG // ID A0A0H4IW75_NEIG1 Unreviewed; 46 AA. AC A0A0H4IW75; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63683.1}; GN ORFNames=NGO_05530 {ECO:0000313|EMBL:AKO63683.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63683.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63683.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63683; AKO63683; NGO_05530. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 46 AA; 5405 MW; 405AA5F086D23F6A CRC64; MAFCHCPDKL LNCLNYFDRR YTHMKDPEQS SKPARRFLCV LSVQAA // ID Q5F5W8_NEIG1 Unreviewed; 792 AA. AC Q5F5W8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=Outer membrane protein assembly factor BamA {ECO:0000256|HAMAP-Rule:MF_01430}; DE Flags: Precursor; GN Name=bamA {ECO:0000256|HAMAP-Rule:MF_01430}; GN ORFNames=NGO_1801 {ECO:0000313|EMBL:AAW90419.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90419.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:4K3B} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS). RX PubMed=23995689; DOI=10.1038/nature12521; RA Noinaj N., Kuszak A.J., Gumbart J.C., Lukacik P., Chang H., RA Easley N.C., Lithgow T., Buchanan S.K.; RT "Structural insight into the biogenesis of beta-barrel membrane RT proteins."; RL Nature 501:385-390(2013). 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:0000256|HAMAP- CC Rule:MF_01430}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000256|HAMAP- CC Rule:MF_01430}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP- CC Rule:MF_01430, ECO:0000256|SAAS:SAAS00560981}. CC -!- SIMILARITY: Belongs to the BamA family. {ECO:0000256|HAMAP- CC Rule:MF_01430, ECO:0000256|SAAS:SAAS00539226}. CC -!- SIMILARITY: Contains 5 POTRA domains. {ECO:0000256|HAMAP- CC Rule:MF_01430}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90419.1; -; Genomic_DNA. DR RefSeq; WP_010951351.1; NC_002946.2. DR RefSeq; YP_208831.1; NC_002946.2. DR PDB; 4K3B; X-ray; 3.20 A; A=1-792. DR PDBsum; 4K3B; -. DR ProteinModelPortal; Q5F5W8; -. DR EnsemblBacteria; AAW90419; AAW90419; NGO_1801. DR GeneID; 3282404; -. DR KEGG; ngo:NGO1801; -. DR PATRIC; 20337252; VBINeiGon24812_2161. DR HOGENOM; HOG000261767; -. DR KO; K07277; -. DR OMA; NLDRGYF; -. DR OrthoDB; EOG6F81K6; -. DR BioCyc; NGON242231:GI2G-1699-MONOMER; -. DR Proteomes; UP000000535; 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4K3B}; KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_01430, KW ECO:0000256|SAAS:SAAS00560982}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01430, KW ECO:0000256|SAAS:SAAS00560982, ECO:0000256|SAAS:SAAS00560990}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01430, KW ECO:0000256|SAAS:SAAS00447731}; KW Signal {ECO:0000256|HAMAP-Rule:MF_01430}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01430, KW ECO:0000256|SAAS:SAAS00560990}; KW Transmembrane beta strand {ECO:0000256|HAMAP-Rule:MF_01430, KW ECO:0000256|SAAS:SAAS00560990}. FT SIGNAL 1 21 {ECO:0000256|HAMAP-Rule:MF_01430}. FT CHAIN 22 792 Outer membrane protein assembly factor FT BamA. {ECO:0000256|HAMAP-Rule:MF_01430}. FT /FTId=PRO_5005078796. FT DOMAIN 24 78 POTRA 1. {ECO:0000256|HAMAP- FT Rule:MF_01430}. FT DOMAIN 91 171 POTRA 2. {ECO:0000256|HAMAP- FT Rule:MF_01430}. FT DOMAIN 175 262 POTRA 3. {ECO:0000256|HAMAP- FT Rule:MF_01430}. FT DOMAIN 267 344 POTRA 4. {ECO:0000256|HAMAP- FT Rule:MF_01430}. FT DOMAIN 347 421 POTRA 5. {ECO:0000256|HAMAP- FT Rule:MF_01430}. FT DOMAIN 448 792 Bac_surface_Ag. FT {ECO:0000259|Pfam:PF01103}. SQ SEQUENCE 792 AA; 87942 MW; 8EB06CA369C15812 CRC64; MKLKQIASAL MMLGISPLAF ADFTIQDIRV EGLQRTEPST VFNYLPVKVG DTYNDTHGSA IIKSLYATGF FDDVRVETAD GQLLLTVIER PTIGSLNITG AKMLQNDAIK KNLESFGLAQ SQYFNQATLN QAVAGLKEEY LGRGKLNIQI TPKVTKLARN RVDIDITIDE GKSAKITDIE FEGNQVYSDR KLMRQMSLTE GGIWTWLTRS DRFDRQKFAQ DMEKVTDFYQ NNGYFDFRIL DTDIQTNEDK TRQTIKITVH EGGRFRWGKV SIEGDTNEVP KAELEKLLTM KPGKWYERQQ MTAVLGEIQN RMGSAGYAYS EISVQPLPNA GTKTVDFVLH IEPGRKIYVN EIHITGNNKT RDEVVRRELR QMESAPYDTS KLQRSKERVE LLGYFDNVQF DAVPLAGTPD KVDLNMSLTE RSTGSLDLSA GWVQDTGLVM SAGVSQDNLF GTGKSAALRA SRSKTTLNGS LSFTDPYFTA DGVSLGYDIY GKAFDPRKAS TSVKQYKTTT AGGGVRMGIP VTEYDRVNFG LAAEHLTVNT YNKAPKRYAD FIRKYGKTDG ADGSFKGLLY KGTVGWGRNK TDSASWPTRG YLTGVNAEIA LPGSKLQYYS ATHNQTWFFP LSKTFTLMLG GEVGIAGGYG RTKEIPFFEN FYGGGLGSVR GYESGTLGPK VYDEYGEKIS YGGNKKANVS AELLFPMPGA KDARTVRLSL FADAGSVWDG RTYTAAENGN NKSVYSENAH KSTFTNELRY SAGGAVTWLS PLGPMKFSYA YPLKKKPEDE IQRFQFQLGT TF // ID A0A0H4J5Z6_NEIG1 Unreviewed; 291 AA. AC A0A0H4J5Z6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63792.1}; GN ORFNames=NGO_10555 {ECO:0000313|EMBL:AKO63792.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63792.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63792.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63792; AKO63792; NGO_10555. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 291 AA; 31676 MW; 53ABDBC143B4E80F CRC64; MGINANPNCA DEAGKLIWEN DPDKNWWANR MDDIRGIIQG AVNPFLTGFQ GVGIGAITDS AVSPVTDTAA QQTLQGINDL GKLSPEAQLA VASLLQDSAF AVKDGINSAR QWADAHPNIT ATAQTALAVA EAAGTVWRGK KVELNPTKWD WVKNTGYEKP AARPMQTVDG EMAGGNKPIK SLPNSAAEKR KQSFKKFSSN WSSASFDSVH KTLTPNAPGI LSPDKVKTRY TSLDGKITII KDNENNYFRI HDNSRKQYLD SNGNAVKTGN LQGKQAKDYL QQQTHIRNLD K // ID Q5F5Q4_NEIG1 Unreviewed; 768 AA. AC Q5F5Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 93. 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 ORFNames=NGO_1863 {ECO:0000313|EMBL:AAW90483.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90483.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90483.1; -; Genomic_DNA. DR RefSeq; WP_003705339.1; NC_002946.2. DR RefSeq; YP_208895.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q4; -. DR EnsemblBacteria; AAW90483; AAW90483; NGO_1863. DR GeneID; 3282381; -. DR KEGG; ngo:NGO1863; -. DR PATRIC; 20337420; VBINeiGon24812_2241. DR HOGENOM; HOG000004018; -. DR KO; K03168; -. DR OMA; RIKYNEI; -. DR OrthoDB; EOG6S7XQ9; -. DR BioCyc; NGON242231:GI2G-1767-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 87048 MW; 1CF0875E9C4F1FF6 CRC64; MAKNLLIVES PSKAKTLKKY LGGDFEILAS YGHVRDLVPK SGAVDPDNGF AMKYQLISRN GKHVDAIVAA 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 DEESEDSKKL PEMSEGDKLP VDKLYGEQHF TTPPPRYNEA TLVKALEEYG IGRPSTYASI ISTLKDREYV TLEQKRFMPT DTGDIVNKFL TEHFAQYVDY HFTAKLEDQL DEIADGKRRW IPVMDKFWKP FIKQVEEKEG IERAKFTTQE LDETCPKCGE HKLQIKFGKM GRFVACAGYP ECSYTRNVNE TAEEAAERIA KAEAEQVELD GRECPKCGGR LVYKYSRTGS KFIGCANYPK CKHVEPLEKP KDTGVQCPQC KKGNLVERKS RYGKLFYSCS TYPDCNYATW NPPVAEECPN CHWPVLAIKT TKRRGVEKVC PQKECGWKEQ IEPPAPQE // ID A0A0H4J5F4_NEIG1 Unreviewed; 43 AA. AC A0A0H4J5F4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Universal stress protein UspA {ECO:0000313|EMBL:AKO63632.1}; GN ORFNames=NGO_03090 {ECO:0000313|EMBL:AKO63632.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63632.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63632.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63632; AKO63632; NGO_03090. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 43 AA; 4963 MW; 8E0429BC9A2D051E CRC64; MPSETLPIIR MWFQTAFVLF SVYSAKIGTV VFYLPEVFAE MVC // ID Q5F5C9_NEIG1 Unreviewed; 168 AA. AC Q5F5C9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=ADP-heptose synthase {ECO:0000313|EMBL:AAW90608.1}; GN ORFNames=NGO_2000 {ECO:0000313|EMBL:AAW90608.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90608.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90608.1; -; Genomic_DNA. DR RefSeq; WP_003686901.1; NC_002946.2. DR RefSeq; YP_209020.1; NC_002946.2. DR ProteinModelPortal; Q5F5C9; -. DR EnsemblBacteria; AAW90608; AAW90608; NGO_2000. DR GeneID; 3282624; -. DR KEGG; ngo:NGO2000; -. DR PATRIC; 20337777; VBINeiGon24812_2412. DR HOGENOM; HOG000284154; -. DR OMA; RGHATYL; -. DR OrthoDB; EOG68Q0W4; -. DR BioCyc; NGON242231:GI2G-1901-MONOMER; -. DR UniPathway; UPA00356; UER00439. DR Proteomes; UP000000535; 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:UP000000535}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00444127}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00444162}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00444162}. FT DOMAIN 34 128 CTP_transf_like. FT {ECO:0000259|Pfam:PF01467}. SQ SEQUENCE 168 AA; 17809 MW; 1185890F9F46B082 CRC64; MVDAWSVPDF ESKICPPEAL AARLALLPRP LVFTNGCFDI LHRGHVTYLA QARSAGAALV LALNTDASVR RLGKGGDRPV NPLENRAAVA AALESVDLVT WFDEDTPAAL IEAVKPEVLV KGGDWVVDKI VGAAETLARG GQVFSIPFLH QTSTTKTLAK IRAAEGGK // ID A0A0H4IW37_NEIG1 Unreviewed; 56 AA. AC A0A0H4IW37; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63643.1}; GN ORFNames=NGO_03735 {ECO:0000313|EMBL:AKO63643.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63643.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63643.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63643; AKO63643; NGO_03735. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 51 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 56 AA; 6494 MW; 46E2E30EAC699588 CRC64; MNTNLNDKDK AMDTAIRFQK RMRIPKFFFL ILGITVVLAF IQDVITGSNF LQITIM // ID A0A0H4IV26_NEIG1 Unreviewed; 77 AA. AC A0A0H4IV26; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Hemagglutinin {ECO:0000313|EMBL:AKO63640.1}; GN ORFNames=NGO_03715 {ECO:0000313|EMBL:AKO63640.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63640.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63640.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63640; AKO63640; NGO_03715. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006914; VENN_dom. DR Pfam; PF04829; PT-VENN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 25 59 PT-VENN. {ECO:0000259|Pfam:PF04829}. SQ SEQUENCE 77 AA; 7709 MW; 2E61AAB351E00396 CRC64; MGAGGSEAAA PIIGKWLYGK GDGGSLNAEE KETVSAITRM LGTAAGAAEG NSSADAVWGC FQTASDFASS FSYPINM // ID A0A0H4IV31_NEIG1 Unreviewed; 294 AA. AC A0A0H4IV31; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63645.1}; GN ORFNames=NGO_03825 {ECO:0000313|EMBL:AKO63645.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63645.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63645.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63645; AKO63645; NGO_03825. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 294 AA; 32048 MW; BE1F52A48B41D5FF CRC64; MAVGTKQEDE IKRHVHKVFS HWANHPDAAA VGYEDRNERQ RSALVSTWTD GDLNDNGFLT PRLDSKMATG GAENRPKALV LKLCIKAADT LGEAVFRIKS HGETANAGAL DASRLAQGLQ EKADRDHTHT TAQIQGLDEK ISAAVAAQFT RQTIGGVDIV RFPDGTMIQT GSYRFARGGS PIGNEVVFPI AFADGNVKCF VSERHSGRVN GERQHNWLFI RAKNHAAAII TNWYESSCDW MAIGKSASGN AASPTPIVPE IPEIDEEPQR ESGRSSTGLR NPRRHRGLDF PVGS // ID Q5F608_NEIG1 Unreviewed; 896 AA. AC Q5F608; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000256|SAAS:SAAS00015000}; DE EC=2.7.7.42 {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000256|SAAS:SAAS00015004}; DE AltName: Full=Glutamine-synthase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802}; DE AltName: Full=[Glutamate--ammonia-ligase] adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802}; GN Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802}; GN ORFNames=NGO_1758 {ECO:0000313|EMBL:AAW90379.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90379.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Adenylation and deadenylation of glutamate--ammonia CC ligase. {ECO:0000256|HAMAP-Rule:MF_00802, CC ECO:0000256|SAAS:SAAS00015010}. 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:0000256|HAMAP- CC Rule:MF_00802, ECO:0000256|SAAS:SAAS00202364}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00802}; CC -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP- CC Rule:MF_00802, ECO:0000256|SAAS:SAAS00540787}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90379.1; -; Genomic_DNA. DR RefSeq; WP_010951341.1; NC_002946.2. DR RefSeq; YP_208791.1; NC_002946.2. DR ProteinModelPortal; Q5F608; -. DR EnsemblBacteria; AAW90379; AAW90379; NGO_1758. DR GeneID; 3281418; -. DR KEGG; ngo:NGO1758; -. DR PATRIC; 20337128; VBINeiGon24812_2104. DR HOGENOM; HOG000256491; -. DR KO; K00982; -. DR OMA; EFMVQYA; -. DR OrthoDB; EOG651SRZ; -. DR BioCyc; NGON242231:GI2G-1654-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423277}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423276}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423277}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423290, ECO:0000313|EMBL:AAW90379.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423259}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00802, KW ECO:0000256|SAAS:SAAS00423290, ECO:0000313|EMBL:AAW90379.1}. FT DOMAIN 50 240 GlnE. {ECO:0000259|Pfam:PF03710}. FT DOMAIN 268 406 GlnD_UR_UTase. FT {ECO:0000259|Pfam:PF08335}. FT DOMAIN 520 754 GlnE. {ECO:0000259|Pfam:PF03710}. FT DOMAIN 786 869 GlnD_UR_UTase. FT {ECO:0000259|Pfam:PF08335}. FT REGION 66 273 GlnE 1. {ECO:0000256|HAMAP- FT Rule:MF_00802}. FT REGION 575 779 GlnE 2. {ECO:0000256|HAMAP- FT Rule:MF_00802}. FT COILED 51 74 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 896 AA; 101730 MW; 5902BD89A1D45A46 CRC64; MSDHRLDTAR RHSLFLARQL DNGKLKPEIF LPMLDKALTD EGFQAFADWD KIRAEESEEE LARQLRELRR YVVSQIIVRD INRISDLNEV TRTITLFADF AVNTALDFAY AYYRDMYGTP IGRYTKSPQH LSVVAMGKAG GYELNVSSDI DLIFVYPESG DTDGRRERGN QEFFTKVGQK LIALLNGITA DGQVFRVDMR LRPDGDSGAL VLSETVLEQY LITQGREWER YAWCKGRVVT PYPNDIKSLV RPFVFRKYLD YGAYEAMRNL HRQIRSEVSK KGMADNIKLG AGGIREVEFI AQIFQMIRGG QMRALQLKGT QETLKKIAEM GIMPSENVET LLAAYRFLRD VEHRLQYWDD RQTQTLPISP EQRQLLAESM GFDSYAAFSD GLNVHRNKVN QLFNEILSEP EEQAQSNSEW QWAWQEKPDE EERLGRLKEH GFDAEAVTAR LEQICHGHKY RRLSAHAQPR FDTIVPLFVQ AAAEQNNPTD TLMRLLDFLE NISLRSAYLA FLNEHPQTLA QLAQIMSQSS WVAAYLNKYP ILLDELISAQ LLDTAFDWQA LAAALSDGIE ACGGDTEAQM DTLRHFQHAQ VFRLAVQDLA GLWTVESLSD QLSALADTVI AAALSCAWAD MPKKHRDTPQ FAVIGYGKLG GKELGYASDL DLVYLYDDPH PEAGDVYSRL ARRLTNRLSA ATGAGSLYET DLRLRPNGDA GFLAHSIAAF GKYQRENAWT WEHQSLTRAR FICGTPEIQT AFDRIRTEML TAERDQTALA GEIIEMREKM FPTHPPADSN VKYARGGVVD VEFIVQYLIL AHARQYPQLL DNYGNIALLN IAADCGLIDK TLAGQSRTAY RLYRRQQHNT KLRDAAKTEV SDELLSHYGN VRKLWREVFG EEAATA // ID Q5F8G7_NEIG1 Unreviewed; 360 AA. AC Q5F8G7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 73. DE SubName: Full=Sulfate adenylate transferase {ECO:0000313|EMBL:AAW89520.1}; GN ORFNames=NGO_0806 {ECO:0000313|EMBL:AAW89520.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89520.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. {ECO:0000256|SAAS:SAAS00313285}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. CC {ECO:0000256|SAAS:SAAS00313287}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89520.1; -; Genomic_DNA. DR RefSeq; WP_003706267.1; NC_002946.2. DR RefSeq; YP_207932.1; NC_002946.2. DR ProteinModelPortal; Q5F8G7; -. DR EnsemblBacteria; AAW89520; AAW89520; NGO_0806. DR GeneID; 3281987; -. DR KEGG; ngo:NGO0806; -. DR PATRIC; 20334766; VBINeiGon24812_0953. DR HOGENOM; HOG000071286; -. DR OMA; PEATLCW; -. DR OrthoDB; EOG6GR38Q; -. DR BioCyc; NGON242231:GI2G-762-MONOMER; -. DR UniPathway; UPA00262; UER00222. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR028281; Sirohaem_synthase_central. DR InterPro; IPR006367; Sirohaem_synthase_N. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR Pfam; PF13241; NAD_binding_7; 1. DR Pfam; PF14824; Sirohm_synth_M; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01470; cysG_Nterm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW NAD {ECO:0000256|SAAS:SAAS00416861}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00416910}; KW Porphyrin biosynthesis {ECO:0000256|SAAS:SAAS00567488}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89520.1}. FT DOMAIN 6 115 NAD_binding_7. FT {ECO:0000259|Pfam:PF13241}. FT DOMAIN 119 145 Sirohm_synth_M. FT {ECO:0000259|Pfam:PF14824}. SQ SEQUENCE 360 AA; 38995 MW; 3F58A09E49E8DCB1 CRC64; MNYFPIFANL AGRPVLVVGG GAVAARKISL LLKAGAEVGV AAKHLNAELS ALAAENKILW LAKEFRAEHI RTVFLIIAAS SDQALNRRVF HLAESCQKPV NVVGDRDHCS FIFPSVIDRD PVQIAVSSSG SAPVLARLLR ERLEALLPPS LGDMAEISGR WRDAGFYFPV QLVVRQDADK ADGFRGYQGR IERGSVTVGQ TVRIEPNGLT AEVSEIIAPK GEVAQAFAGE AATIRLDRDI DVSRGDLFVD KNFPLAPQKH PEATLCWFDE RPLNTARKYL LKHGTQTVSA KVGEIESVLD VRTLEQEAGA ESLKMNDIAK VRINLQKPVT ATPYAENTAA GSFILIDEAT YGTVAAGMIL // ID A0A0H4ISA2_NEIG1 Unreviewed; 68 AA. AC A0A0H4ISA2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63796.1}; GN ORFNames=NGO_10580 {ECO:0000313|EMBL:AKO63796.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63796.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63796.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63796; AKO63796; NGO_10580. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 68 AA; 7735 MW; D490F0DB2A34EBD0 CRC64; MNILSINNQN STISLTQDEV FVLRAILNEI YAGVCVDSRE FENVSGVRKH EVDNLQQQFA GIYKKMTT // ID A0A0H4IRR3_NEIG1 Unreviewed; 190 AA. AC A0A0H4IRR3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Hemin transporter {ECO:0000313|EMBL:AKO63641.1}; GN ORFNames=NGO_03720 {ECO:0000313|EMBL:AKO63641.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63641.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63641.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63641; AKO63641; NGO_03720. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR013686; Polypept-transport_assoc_ShlB. DR Pfam; PF08479; POTRA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 35 114 POTRA_2. {ECO:0000259|Pfam:PF08479}. SQ SEQUENCE 190 AA; 20944 MW; F60E727C87995E86 CRC64; MQPEQDVRLD GTDTGIEKMA TQVGGANSDE ASPCFPISEV ELVGEEAAKF RFALNHALCQ THFVSGKCLH AGDINQIMSL AQNALIGRGY TTTRILAAPQ DLNSGKLQLT LMPGYLRSIR IDRSNDDQTH AGRIAAFQNK FPTRSNDLLN LRDLEQGLEN LKCLPTAEAD LQIVPVEREP NQSDVVVQWR // ID A0A0H4IW66_NEIG1 Unreviewed; 56 AA. AC A0A0H4IW66; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63673.1}; GN ORFNames=NGO_04995 {ECO:0000313|EMBL:AKO63673.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63673.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63673.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63673; AKO63673; NGO_04995. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 56 AA; 6393 MW; BE7DAC23697606E7 CRC64; MPALCAYRFN AFPKLINNLK KAGKPKMVII VAIMRKLAKP AYYIVKTGQP YDAERH // ID Q5F755_NEIG1 Unreviewed; 141 AA. AC Q5F755; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Osmoprotectant transport activator ProQ {ECO:0000313|EMBL:AAW89982.1}; GN ORFNames=NGO_1332 {ECO:0000313|EMBL:AAW89982.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89982.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89982.1; -; Genomic_DNA. DR RefSeq; WP_002238237.1; NC_002946.2. DR RefSeq; YP_208394.1; NC_002946.2. DR ProteinModelPortal; Q5F755; -. DR SMR; Q5F755; 1-116. DR EnsemblBacteria; AAW89982; AAW89982; NGO_1332. DR GeneID; 3282043; -. DR KEGG; ngo:NGO1332; -. DR PATRIC; 20336033; VBINeiGon24812_1566. DR HOGENOM; HOG000219072; -. DR OMA; TASTKYL; -. DR OrthoDB; EOG6RJV9P; -. DR BioCyc; NGON242231:GI2G-1246-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 141 AA; 15500 MW; B2B114D768A4EC63 CRC64; MTQETALGAA LKSAVQTMSK KKQTEMIADH IYGKYDVFKR FKPLALGIDQ DLIAALPQYD SALIARVLAN HCRRPRYLKA LARGGKRFDL NNRFKGEVTP EEQAIAQNHP FVQQALQQQS AQAAAETPSV EAEAAESSAA E // ID Q5F862_NEIG1 Unreviewed; 292 AA. AC Q5F862; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862}; DE EC=1.5.1.20 {ECO:0000256|RuleBase:RU003862}; GN ORFNames=NGO_0929 {ECO:0000313|EMBL:AAW89625.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89625.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10- CC methylenetetrahydrofolate + NAD(P)H. CC {ECO:0000256|RuleBase:RU003862}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU003862}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|RuleBase:RU003862}. CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase CC family. {ECO:0000256|RuleBase:RU003862}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89625.1; -; Genomic_DNA. DR RefSeq; WP_010951150.1; NC_002946.2. DR RefSeq; YP_208037.1; NC_002946.2. DR ProteinModelPortal; Q5F862; -. DR SMR; Q5F862; 3-292. DR EnsemblBacteria; AAW89625; AAW89625; NGO_0929. DR GeneID; 3282606; -. DR KEGG; ngo:NGO0929; -. DR PATRIC; 20335041; VBINeiGon24812_1090. DR HOGENOM; HOG000246232; -. DR KO; K00297; -. DR OMA; EMHPQAR; -. DR OrthoDB; EOG6D2KVW; -. DR BioCyc; NGON242231:GI2G-867-MONOMER; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000535; 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:InterPro. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004255}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW FAD {ECO:0000256|RuleBase:RU003862}; KW Flavoprotein {ECO:0000256|RuleBase:RU003862}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003862}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 292 AA; 33098 MW; DE8F126A3584FB9D CRC64; MNYAKEINAL NNSLSDLKGN INVSFEFFPP KNEQMETMLW DSIHRLQTLH PKFVSVTYGA NSGERDRTHG IVKRIKQETG LEAASHLTGI DASHDELRQI AKDYWDSGIR RIVALRGDEP AGYEKKPFYA EDLVKLLRSV ADFDISVAAY PEVHPEAKSA QADLINLKRK IDAGANHVIT QFFFDVERYL RFRDRCVMLG IDVEIVPGIL PVTNFKQLGK MAQVTNVKIP KWLSQMYEGL DDDQGTRNLV AASIAIDMVK VLSREGVKDF HFYTLNRSEL TYAICHILGA RP // ID A0A0H4ISX9_NEIG1 Unreviewed; 59 AA. AC A0A0H4ISX9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63704.1}; GN ORFNames=NGO_06740 {ECO:0000313|EMBL:AKO63704.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63704.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63704.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63704; AKO63704; NGO_06740. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6661 MW; 7281F6A31F92C694 CRC64; MIKPNLRPKL GSSALIAFLS LYSSLVLNYA FFAKVVELRP FNDTGADIFL YTMPVVLFF // ID A0A0H4ISV1_NEIG1 Unreviewed; 178 AA. AC A0A0H4ISV1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Autotransporter {ECO:0000313|EMBL:AKO63684.1}; GN ORFNames=NGO_05610 {ECO:0000313|EMBL:AKO63684.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63684.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63684.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63684; AKO63684; NGO_05610. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR Gene3D; 3.40.50.200; -; 1. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR SUPFAM; SSF52743; SSF52743; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 178 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206195. SQ SEQUENCE 178 AA; 18661 MW; BC0760716DC98559 CRC64; MRTTSTFPTK TFKPAAMALA VATTLSACLG GGGGGTSAPD FNAGGTGIGS NSRATIAESA AVSYAGIKNE MCKDRSMLCA GRDDVAVTDR DAKIKAPRIC IPETFQTQMT NIKNMINLKP AIEAGYTGRG VEVGIVDTGE SVGSISFPEL YGRKEHGYNE NYKNKLQKLY GVYAEGSA // ID A0A0H4IT76_NEIG1 Unreviewed; 171 AA. AC A0A0H4IT76; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Type II restriction enzyme NgoPII {ECO:0000313|EMBL:AKO63774.1}; GN ORFNames=NGO_09570 {ECO:0000313|EMBL:AKO63774.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63774.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63774.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63774; AKO63774; NGO_09570. DR Proteomes; UP000000535; 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 InterPro; IPR019046; Restrct_endonuc_II_NgoPII. DR Pfam; PF09521; RE_NgoPII; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 171 AA; 19769 MW; 62DACCEAC414F67F CRC64; MTACLQKPAK MRKNGKRKTL SIIVGVVDKK KNLKHLAMVY GIDYCADAEC YLKIKNQIKE GIGNIGGIQF AETKELGRVN RIDPLNITYL RVRGMWGIEN PWFVFNYIYQ RNMEKSFNFM AIINEDKWNS FNNTDKLLAI QDSKLAISDI KIKNPNNPAR LRNAKLITYH L // ID Q5F6W9_NEIG1 Unreviewed; 503 AA. AC Q5F6W9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Probable protein kinase UbiB {ECO:0000256|HAMAP-Rule:MF_00414, ECO:0000256|SAAS:SAAS00063507}; DE EC=2.7.-.- {ECO:0000256|HAMAP-Rule:MF_00414, ECO:0000256|SAAS:SAAS00063486}; DE AltName: Full=Ubiquinone biosynthesis protein UbiB {ECO:0000256|HAMAP-Rule:MF_00414}; GN Name=ubiB {ECO:0000256|HAMAP-Rule:MF_00414}; GN ORFNames=NGO_1424 {ECO:0000313|EMBL:AAW90068.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90068.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is probably a protein kinase regulator of UbiI activity CC which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00414, ECO:0000256|SAAS:SAAS00063478}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis CC [regulation]. {ECO:0000256|HAMAP-Rule:MF_00414, CC ECO:0000256|SAAS:SAAS00063476}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00414}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00414}. CC -!- SIMILARITY: Belongs to the ABC1 family. UbiB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00414, ECO:0000256|SAAS:SAAS00561173}. CC -!- SIMILARITY: Contains 1 protein kinase domain. {ECO:0000256|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; AE004969; AAW90068.1; -; Genomic_DNA. DR RefSeq; WP_003703693.1; NC_002946.2. DR RefSeq; YP_208480.1; NC_002946.2. DR ProteinModelPortal; Q5F6W9; -. DR EnsemblBacteria; AAW90068; AAW90068; NGO_1424. DR GeneID; 3281752; -. DR KEGG; ngo:NGO1424; -. DR PATRIC; 20336263; VBINeiGon24812_1680. DR HOGENOM; HOG000264440; -. DR KO; K03688; -. DR OMA; AKTEKFH; -. DR OrthoDB; EOG61P6SS; -. DR BioCyc; NGON242231:GI2G-1333-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; 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; IPR000719; Prot_kinase_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. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448093}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448107}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448107}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448097}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448107, ECO:0000256|SAAS:SAAS00448109}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448093}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448097}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448109}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448109}; KW Ubiquinone {ECO:0000313|EMBL:AAW90068.1}; KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00414, KW ECO:0000256|SAAS:SAAS00448072}. FT TRANSMEM 13 35 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00414}. FT TRANSMEM 485 502 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00414}. FT DOMAIN 120 489 Protein kinase. {ECO:0000256|HAMAP- FT Rule:MF_00414, FT ECO:0000259|PROSITE:PS50011}. FT NP_BIND 126 134 ATP. {ECO:0000256|HAMAP-Rule:MF_00414}. FT ACT_SITE 283 283 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_00414}. FT BINDING 148 148 ATP. {ECO:0000256|HAMAP-Rule:MF_00414}. SQ SEQUENCE 503 AA; 57331 MW; 587203C30AB71361 CRC64; MKWLKRLTVI VGTFYRYRLA GLCVSLMGSG WICALLKMMP QSSKLKNEPP AVRLRLALES LGPIFIKFGQ VLSTRPDLIP HDYAVELAKL QDKVPPFDAR LSREQIEKSL GQPIEKLYAE FETEPVASAS IAQVHKARLH SGERVAVKVL RPNLLPLIEQ DLSLMRFGAA WVERLFSDGK RLKPREVVAE FDKYLHDELD LMREAANAGQ LGRNFQNSNM LIVPKVFYDY CTSDVLTIEW MDGTPVSDIA KLKADGIDLH KLADYGVEIF FTQVFRDGFF HADMHPGNIL VAADNRYIAL DFGIVGTLTD YDKRYLAINF LAFFNRDYRR VATAHIESGW VPADTRAEEL EAAVRAVCEP VFNKPISQIS FGLVLMRLFE VSRRFNVEIQ PQLVLLQKTL LNIEGLGRQL DPDLDLWKTA KPFLVKWMNG QVGPKALWRN LKNEAPDWAQ IIPSLPRKIN ALVDEARRQE MRDAYIHLVK VQQRQSLWLA AIAVVLLLIL LLK // ID A0A0H4IRX3_NEIG1 Unreviewed; 250 AA. AC A0A0H4IRX3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000256|HAMAP-Rule:MF_01887}; DE EC=2.1.1.185 {ECO:0000256|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887}; DE AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887}; GN Name=rlmB {ECO:0000256|HAMAP-Rule:MF_01887}; GN ORFNames=NGO_04950 {ECO:0000313|EMBL:AKO63671.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63671.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in CC 23S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01887}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|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; AE004969; AKO63671.1; -; Genomic_DNA. DR RefSeq; WP_003706327.1; NC_002946.2. DR RefSeq; YP_008914850.1; NC_002946.2. DR EnsemblBacteria; AKO63671; AKO63671; NGO_04950. DR GeneID; 19592995; -. DR KEGG; ngo:NGO0942a; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01887}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887, KW ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:AKO63671.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01887}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01887}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01887, KW ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:AKO63671.1}. FT DOMAIN 6 82 SpoU_sub_bind. FT {ECO:0000259|SMART:SM00967}. FT BINDING 197 197 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_01887}. FT BINDING 217 217 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01887}. FT BINDING 226 226 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000256|HAMAP- FT Rule:MF_01887}. SQ SEQUENCE 250 AA; 27410 MW; 1308B209100E2AD9 CRC64; MANQRPIYGF HAVNARLWQN PKSITELYIQ EGKSDARTRE VLEKAANENI RVYFADADRL NAISKGARHQ GVVGFIDASK NHVHLEDVLE NLSEPPLLLI LDGITDPHNL GACLRTADAM GVHAVIAPKD KSAGLNATVS KVACGAAETV PYITVTNLAR TLRELKEYGI WIIGTDMGGD ADLYHCNLPD STAWVMGNEG DGMRRLTREH CDMLVSIPMF GTVESMNVSV SAGMVLSETR RQRVLKNKKA // ID A0A0H4IT57_NEIG1 Unreviewed; 377 AA. AC A0A0H4IT57; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63754.1}; GN ORFNames=NGO_08475 {ECO:0000313|EMBL:AKO63754.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63754.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63754.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63754; AKO63754; NGO_08475. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 377 AA; 43085 MW; F64B7E2753FA319D CRC64; MFKKFKPVLL SFFALVFAFW LGTGIAYEIN PRWFLSDTAT EVPENPNAFV AKLARLFRNA DRAVVIVKES MRTEESLAGA VDDGPLQSEK DYLALAIRLS RLKEKAKWFH VTEQEHGEEV WLDYYIGEGG LVAVSLSQRS PEAFVNAEYL YRNDRPFSVN VYGGTAHGEN YETTGEYRVV WQPDGSVFDA AGRGKIGEDV YEHCLGCYQM AQVYLAKYRD VANDEQKVWD FREESNRIAS DSRDYVFYQN MRELMPRGMK ANSLVVGYDA DGLPQKVYWS FDNGKKRQSF EYYLKNGNLF IAQSSTVALK ADGVTADMQT YHAQQTWYLD GGRIIREEKQ GDRLPDFPLN LEDLEKEVSR YAEAAARRSG GRRGLSH // ID A0A0H4J5Q2_NEIG1 Unreviewed; 199 AA. AC A0A0H4J5Q2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=NosX protein {ECO:0000313|EMBL:AKO63712.1}; GN ORFNames=NGO_07160 {ECO:0000313|EMBL:AKO63712.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63712.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63712.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63712; AKO63712; NGO_07160. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0017013; P:protein flavinylation; IEA:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like. DR PANTHER; PTHR30040:SF2; PTHR30040:SF2; 1. DR Pfam; PF02424; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 199 AA; 21754 MW; EA4F61090C67E337 CRC64; MWKLYADYFA ARPDAETPPE NSVKETLKRV GFGKVSFDDR EIRFAEKGMG LSLNGIAQGY ITDKVVALLK ANGVPAALVD MGEIRGFDTN GRRMWNVGIR NPDDEEGVLA NITMKDKAFA TSGGYGTVMD KAGRLTHLFD PRTGVSTPRY KSMSVMADDA AVADALSTAF SVMDLPLIRS VAESRRLKVR LAMPDNIVD // ID Q5F748_NEIG1 Unreviewed; 330 AA. AC Q5F748; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Asparaginase {ECO:0000313|EMBL:AAW89989.1}; GN ORFNames=NGO_1339 {ECO:0000313|EMBL:AAW89989.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89989.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the asparaginase 1 family. CC {ECO:0000256|RuleBase:RU004456}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89989.1; -; Genomic_DNA. DR RefSeq; WP_003693790.1; NC_002946.2. DR RefSeq; YP_208401.1; NC_002946.2. DR ProteinModelPortal; Q5F748; -. DR EnsemblBacteria; AAW89989; AAW89989; NGO_1339. DR GeneID; 3281930; -. DR KEGG; ngo:NGO1339; -. DR PATRIC; 20336047; VBINeiGon24812_1573. DR HOGENOM; HOG000227974; -. DR KO; K01424; -. DR OMA; LECYGSG; -. DR OrthoDB; EOG683S61; -. DR BioCyc; NGON242231:GI2G-1253-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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; IPR027475; Asparaginase/glutaminase_AS2. 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; PS00917; ASN_GLN_ASE_2; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 178 Asparaginase. {ECO:0000259|Pfam:PF00710}. FT ACT_SITE 13 13 O-isoaspartyl threonine intermediate. FT {ECO:0000256|PIRSR:PIRSR001220-1}. SQ SEQUENCE 330 AA; 34892 MW; E5C5377AC98976D5 CRC64; MKQKIFVLYT GGTIGMTQSS AGLRPDTALV GQALAPFSDG MDFDWHVCEP LIDSSAVQLQ NWCAWLDIIA AALPQYDGVL VLHGTDTLAY TANMFALALQ GLDKPIVLTG SQWPYNAEGS DAPRNLVTAV AAFPLGLKQT LIAFDGKLYP AVGSSKISTE TAAGFGNAHF GALAEWDETR GWHNVRIPNQ DAADVSDGLE IRYPDPQAKI AVRTLIPGFA VQELADGLGQ LPAQALILQS YGHGNTSAGE GFIRAVQDFT QQGKLLLNIS QVPQGCAAAV YAQGDALRRA GVVNGGKCNL ETATALMTLA VSEGWGADGV KHELQRLGLV // ID A0A0H4IT33_NEIG1 Unreviewed; 290 AA. AC A0A0H4IT33; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63724.1}; GN ORFNames=NGO_07590 {ECO:0000313|EMBL:AKO63724.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63724.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63724.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63724; AKO63724; NGO_07590. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 77 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 164 183 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 249 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 274 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 290 AA; 32194 MW; 8AAC8F861BF37876 CRC64; MAVLLLVAAV LLPFLPQLAA FFVAAYWLVL LLFCAWLIWL DRNTDNFALL MLLAAFTVFQ TAYAVSGDLN LLRAQVHLNM AAVMFVSVRV SVLLGTETLK ECRLKDPVFI PNVIYKNIAI TLLLHAAAEL WLPAQTAGFT ALAVGFILLA KLRELHHHEL LRKHYVRTYY LLQLFAAAGY LWTGAAKLQN LPASAPLHLI TLGGMTGGVM MVWLTAGLWH SGFTKLDYPK LCRIAVSILF ASAVSRAVLM NVNPIFFITV PEILTAAVFM LYLLTFVPIF RANAFTDDPE // ID Q5F6Q4_NEIG1 Unreviewed; 912 AA. AC Q5F6Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE SubName: Full=Ligand-gated channel {ECO:0000313|EMBL:AAW90133.1}; GN ORFNames=NGO_1495 {ECO:0000313|EMBL:AAW90133.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90133.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90133.1; -; Genomic_DNA. DR RefSeq; WP_010951283.1; NC_002946.2. DR RefSeq; YP_208545.1; NC_002946.2. DR ProteinModelPortal; Q5F6Q4; -. DR EnsemblBacteria; AAW90133; AAW90133; NGO_1495. DR GeneID; 3281624; -. DR KEGG; ngo:NGO1495; -. DR PATRIC; 20336454; VBINeiGon24812_1774. DR HOGENOM; HOG000219090; -. DR KO; K16087; -. DR OMA; TFAYNRV; -. DR OrthoDB; EOG6HB9KP; -. DR BioCyc; NGON242231:GI2G-1399-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|SAAS:SAAS00444644}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00444644, KW ECO:0000256|SAAS:SAAS00447760}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357, KW ECO:0000256|SAAS:SAAS00444615}; KW Transmembrane {ECO:0000256|SAAS:SAAS00447760}; KW Transmembrane beta strand {ECO:0000256|SAAS:SAAS00447760}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 912 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255495. FT DOMAIN 62 169 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 622 911 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 912 AA; 101945 MW; D395EDD94F79D16A CRC64; MQQQHLFRFN ILCLSLMTAL PAYAENVQAG QAQEKQLDTI QVKAKKQKTR RDNEVTGLGK LVKTADTLSK EQVLDIRDLT RYDPGIAVVE QGRGASSGYS IRGMDKNRVA LTVDGLAQIQ SYTAQAALGG TRTAGSSGAI NEIEYENVKA VEISKGSNSV EQGSGALAGS VAFQTKTADD VIGEGRQWGI QSKTAYSGKN RGLTQSIALA GRIGGAEALL IRTGRHAGEI RAHEAAGRGV QSFNRLVPVD DASTYAYFIV EEECKNEGYE KCKAKKDVDG KDERQTVSTR DYTGPNRFLA DPLSYESRSW LFRPGFRFEN KRHYIGGILE RTQQTFDTRD MTVPAFLTKA VFDENKKYGS IRGYGKYAGG RKYSGLITNG ENGAEVGAEY GTGVFYDETH TKSRYGLEYV YTNADKDTWA DYARLSYDRQ GIGLDNHFQQ THCSADGSDK YCRPSADKPS SYYKSDRVIY GESHRLLQAA FKKSFDTAKI RHNLSVNLGY DRFGSDLRHQ DYYYQHANRA YSLKTPPQNN GKKINPNGSE KNPYWVSIGG GNVVTGQICL FGNNTYTDCT PRSINGKSYY AAVRDNVRLG RWADVGAGLR YDYRSTHSDD GSVSTGTHRT LSWNTGIVLK PADWLDLTYR TSTGFRLPSF AEMYGWRSGG KIKAVKIDPE KSFNKEAGIV FKGDFGNLEA SWFNNAYRDL IVRGYEAQIK DGKEQVKGDP AYLNAQSARI TGINILGKID WNGVWDKLPE GWYSTFAYNR VRVRDIKKRA DRTDIQSHLF DAIQPSRYVV GSGYDQPEGK WGVNGMLTYS KAKEITELLG SRALLNGNSR DTKATARRTR PWYIVDVSGY YTVKKHFTLR AGVYNLLNHR YVTWENVRQT AAGAVNQHKN VGVYNRYAAP GRNYTFSLEM KF // ID A0A0H4IT89_NEIG1 Unreviewed; 84 AA. AC A0A0H4IT89; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63789.1}; GN ORFNames=NGO_10430 {ECO:0000313|EMBL:AKO63789.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63789.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63789.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63789; AKO63789; NGO_10430. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 84 AA; 9752 MW; 36A3D07ACF4430A1 CRC64; MSGVLQAVIK IGSKTKDRKI GRIRVSLIIE IRSFRKNGLG GRGNAVCEMR QIWEIDAAFV FYVFIYSVWR NMLLLKSVLW MNCR // ID Q5F806_NEIG1 Unreviewed; 590 AA. AC Q5F806; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00051044}; DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00051045}; GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974}; GN ORFNames=NGO_0998 {ECO:0000313|EMBL:AAW89681.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89681.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA CC molecules used as primers for DNA polymerase during DNA CC replication. {ECO:0000256|HAMAP-Rule:MF_00974, CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00079980}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00974}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00974}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00974, CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP- CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, CC ECO:0000256|PIRSR:PIRSR002811-1}; CC -!- SUBUNIT: Monomer. {ECO:0000256|PIRSR:PIRSR002811-1}. CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00974}. CC -!- SIMILARITY: Belongs to the DnaG primase family. CC {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, CC ECO:0000256|SAAS:SAAS00534519}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|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; AE004969; AAW89681.1; -; Genomic_DNA. DR RefSeq; WP_003698307.1; NC_002946.2. DR RefSeq; YP_208093.1; NC_002946.2. DR ProteinModelPortal; Q5F806; -. DR EnsemblBacteria; AAW89681; AAW89681; NGO_0998. DR GeneID; 3282186; -. DR KEGG; ngo:NGO0998; -. DR PATRIC; 20335198; VBINeiGon24812_1167. DR HOGENOM; HOG000014483; -. DR KO; K02316; -. DR OMA; PARENTG; -. DR OrthoDB; EOG6XDGTR; -. DR BioCyc; NGON242231:GI2G-924-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00440993}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|SAAS:SAAS00514060}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00514084}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|SAAS:SAAS00415496}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00514058}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00514091}; KW Primosome {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00514054}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00514084}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00514091}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRSR:PIRSR002811- KW 1, ECO:0000256|SAAS:SAAS00514058}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974, KW ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00514058}. FT DOMAIN 255 337 Toprim. {ECO:0000256|HAMAP-Rule:MF_00974, FT ECO:0000259|PROSITE:PS50880}. FT ZN_FING 37 61 CHC2-type. {ECO:0000256|HAMAP- FT Rule:MF_00974, FT ECO:0000256|PIRSR:PIRSR002811-1}. FT METAL 261 261 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00974}. FT METAL 305 305 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00974}. FT METAL 305 305 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00974}. FT METAL 307 307 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00974}. SQ SEQUENCE 590 AA; 65801 MW; CB532ADCDFA22E77 CRC64; MIPSDFIDEL LAKTDIVGII DEQVPLKKGG ANYMACCPFH KEKTPSFSVS PTKQFYHCFS CGAHGSAIGF VMEHQGLSFP EAVQFLADRV GMIVPKVRGQ NDNPEVRAER KKKQQTLEET TAAAADFYAQ QLKFNPAAKA YLDKRGLSAE VIAHYGLGYA PDGWQPLAQV FQPYPNTALV DTGMVIDNEG RHYDRFRHRI MFPIRNPRGQ VIGFGGRVLD DSKPKYLNSP DTPLFDKGKN LYGLYEGRAA VKEAERILVV EGYMDVVALA QFGVGYGVAA LGTATTAEHV KILMRQADSI YFCFDGDSAG RKAAWRALEN ALPQLKDDKS LHFLFLPEEH DPDSYIRAYG KAQFEDALLN QSKPLSEYFW EHLSDGIHLN TQEGKAELVK TSSPLLVQIT APALAYLLKQ RLSELVGIDP DNLAQLLGQE APKRHVKQKN YKLPPISVKQ PVMPTLVQRQ IRSLLINPDW AAYIDLPDYL ALDGDFACLA NLAETIKNHP SVPATAQVLE HMRGSPYEET INRIFRSALQ SEEMEGGGEE DCENFQIGIK KLLNELKYSQ IETLKQKSLQ SGLNESEKKL LLSLLTAKQN // ID Q5F908_NEIG1 Unreviewed; 275 AA. AC Q5F908; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 63. DE RecName: Full=S-formylglutathione hydrolase {ECO:0000256|RuleBase:RU363068}; DE EC=3.1.2.12 {ECO:0000256|RuleBase:RU363068}; GN ORFNames=NGO_0600 {ECO:0000313|EMBL:AAW89329.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89329.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89329.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F908; -. DR ESTHER; neig1-q5f908; A85-EsteraseD-FGH. DR EnsemblBacteria; AAW89329; AAW89329; NGO_0600. DR PATRIC; 20334274; VBINeiGon24812_0709. DR HOGENOM; HOG000263929; -. DR OMA; TEQPWAT; -. DR OrthoDB; EOG63587Z; -. DR BioCyc; NGON242231:GI2G-569-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU363068}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Serine esterase {ECO:0000256|RuleBase:RU363068}. SQ SEQUENCE 275 AA; 31367 MW; 84339D87C546BE78 CRC64; MKLIEQHQIF GGSQQVWAHH AQTLQCEMKF AVYLPDNPEN QPLGVIYWLS GLTCTEQNFI TKSSFRRYAA EHQVVVVAPD TGPRGEQVPN GAAYDLGQGA GFYLNATEQP WAANYQMYDY ILNELPRLIE EHFPTNGKRS IMGHSMDGHG ALVLALRNRE HYQSVSAFSP ILSPSLVPWG EKAFTAYLGK DREKWQQYDA NSLIQQGYKV QGMRIDQGLE DEFLPTQLRT KDFIETCRAA NQPIDVRFHK GYDHSYYFIA SFIGEHIAYH AAFLK // ID A0A0H4IV92_NEIG1 Unreviewed; 109 AA. AC A0A0H4IV92; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Modification methylase {ECO:0000313|EMBL:AKO63695.1}; GN ORFNames=NGO_06150 {ECO:0000313|EMBL:AKO63695.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63695.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63695.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63695; AKO63695; NGO_06150. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AKO63695.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63695.1}. FT DOMAIN 43 104 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 109 AA; 12379 MW; AD7EBF048A575CAB CRC64; MAFAHIPELQ LECFIGKDNS FKDTFGRLWW DKPAPTITTK FFSISNGRFA HPEEDRALSL REGATLQSFP RNYVFKAGSR DKIARLIGNA VPPMYTEKIG RAIVDNIEC // ID Q5F6X9_NEIG1 Unreviewed; 410 AA. AC Q5F6X9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE Short=Na(+)-NQR subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE Short=Na(+)-translocating NQR subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE EC=1.6.5.8 {ECO:0000256|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR complex subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR-1 subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; GN Name=nqrB {ECO:0000256|HAMAP-Rule:MF_00426}; GN ORFNames=NGO_1414 {ECO:0000313|EMBL:AAW90058.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90058.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00426}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000256|HAMAP-Rule:MF_00426}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00426, CC ECO:0000256|PIRSR:PIRSR016055-50}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000256|HAMAP-Rule:MF_00426}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00426}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00426}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000256|HAMAP- CC Rule:MF_00426, ECO:0000256|SAAS:SAAS00571749}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90058.1; -; Genomic_DNA. DR RefSeq; WP_003689269.1; NC_002946.2. DR RefSeq; YP_208470.1; NC_002946.2. DR EnsemblBacteria; AAW90058; AAW90058; NGO_1414. DR GeneID; 3281781; -. DR KEGG; ngo:NGO1414; -. DR PATRIC; 20336235; VBINeiGon24812_1666. DR HOGENOM; HOG000273666; -. DR KO; K00347; -. DR OMA; TVFYTPG; -. DR OrthoDB; EOG65BDMX; -. DR BioCyc; NGON242231:GI2G-1323-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00426}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00426}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00426, KW ECO:0000256|PIRSR:PIRSR016055-50}; KW FMN {ECO:0000256|HAMAP-Rule:MF_00426, ECO:0000256|PIRSR:PIRSR016055- KW 50}; Ion transport {ECO:0000256|HAMAP-Rule:MF_00426}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00426, KW ECO:0000256|SAAS:SAAS00462498}; NAD {ECO:0000256|HAMAP-Rule:MF_00426}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00426}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00426, KW ECO:0000256|PIRSR:PIRSR016055-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sodium {ECO:0000256|HAMAP-Rule:MF_00426}; KW Sodium transport {ECO:0000256|HAMAP-Rule:MF_00426}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00426, KW ECO:0000256|SAAS:SAAS00462498}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00426, KW ECO:0000256|SAAS:SAAS00462498}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00426}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00426}. FT TRANSMEM 56 76 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 119 139 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 159 179 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 266 286 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 293 313 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 318 338 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 347 367 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT TRANSMEM 377 397 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00426}. FT MOD_RES 232 232 FMN phosphoryl threonine. FT {ECO:0000256|HAMAP-Rule:MF_00426, FT ECO:0000256|PIRSR:PIRSR016055-50}. SQ SEQUENCE 410 AA; 44490 MW; 3CF667833999BAB1 CRC64; MGLKHFLEKI EPHFLPGGKH EKWYALYEAA ATIFYTSGAV TRKAAHVRDA LDSKRMMILV WLALFPAMFY GMYNVGAQAF GALTPDLLQQ SIANDWHYAL ANALGINMSP EAGVLGKMLF GAIYFLPIYA TVFIVGGFWE VLFASVRKHE INEGFFVTSI LFALIVPPTL PLWQAALGIS FGVVVAKEVF GGTGKNFMNP ALAGRAFLFF AYPANLSGDA VWTAVDGYSG ATALAQWAAH GADGLKNAVT GQTITWMDAF IGKLPGSIGE VSTLALLIGG AFIVFARIAS WRIIAGVMIG MIAMSSLFNF IGSDTNAMFA MPWYWHLVVG GFAIGMLFMA TDPVSASFTN VGKWWYGALI GVMCVLIRVA NPAYPEGMML AILFANLFAP IFDYFVAQAN IKRRKARSNG // ID Q5F7B8_NEIG1 Unreviewed; 574 AA. AC Q5F7B8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:AAW89919.1}; GN ORFNames=NGO_1260 {ECO:0000313|EMBL:AAW89919.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89919.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89919.1; -; Genomic_DNA. DR RefSeq; WP_010951228.1; NC_002946.2. DR RefSeq; YP_208331.1; NC_002946.2. DR ProteinModelPortal; Q5F7B8; -. DR EnsemblBacteria; AAW89919; AAW89919; NGO_1260. DR GeneID; 3282591; -. DR KEGG; ngo:NGO1260; -. DR PATRIC; 20335851; VBINeiGon24812_1480. DR HOGENOM; HOG000071212; -. DR OMA; IVCATHK; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NGON242231:GI2G-1177-MONOMER; -. DR Proteomes; UP000000535; 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 GO; GO:0043565; F:sequence-specific DNA binding; 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; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002078; Sigma_54_int. DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2. DR Pfam; PF02954; HTH_8; 1. DR Pfam; PF00158; Sigma54_activat; 1. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1. DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00515313}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00515313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|SAAS:SAAS00516031}; KW Transcription regulation {ECO:0000256|SAAS:SAAS00516031}; 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 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 188 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 205 472 Sigma-54 factor interaction. FT {ECO:0000259|PROSITE:PS50045}. SQ SEQUENCE 574 AA; 65048 MW; 0532A8994397FFB6 CRC64; MVISNPRELE KLKDRIPNLI NIIRVAIVFP LMIMHILGLE TGSRANLHAS WTAWAFYLWL AIACWLIFFS TLNPQWQWQW QALRIPSFSA VADITMIGVL TYLFGGIDSG FGILILPFVG SSCLLSYGRY PLLYASYASI LLIFNALADS NINMYPLILD AKTVTNTFVV VAGSYFVAMI ASLSVRYIDR AGKLAHENHV AYRRIRGLNQ IVLNRVQEAV VVINVEHQTI LFNKKAKDLL PMLEIGQHTS LFDPVAILWD KTSSRTFEHH IDTPELTARI RAVPMNKKQN KLLILYIRPQ SEIQAEALSV KLAALGQLTA NLAHEIRNPM SAIRHADGGT LFLDEVADLP LSMQVKLLRA IQEKAVRRIG DATEQPVDVR IVCATHKNLE ALVESGAFRQ DLYYRLNVVS LNMPSLREMR ENLKLPTPYL LYKHSHNNRP YTLSPAAQQM LLNYSYPGNF RELENILERA VALCVGYTVQ IDDLQIQDVH HKPVRTETAV PVADTLPSEI AAAPSRLLPF DPDTMQIQDY LDKIERDIIG QVLKQTEGNR TQAAKRLGIS FRSMRYRMER LNID // ID Q5F6Y5_NEIG1 Unreviewed; 160 AA. AC Q5F6Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE SubName: Full=ArsR family transcriptional regulator {ECO:0000313|EMBL:AAW90052.1}; GN ORFNames=NGO_1407 {ECO:0000313|EMBL:AAW90052.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90052.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90052.1; -; Genomic_DNA. DR RefSeq; WP_002221359.1; NC_002946.2. DR RefSeq; YP_208464.1; NC_002946.2. DR ProteinModelPortal; Q5F6Y5; -. DR SMR; Q5F6Y5; 1-158. DR EnsemblBacteria; AAW90052; AAW90052; NGO_1407. DR GeneID; 3281156; -. DR KEGG; ngo:NGO1407; -. DR PATRIC; 20336221; VBINeiGon24812_1659. DR HOGENOM; HOG000115327; -. DR KO; K03719; -. DR OMA; ATHADLF; -. DR OrthoDB; EOG6F29D2; -. DR BioCyc; NGON242231:GI2G-1317-MONOMER; -. DR Proteomes; UP000000535; 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; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000704}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|RuleBase:RU000704}; KW Transcription regulation {ECO:0000256|RuleBase:RU000704}. FT DOMAIN 6 69 HTH asnC-type DNA-binding. FT {ECO:0000259|PROSITE:PS50956}. SQ SEQUENCE 160 AA; 18018 MW; 71149C4F6F06DE94 CRC64; MPQLTLDKTD IKILQVLQEN GRLTNVELSE RVALSPSPCL RRLKQLEDAG IVRQYAALLS PESVNLGLQA FIRVSIRKAK DAREDFAASV RKWPEVLSCF ALTGETDYLL QAFFTDMNAF SHFVLDTLLS HHGVQDAQSS FVLKEIKHTT SLPLNHLLKE // ID Q5F6H3_NEIG1 Unreviewed; 576 AA. AC Q5F6H3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Septum formation inhibitor Maf {ECO:0000313|EMBL:AAW90214.1}; GN ORFNames=NGO_1585 {ECO:0000313|EMBL:AAW90214.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90214.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90214.1; -; Genomic_DNA. DR RefSeq; WP_010951299.1; NC_002946.2. DR RefSeq; YP_208626.1; NC_002946.2. DR ProteinModelPortal; Q5F6H3; -. DR EnsemblBacteria; AAW90214; AAW90214; NGO_1585. DR GeneID; 3281080; -. DR KEGG; ngo:NGO1585; -. DR PATRIC; 20336698; VBINeiGon24812_1895. DR HOGENOM; HOG000220763; -. DR OMA; DCPPKPK; -. DR OrthoDB; EOG66F037; -. DR BioCyc; NGON242231:GI2G-1482-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003587; Hint_dom_N. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 576 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256591. SQ SEQUENCE 576 AA; 63177 MW; 653E5C7DABE45FB4 CRC64; MKPLRRLTNL LAACAVAAVA LIQPALAADL AQDPFITDNT QRQHYEPGGK YHLFGDPRGS VSDRTGKINV IQDYTHQMGN LLIQQAAIQG NLGYTVRFSG HGHEEHAPFD NHAADSASEE KGNVDDGFTV YRLNWEGHEH HPADAYDGPK GGNYPKPTGA RDEYTYHVNG TARSIKLNPT DTRSIRQRIF DNYNNLGSNF SDRADEANRK MFEHNAKLDR WGNSMEFVNG VAAGALNPFI SAGEALGIGD ILYGTRYAID KAAMRNIAPL PAEGKFAAIG GLGSAAGFEK NTREAVDRWI QENPNAAETV EALVNVLPFA KVKNLTKAAK PGKAAVSGDF SKSYTCSFHG STLVKTADGY KAIAHIQAGD RVLSKDEASG ETGYKPVTAR YGNPYQETVY IEVSDGIGNS QTLISNRIHP FYSDGKWIKA EDLKAGSRLL SESGKTQTVR NIVVKPKPLK AYNLTVADWH TYFVKGNQAE TEGVWVHNDC PPKPKPTNHA QQRKEEAKND SHRSVGDSNR VVREGKQYLD SDTGNHVYVK GDKVVILTPD GRQVTQFKNS KANTSKRVKN GKWTPK // ID Q5F9K1_NEIG1 Unreviewed; 258 AA. AC Q5F9K1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89136.1}; GN ORFNames=NGO_0392 {ECO:0000313|EMBL:AAW89136.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89136.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89136.1; -; Genomic_DNA. DR RefSeq; WP_003692783.1; NC_002946.2. DR RefSeq; YP_207548.1; NC_002946.2. DR ProteinModelPortal; Q5F9K1; -. DR EnsemblBacteria; AAW89136; AAW89136; NGO_0392. DR GeneID; 3283017; -. DR KEGG; ngo:NGO0392; -. DR PATRIC; 20333791; VBINeiGon24812_0473. DR HOGENOM; HOG000218867; -. DR OMA; QPVNLVH; -. DR OrthoDB; EOG6SZ1GS; -. DR BioCyc; NGON242231:GI2G-371-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 258 AA; 28808 MW; C82149AF534AE4CF CRC64; MRAVPPPHIS ITGLGYLGLP LAQKFYRHGS RVAAIKRSLT SDDINLPIHL DTFDLNRTDA FQTALWRHHA DKPVWFFLLP PSFLAHYADT VKQWAELARA CNVQHLIFTS STSVYGDKAR ECDETAAPDP QTESARQILA AEQHLLDNGV PNIDILRLGG LYCAERHPVS RLVQKQNIQG GNRPVNIVHR DIAVENLFQT ASNPGGRRLK NIIEPRHPTR REFYTEEAAK LGLPAPDFSP DDSVGKIIRT VCDNGLSL // ID A0A0H4IWD1_NEIG1 Unreviewed; 139 AA. AC A0A0H4IWD1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63723.1}; GN ORFNames=NGO_07535 {ECO:0000313|EMBL:AKO63723.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63723.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63723.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63723; AKO63723; NGO_07535. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 139 AA; 16274 MW; 22220FA2F10AA895 CRC64; MIEMSKDYRN DLYDVYVSYP PQVDRGLIRE CLKENLGEEK AEGLIESLDS KPQVLVEEKC TWAKREELHD YFSYLGLDII TRIWSWKRSC RRRRGRAKEE ARMGKCPNIL NFTAGGKMIF PYVGNPSRPA ISNRWFSGC // ID A0A0H4IUY8_NEIG1 Unreviewed; 59 AA. AC A0A0H4IUY8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63595.1}; GN ORFNames=NGO_00595 {ECO:0000313|EMBL:AKO63595.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63595.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63595.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63595; AKO63595; NGO_00595. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6798 MW; D0F6158A9365E53C CRC64; MNRRTGTDAP APSRYRLFRI GCRREMTDGC RNVGRREWNA RLIPHMLAVL PARAVLCSK // ID A0A0H4ISL7_NEIG1 Unreviewed; 112 AA. AC A0A0H4ISL7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Methylase {ECO:0000313|EMBL:AKO63614.1}; GN ORFNames=NGO_01615 {ECO:0000313|EMBL:AKO63614.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63614.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63614.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63614; AKO63614; NGO_01615. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AKO63614.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63614.1}. FT DOMAIN 40 107 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 112 AA; 12968 MW; 2E0105BD430C2C62 CRC64; MIYKNKIKED GQDERLKEKA AQYRLFENND TFQTALKPKF TFIDLFAGIG GFRIAMQNLG GEYVFSSEWD EKAKLTYEAN FGEVPFGDIT LEEIKQYIPK QFDVLCGFTL SK // ID Q5F5W2_NEIG1 Unreviewed; 463 AA. AC Q5F5W2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Transporter {ECO:0000313|EMBL:AAW90425.1}; GN ORFNames=NGO_1807 {ECO:0000313|EMBL:AAW90425.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90425.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90425.1; -; Genomic_DNA. DR RefSeq; WP_003690317.1; NC_002946.2. DR RefSeq; YP_208837.1; NC_002946.2. DR EnsemblBacteria; AAW90425; AAW90425; NGO_1807. DR GeneID; 3282388; -. DR KEGG; ngo:NGO1807; -. DR PATRIC; 20337266; VBINeiGon24812_2168. DR HOGENOM; HOG000255106; -. DR KO; K03310; -. DR OMA; FWMWVTG; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NGON242231:GI2G-1705-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 18 39 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; 48539 MW; C3B77784467564EF CRC64; MQVFLDNLKA FFETVSSWVW GSVMLMLLVG TGIVLTVMLK GLQFTMLGYA LKQAFVPSKK YEGGAGHEGD ISHFAALMTA LSATIGTGNI AGVATAVVTG GPGAVFWMWM TAIFGMATKY GEGVLAVKYR VNNSKGEMSG GPMYYIEKGL GKNWKWMAVA FALFGTFASF GIGSSVQSNS VAQAVQTSFG IEPAYTGITL TVLTAVVVLG GIKGIAKAAS FIVPAMAVFY VLGGLSIIVI NSDALMPAVK LIFSDAFSAQ AVAGGAIGTV IRYGVARGVF SNEAGMGSAP IAAAAAKTDH PVRQALVSMT GTFLDTIVVC SITGIVLVMG LLGAGGEFVK PELSGAALTT VTFQKMLPGI GGWIVTIGLI FFAYSTILGW CYYGEKCAVY VFGEKFAALY RVGYVSSVMP GTVLSLDLVW LASDTFNGLM ALPNLTALLL MAKVIVNETR DFKQKITNGE LPH // ID A0A0H4IS89_NEIG1 Unreviewed; 86 AA. AC A0A0H4IS89; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63781.1}; GN ORFNames=NGO_10080 {ECO:0000313|EMBL:AKO63781.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63781.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63781.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63781; AKO63781; NGO_10080. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 8906 MW; D6A73047174889A2 CRC64; MNAGQHDVGV DGNLAAVEFG QAGGIVEDGR RVGGICRALR VDRLCAEVVA GCVDRCGGKG SAEQQDGFFS VKGVISVSVK RRTVDK // ID Q5F503_NEIG1 Unreviewed; 266 AA. AC Q5F503; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 88. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90734.2}; GN ORFNames=NGO_2137 {ECO:0000313|EMBL:AAW90734.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90734.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90734.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F503; -. DR EnsemblBacteria; AAW90734; AAW90734; NGO_2137. DR PATRIC; 20338123; VBINeiGon24812_2584. DR OMA; THGLEVI; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-2028-MONOMER; -. DR Proteomes; UP000000535; 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:SF455; PTHR24220:SF455; 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}; KW Cell membrane {ECO:0000256|SAAS:SAAS00419761}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00419641}; KW Membrane {ECO:0000256|SAAS:SAAS00419761}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00419679}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transport {ECO:0000256|SAAS:SAAS00419735}. FT DOMAIN 23 263 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 266 AA; 28987 MW; AA671D408DB27EB3 CRC64; MSALSSAPVV SDIGLCCMGK TMIILDKVSK HYQTRDKTRF AAVEPTSLEI QDGEIFGLMG YSGAGKSTLL RLINLLERPD TGKVNVCGQE LTALDAAALR QARQNIGMVF QQFNLLSNRT VAGNVAFPLE IAGWPSEKIK ARVAECLEIV GLTERAGHYP AQLSGGQKQR VGIARALAPK PQVILADEPT SALDPATTRS VLECLEDINK RFNVTIVIVT HEMSVIRRLC DRAALLDKGK VVEIVEVRGN QIHAQSEIGR ELIRED // ID Q5FAB0_NEIG1 Unreviewed; 679 AA. AC Q5FAB0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 77. 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 ORFNames=NGO_0117 {ECO:0000313|EMBL:AAW88877.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88877.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88877.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FAB0; -. DR EnsemblBacteria; AAW88877; AAW88877; NGO_0117. DR PATRIC; 20333135; VBINeiGon24812_0151. DR HOGENOM; HOG000036617; -. DR OMA; YEDETRI; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; NGON242231:GI2G-106-MONOMER; -. DR Proteomes; UP000000535; 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:AAW88877.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:AAW88877.2}; KW Hydrolase {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAW88877.2}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363016, KW ECO:0000313|EMBL:AAW88877.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 274 435 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 457 614 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. SQ SEQUENCE 679 AA; 74706 MW; 3B06EA60A823B77C CRC64; MSPETQKQLK ITDVSAKKLD KLNLHTAWDL VLHLPLRYED ETHIMPIKDA PIGVPCQVEG EVIHQEVTFK PRKQLIVQIA DGSGSVLFLR FIHFYASHQK QTAVGKRIRA VGEIKHGFYG DEMIHPKIRD AEGGGLAESL TPVYPTVNGL NQPTLRRIIQ TALDVTPLHD TLPDALLGRL KLPRLAESLR LLHSPPPSFT IHQLSDGTLP AWQRLKFDEL LAQQLSMRLA RQKRVSGTAA ALRGDGTLTQ ALRQALPFAL TDAQEKVVSE ICRDMAQTHP MHRLLQGDVG SGKTIVAALS ALTAIESGAQ VAVMAPTEIL AEQHFIKFKQ WLEPLGIEVV CLFGSLRKKA KDEAKAKLAD GSVKIAVGTH ALFSDGVAFH NLGLSIVDEQ HRFGVAQRLA LKNKGREVHQ LMMSATPIPR TLAMSFFADL DVSVIDELPP GRTPIKTRLV NNVRRAEVEG FVLGTCRKGR QAYWVCPLIE ESETLQLQTA AETLARLQTA LPEPNIGLVH GRMKAAEKAE VMAEFAAGRL NVLVATTVIE VGVDVPNAAL MVIEHAERMG LAQLHQLRGR VGRGAGESVC VLLFAEPLGE LAKARLKVIY EHTDGFEIAR QDLNIRGPGE FLGARQSGVP MLRFAKLEED LHLLEQARET APMLIEQNPE IVEAHLARWL SGREGYLGV // ID Q5FAA1_NEIG1 Unreviewed; 408 AA. AC Q5FAA1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=UPF0761 membrane protein NGO_0127 {ECO:0000256|HAMAP-Rule:MF_00672}; GN ORFNames=NGO_0127 {ECO:0000313|EMBL:AAW88886.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88886.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00672, ECO:0000256|SAAS:SAAS00038166}; Multi-pass membrane CC protein {ECO:0000256|HAMAP-Rule:MF_00672, CC ECO:0000256|SAAS:SAAS00038166}. CC -!- SIMILARITY: Belongs to the UPF0761 family. {ECO:0000256|HAMAP- CC Rule:MF_00672, ECO:0000256|SAAS:SAAS00539205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88886.1; -; Genomic_DNA. DR RefSeq; WP_003690589.1; NC_002946.2. DR RefSeq; YP_207298.1; NC_002946.2. DR ProteinModelPortal; Q5FAA1; -. DR DNASU; 3281248; -. DR EnsemblBacteria; AAW88886; AAW88886; NGO_0127. DR GeneID; 3281248; -. DR KEGG; ngo:NGO0127; -. DR PATRIC; 20333161; VBINeiGon24812_0164. DR HOGENOM; HOG000259417; -. DR KO; K07058; -. DR OMA; SVMTMMT; -. DR OrthoDB; EOG63NMKT; -. DR BioCyc; NGON242231:GI2G-115-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00672, KW ECO:0000256|SAAS:SAAS00434739}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00672, KW ECO:0000256|SAAS:SAAS00434739}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00672, KW ECO:0000256|SAAS:SAAS00434734, ECO:0000256|SAAS:SAAS00434739}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00672, KW ECO:0000256|SAAS:SAAS00434734}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00672, KW ECO:0000256|SAAS:SAAS00434734}. FT TRANSMEM 43 63 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 100 120 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 139 159 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 182 201 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 210 230 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. FT TRANSMEM 248 268 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00672}. SQ SEQUENCE 408 AA; 46384 MW; 7D0A2BD36E66A282 CRC64; MTFLQRWQGL ADNKICAFAW FVIRRFSEER VPQAAASMTF TTLLALVPVL TVMVAVASIF PVFDRWSDSF VSFVNQTIVP QGADMVFDYI DAFRDQANRL TAIGSVMLVV TSLMLIRTID NAFNRIWRVN TQRPWMMQFL VYWALLTFGP LSLGVGISFM VGSVQDSVLS SGAQQWADAL KTAARLAFMT LLLWGLYRFV PNRFVPARQA FVGALITAFC LETARFLFTW YMGNFDGYRS IYGAFAAVPF FLLWLNLLWT LVLGGAVLTS SLSYWQGEAF RRGFDSRGRF DDVLKILLLL DAAQKEGRTL SVQEFRRHIN MGYDELGELL EKLARYGYIY SGRQGWVLKT GADSIELSEL FKLFVYRPLP VERDHVNQAV DAVMTPCLQT LNMTLAEFDA QAKKQQQS // ID Q5F906_NEIG1 Unreviewed; 104 AA. AC Q5F906; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 74. DE RecName: Full=Integration host factor subunit beta {ECO:0000256|HAMAP-Rule:MF_00381, ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00062449}; DE Short=IHF-beta {ECO:0000256|HAMAP-Rule:MF_00381}; GN Name=ihfB {ECO:0000256|HAMAP-Rule:MF_00381}; GN Synonyms=himD {ECO:0000256|HAMAP-Rule:MF_00381}; GN ORFNames=NGO_0603 {ECO:0000313|EMBL:AAW89331.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89331.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00381, CC ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00021201}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC {ECO:0000256|HAMAP-Rule:MF_00381, ECO:0000256|RuleBase:RU003941, CC ECO:0000256|SAAS:SAAS00560763}. CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. CC {ECO:0000256|HAMAP-Rule:MF_00381, ECO:0000256|RuleBase:RU003939, CC ECO:0000256|SAAS:SAAS00560676}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89331.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F906; -. DR SMR; Q5F906; 45-97. DR EnsemblBacteria; AAW89331; AAW89331; NGO_0603. DR PATRIC; 20334282; VBINeiGon24812_0713. DR HOGENOM; HOG000043828; -. DR OMA; FVPFFKP; -. DR OrthoDB; EOG615VS6; -. DR BioCyc; NGON242231:GI2G-571-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_00381, KW ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00447986}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00381, KW ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00560702}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00381, KW ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00448004}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00381, KW ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00448004}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_00381, KW ECO:0000256|RuleBase:RU003941, ECO:0000256|SAAS:SAAS00448011}. SQ SEQUENCE 104 AA; 11804 MW; 12DFA7350CDCBD8D CRC64; MTKSELMVRL AEVFAAKNGT HLLAKDVEYS VKVLVDTMTR SLARGQRIEI RGFGSFDLNH RPARIGRNPK TGERVEVPEK HVPHFKPGKE LRERVDLALK ENAN // ID Q5FA13_NEIG1 Unreviewed; 199 AA. AC Q5FA13; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020486}; DE EC=3.6.1.19 {ECO:0000256|HAMAP-Rule:MF_01405, ECO:0000256|SAAS:SAAS00020468}; DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01405}; GN ORFNames=NGO_0221 {ECO:0000313|EMBL:AAW88974.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88974.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_01405}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00020483}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01405}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_01405}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01405, CC ECO:0000256|SAAS:SAAS00020467}. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP- CC Rule:MF_01405, ECO:0000256|RuleBase:RU003781, CC ECO:0000256|SAAS:SAAS00542593}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88974.1; -; Genomic_DNA. DR RefSeq; WP_003687551.1; NC_002946.2. DR RefSeq; YP_207386.1; NC_002946.2. DR ProteinModelPortal; Q5FA13; -. DR EnsemblBacteria; AAW88974; AAW88974; NGO_0221. DR GeneID; 3281441; -. DR KEGG; ngo:NGO0221; -. DR PATRIC; 20333381; VBINeiGon24812_0273. DR HOGENOM; HOG000293319; -. DR KO; K02428; -. DR OMA; CEGLWHG; -. DR OrthoDB; EOG6CZQQP; -. DR BioCyc; NGON242231:GI2G-204-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|RuleBase:RU003781, ECO:0000256|SAAS:SAAS00425982}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425988}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00426004}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425941}; KW Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425996}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01405, KW ECO:0000256|SAAS:SAAS00425966}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT REGION 12 17 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT REGION 73 74 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT METAL 73 73 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_01405}. FT BINDING 160 160 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01405}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01405}. SQ SEQUENCE 199 AA; 21317 MW; E25B6DD0DB9B4651 CRC64; MSEKPEKIVL ASGNAGKLKE FGNLFKPYGI TVLPQSAFGI PECPEPYPTF VENALAKARH AAGHSGLPAL ADDSGICAAA LNGAPGIHSA RYAGSNPKSD TANNLKLAAE LAGKADKSCS YVCVLVFVRH KDDPRPIIAE GIWHGQWHDT PLGQNGFGYD PYFYLPEHGK TAAELDSEVK NRESHRAQAL ADLIRKLAL // ID Q5F6Z3_NEIG1 Unreviewed; 553 AA. AC Q5F6Z3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 72. DE SubName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase {ECO:0000313|EMBL:AAW90044.2}; GN ORFNames=NGO_1396 {ECO:0000313|EMBL:AAW90044.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90044.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90044.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6Z3; -. DR EnsemblBacteria; AAW90044; AAW90044; NGO_1396. DR PATRIC; 20336185; VBINeiGon24812_1641. DR HOGENOM; HOG000259450; -. DR OMA; FKLDQNS; -. DR OrthoDB; EOG6ZPSVS; -. DR BioCyc; NGON242231:GI2G-1309-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR007859; ETFD_OxRdtase/FixX. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR PANTHER; PTHR10617:SF107; PTHR10617:SF107; 1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF05187; ETF_QO; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ubiquinone {ECO:0000313|EMBL:AAW90044.2}. FT DOMAIN 13 62 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 553 AA; 61025 MW; 8C45996533E0D7C6 CRC64; MTESITRDSM QYDVVIVGAG PSGLSAAIKL KQLAEQNGRE ISVCVVEKGS EAGAHSLAGA VIDPIALNEL IPDWKEKGAP LTRTVTQDKV LFLTEKKAFN LPITPNFDNH GNYIVSLGEV VRWLAEQAEN MGVEIYPGFA AAEVLYHEDG SVKGIATGNM GVGKDGGPTD SFQPGMELWA RQTLFAEGCR GSLSKQIIER FQLDQNSQPQ TYGLGIKEVW EVPSEQHQPG LVVHSAGWPL DSKTYGGAFI YHFDDNKVAV GFVVGLDYQN PYLSPFEEFQ RFKTHPEIRK TFEGGRRIAY GARSLIEGGL QSLPKLSFKG GVLIGDAAGF LNMPRIKGIH TSMKSAMLAA EAVFPLLENF EEVESFDSGK EAGNYQKLFE QSWLYQELYA ARNVRPSFKW GVYLGSLYTG IDQMIFRGKA PWTLKHHGKD NEQLKKAAVC KPIDYPKPDG VLTFDRLSSV FLANLAHEEN QPDHLVLNNP QTMIDVNYKE YASPETRYCP AGVYEIIEEN GSPRLQINAA NCVHCKTCDI KDPTQNITWI CPEGASGPNY GGM // ID A0A0H4J5N9_NEIG1 Unreviewed; 234 AA. AC A0A0H4J5N9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AKO63702.1}; GN ORFNames=NGO_06725 {ECO:0000313|EMBL:AKO63702.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63702.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63702.1; -; Genomic_DNA. DR RefSeq; WP_030003515.1; NC_002946.2. DR RefSeq; YP_008914854.1; NC_002946.2. DR EnsemblBacteria; AKO63702; AKO63702; NGO_06725. DR GeneID; 19593003; -. DR KEGG; ngo:NGO1277a; -. DR Proteomes; UP000000535; 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; -; 3. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 234 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 234 AA; 26546 MW; 3CBC43F38B99CD32 CRC64; MQADLAYAAE RITHDYPEPT GAKKGKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWNDN KYSVNIKELG RKDGTSSSGR YLNIQTRKTE NQENGTFHAV SSLGLSTVYD FRANDKFKPY IGVRVAYGHV RHQVHSMEKE TTTVTTYPSD GSAKTSVPSE MPPKPAYHEN RSSRRLGFGA MAGVGIDVAP GLTLDAGYRY HYWGRLENTR FKTHEASLGM RYRF // ID A0A0H4IT95_NEIG1 Unreviewed; 67 AA. AC A0A0H4IT95; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63794.1}; GN ORFNames=NGO_10565 {ECO:0000313|EMBL:AKO63794.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63794.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63794.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63794; AKO63794; NGO_10565. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7743 MW; 382C345A6B7C1BF7 CRC64; MLKRNLGFDT FKLITIFFLG IRRLQSKHIR AIWDDKSGAI VIRDPNSKDG GTAFRPTLGK TYFDKQK // ID Q5F9X6_NEIG1 Unreviewed; 307 AA. AC Q5F9X6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 100. DE RecName: Full=GTPase Era {ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|SAAS:SAAS00085723}; GN Name=era {ECO:0000256|HAMAP-Rule:MF_00367}; GN ORFNames=NGO_0260 {ECO:0000313|EMBL:AAW89011.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89011.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00367, ECO:0000256|SAAS:SAAS00337158}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367, CC ECO:0000256|SAAS:SAAS00085777}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367}. CC Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral CC membrane protein {ECO:0000256|HAMAP-Rule:MF_00367}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. {ECO:0000256|HAMAP- CC Rule:MF_00367, ECO:0000256|RuleBase:RU003761, CC ECO:0000256|SAAS:SAAS00534654}. CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain. CC {ECO:0000256|HAMAP-Rule:MF_00367}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000256|HAMAP- CC Rule:MF_00367}. CC -!- SIMILARITY: Contains Era-type G (guanine nucleotide-binding) CC domain. {ECO:0000256|SAAS:SAAS00494973}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89011.2; -; Genomic_DNA. DR RefSeq; WP_025455773.1; NC_002946.2. DR RefSeq; YP_207423.2; NC_002946.2. DR ProteinModelPortal; Q5F9X6; -. DR EnsemblBacteria; AAW89011; AAW89011; NGO_0260. DR GeneID; 3281558; -. DR KEGG; ngo:NGO0260; -. DR PATRIC; 20333479; VBINeiGon24812_0320. DR HOGENOM; HOG000245597; -. DR KO; K03595; -. DR OMA; FDDITHN; -. DR OrthoDB; EOG68DD1Q; -. DR BioCyc; NGON242231:GI2G-243-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00367}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00367}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|SAAS:SAAS00415684}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|RuleBase:RU003761, ECO:0000256|SAAS:SAAS00494972}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00367}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|RuleBase:RU003761, ECO:0000256|SAAS:SAAS00494972}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|SAAS:SAAS00415696}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|SAAS:SAAS00415641}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00367, KW ECO:0000256|SAAS:SAAS00415641}. FT DOMAIN 17 186 Era-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51713}. FT DOMAIN 209 293 KH type-2. {ECO:0000259|PROSITE:PS50823}. FT NP_BIND 25 32 GTP. {ECO:0000256|HAMAP-Rule:MF_00367}. FT NP_BIND 72 76 GTP. {ECO:0000256|HAMAP-Rule:MF_00367}. FT NP_BIND 133 136 GTP. {ECO:0000256|HAMAP-Rule:MF_00367}. SQ SEQUENCE 307 AA; 34538 MW; 9A9D2089F1DC0001 CRC64; MDIETFLAGE RAAGGYRCGF VAIVGRPNVG KSTLMNHLIG QKISITSKKA QTTRNRVTGI YTDDTAQFVF VDTPGFQTDH RNALNDRLNQ NVTEALGGVD VVVFVVEAMR LTDADRVVLK QLPKHTPVIL VINKIDKDKA KDRYALEAFV AQVRAEFEFA AAEAVSAKHG LRIANLLELL KPYLPESVPM YPEDMVTDKS ARFLAMEIVR EKLFRYLGEE LPYAMNVEVE QFEEGDGLNR IYIAVLVDKE SQKAILIGKG GERLKKISTE ARLDMEKLFD NKVFLKVWVK VKSGWADDIR FLRELGL // ID A0A0H4IRW8_NEIG1 Unreviewed; 152 AA. AC A0A0H4IRW8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63666.1}; GN ORFNames=NGO_04780 {ECO:0000313|EMBL:AKO63666.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63666.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63666.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63666; AKO63666; NGO_04780. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR SUPFAM; SSF48295; SSF48295; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 152 AA; 17491 MW; 6C999A47BA38FB70 CRC64; MIFVNSLYFS ISDSLVRKWV ARYRLHGESG IKRRKHTTKY SVEYKLEAIR PVTGQGMSQK AAADQLNLPE CSVLPQWLRL YRLNGINGLK PKPKGRKPVK KQYPPQTKKA DYLKTKEELF AELAYLKAEA AVLKKLDALK EVRQKERNSS QG // ID Q5F7C6_NEIG1 Unreviewed; 300 AA. AC Q5F7C6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 61. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89911.1}; GN ORFNames=NGO_1252 {ECO:0000313|EMBL:AAW89911.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89911.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89911.1; -; Genomic_DNA. DR RefSeq; WP_003689718.1; NC_002946.2. DR RefSeq; YP_208323.1; NC_002946.2. DR EnsemblBacteria; AAW89911; AAW89911; NGO_1252. DR GeneID; 3281854; -. DR KEGG; ngo:NGO1252; -. DR PATRIC; 20335837; VBINeiGon24812_1473. DR HOGENOM; HOG000271939; -. DR OMA; SIWYYVI; -. DR OrthoDB; EOG6JTC7T; -. DR BioCyc; NGON242231:GI2G-1169-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 92 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 145 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 151 168 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 207 227 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 259 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 284 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 10 141 EamA. {ECO:0000259|Pfam:PF00892}. FT DOMAIN 162 282 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 300 AA; 32582 MW; AD1AB310B7BE4390 CRC64; MDTAKKDILG SGWMLVAAAC FTVMNVLIKE ASAKFALGSG ELVFWRMLFS TVTLGAAAVL RRDTFRTPHW KNHLNRSMVG TGAMLLLFYA VTHLPLTTGV TLSYTSSIFL AVFSFLILKE RISVYTQAVL LLGFAGVVLL LNPSFRSGQE PAALAGLAGG AMSGWAYLKV RELSLAGEPG WRVVFYLSAT GVAMSSVWAT LTGWHTLSFP SAVYLSGIGV SALIAQLSMT RAYKVGDKFT VASLSYMTVV FSALSAAFFL GEELFWQEIL GMCIIILSGI LSSIRPIAFK QRLQALFRQR // ID Q5FA45_NEIG1 Unreviewed; 372 AA. AC Q5FA45; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Deacetylase {ECO:0000313|EMBL:AAW88942.1}; GN ORFNames=NGO_0187 {ECO:0000313|EMBL:AAW88942.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88942.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88942.1; -; Genomic_DNA. DR RefSeq; WP_010951007.1; NC_002946.2. DR RefSeq; YP_207354.1; NC_002946.2. DR ProteinModelPortal; Q5FA45; -. DR EnsemblBacteria; AAW88942; AAW88942; NGO_0187. DR GeneID; 3281567; -. DR KEGG; ngo:NGO0187; -. DR PATRIC; 20333303; VBINeiGon24812_0234. DR HOGENOM; HOG000225183; -. DR OMA; CEHADAT; -. DR OrthoDB; EOG6TN43P; -. DR BioCyc; NGON242231:GI2G-172-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 372 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256255. FT DOMAIN 41 327 Hist_deacetyl. FT {ECO:0000259|Pfam:PF00850}. SQ SEQUENCE 372 AA; 41130 MW; DC79383C7C0B695A CRC64; MPLTRLFLKL YALLRLFLGK NAQTAWIFHP ACTGHDPGAN HPDSPDRILC IEQALRRAGI WQHLQTVEAE EISDTRLALV RSSKYLNRLE SCLPEDGKIC RLDDDTVISK NSLSAARFSA GSAVQAVDMV MKRKAWHAFC AARPPEHHAK SGKAGGFCLL NNVAAGVMHA IAEYRLKRIA VIDFDVHYGD GTAEIFKDDP RILFFNLFET DLFPFPENNG MPDGGNMVHL PLPSGTGSRT FREAVRRQWL PRLAAFKPEL VLLSAGFDAH RLDESGRLNL HEADFAWLTH KIIQTASSCP GKIVSVLEGG YTLEPLAQSA AEHIRVLAGL GKSDAATAYQ KTLNPTKKPF AKPKTGQVRQ PTQSDRYDIN AV // ID Q5F9I3_NEIG1 Unreviewed; 443 AA. AC Q5F9I3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 55. DE SubName: Full=Peptidase PmbA {ECO:0000313|EMBL:AAW89154.1}; GN Name=pmbA {ECO:0000313|EMBL:AAW89154.1}; GN ORFNames=NGO_0411 {ECO:0000313|EMBL:AAW89154.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89154.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89154.1; -; Genomic_DNA. DR RefSeq; WP_003687847.1; NC_002946.2. DR RefSeq; YP_207566.1; NC_002946.2. DR ProteinModelPortal; Q5F9I3; -. DR EnsemblBacteria; AAW89154; AAW89154; NGO_0411. DR GeneID; 3282532; -. DR KEGG; ngo:NGO0411; -. DR PATRIC; 20333833; VBINeiGon24812_0494. DR HOGENOM; HOG000224928; -. DR KO; K03592; -. DR OMA; TCEVPVL; -. DR OrthoDB; EOG65J4ZF; -. DR BioCyc; NGON242231:GI2G-389-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 443 AA; 47796 MW; 780EADFED348DA48 CRC64; MLFNHTASEL LDLCRRTLDL AKAAGATAAE ADFSESLGQS VSVRLGEIEQ IEFQQDKSLD ITVYVGKRKG RAGTADFSEQ ALRDTVRAAA DIARHTAEDG CAGLADPELM AQHIGDPDLY HEWDLDTEAA VGLAKQCEQA ALDTDSRIEN SEGAAVQTGH YQYVYGNTHG FAAHRQSTHH SISCSVVAAD ENGMQRDYWY DSACRHPDMD SPETIGQTAA RRTLRRLGSR SIPTGSYPVL FDTTVSGGLI GHLVGTLSGG ALYRQSSFLI DSIGKKVLPD FLNLREEPHI PRSFRSSYFD AEGVATAPRF VIQNGIVEGY FLGSYSARKL GMQTTGNAGG AHNLYLNHTH ETQSDLLKEM GTGLLVTELM GQGANTITGD YSRGAAGFWV ENGVIAYPVH EITVAGRLQD MYRDIVGVAD DALRRSSNKI GSILIAGMTV AGS // ID A0A0H4J5H3_NEIG1 Unreviewed; 189 AA. AC A0A0H4J5H3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Tail fiber protein {ECO:0000313|EMBL:AKO63647.1}; GN ORFNames=NGO_03835 {ECO:0000313|EMBL:AKO63647.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63647.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63647.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63647; AKO63647; NGO_03835. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR005068; Phage_lambda_Stf-r2. DR Pfam; PF03406; Phage_fiber_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 189 AA; 19323 MW; BD2696AA98C1B36A CRC64; MANATEQNQF DQAVRLIEPG DSVVVGPGAP VNQPLQALAN RTLLLKNQTE ALQTASDTKA AASTAVNAGD GLTGGGSLAQ SRTIALGAPG QITATSQNTV PKNGHTHAID TARTDRAGIV RLDNAISEAE DTAATPKAVK TALDQARAAA ATADLKVSLS DNQTVTGQKT FTAETQFQSG IRLSANPTH // ID A0A0H4IV86_NEIG1 Unreviewed; 305 AA. AC A0A0H4IV86; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63690.1}; GN ORFNames=NGO_06020 {ECO:0000313|EMBL:AKO63690.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63690.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63690.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63690; AKO63690; NGO_06020. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat. DR Pfam; PF05681; Fumerase; 1. DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 11 288 Fumerase. {ECO:0000259|Pfam:PF05681}. SQ SEQUENCE 305 AA; 33003 MW; C2C0C970182CB98F CRC64; MTVIKQEDFI QSICDAFQFI SYYHPKDYID ALYKAWQKEE NPAAKDAMTQ ILVNSRMCAE NNRPICQDTG IATVFLKVGM DVQWDADMSV EKMVNEGVRR AYTWEGNTLR ASVLADPAGK RQNTKDNTPA VIHMSIVPGG KVEVTCAAKG GGSENKSKLA MLNPSDNIVD WVLKTIPTMG AGWCPPGILG IGIGGTPEKA VLMAKESLMS HIDIQELQEK AASGAELSTT EALRLELFEK VNALGIGAQG LGGLTTVLDV KILDYPTHAA SKPIAMIPNC AATRHVEFEL DGSGPVELTP PRVED // ID A0A0H4ISB8_NEIG1 Unreviewed; 143 AA. AC A0A0H4ISB8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63811.1}; GN ORFNames=NGO_11140 {ECO:0000313|EMBL:AKO63811.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63811.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63811.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63811; AKO63811; NGO_11140. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 143 AA; 15273 MW; E6215638C173A7B2 CRC64; MPTDPDSRLR GNDEAILLAE GQKSAVTGYC PNHGIWPKDN TSAGVASSAA DIKGKYVQKV EVNNGVVTAT MASSNVNKEI QGKRLSLWAK RENGSVKWFC GQPVTRDDKA KDDVKADGTA GTKIDTKHLP STCRDESSLP GIT // ID Q5F564_NEIG1 Unreviewed; 351 AA. AC Q5F564; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE SubName: Full=Glycosyl transferase family 1 {ECO:0000313|EMBL:AAW90673.1}; GN ORFNames=NGO_2072 {ECO:0000313|EMBL:AAW90673.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90673.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90673.1; -; Genomic_DNA. DR RefSeq; WP_010951397.1; NC_002946.2. DR RefSeq; YP_209085.1; NC_002946.2. DR ProteinModelPortal; Q5F564; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW90673; AAW90673; NGO_2072. DR GeneID; 3282845; -. DR KEGG; ngo:NGO2072; -. DR PATRIC; 20337975; VBINeiGon24812_2510. DR HOGENOM; HOG000220771; -. DR OMA; FPSTGHT; -. DR OrthoDB; EOG68DD0W; -. DR BioCyc; NGON242231:GI2G-1967-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90673.1}. FT DOMAIN 16 170 Glyco_trans_4-like_N. FT {ECO:0000259|Pfam:PF13439}. SQ SEQUENCE 351 AA; 39169 MW; C1623496193505FC CRC64; MKLKIDIATN NFKHGGGTER YTLDLVKGLN RQNITPAVYA TKFDHGIPEY AMIEPHLVDQ RRTLKKLRSF LFSSRLAQTR KNSAAKLIAC HHADYADLLI CGGTHLGYLH HMAQKPNLLD RLAIRRNRSN YATAKLIVAH SHMMRRELVG LYGVPPERIQ VAPPPADTER FFPQPRETAA LRAKYGFADH ETVFLFPSTG HTRKGLELLA DFFEQTELPV KLAVAGSPLP RPMKNVVGLG FCTDMPELYR AADFTIMASL YEPFGLVGVE SALCGTRVVL SENMACTEVM NEEAGFFFSR QNPETLAQAV AQAVSLKKQG GHRLSDPMRA LNYNPSLSHH IDRLTDMLAS V // ID Q5F9H9_NEIG1 Unreviewed; 452 AA. AC Q5F9H9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 79. 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 ORFNames=NGO_0415 {ECO:0000313|EMBL:AAW89158.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89158.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89158.1; -; Genomic_DNA. DR RefSeq; WP_010359904.1; NC_002946.2. DR RefSeq; YP_207570.1; NC_002946.2. DR ProteinModelPortal; Q5F9H9; -. DR EnsemblBacteria; AAW89158; AAW89158; NGO_0415. DR GeneID; 3283001; -. DR KEGG; ngo:NGO0415; -. DR PATRIC; 20333841; VBINeiGon24812_0498. DR HOGENOM; HOG000256526; -. DR KO; K00970; -. DR OMA; RFMAKLD; -. DR OrthoDB; EOG6PZX7Q; -. DR BioCyc; NGON242231:GI2G-393-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_00957}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|SAAS:SAAS00415369}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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:0000256|HAMAP-Rule:MF_00957, KW ECO:0000256|RuleBase:RU003953, ECO:0000256|SAAS:SAAS00415377}. FT DOMAIN 55 177 PolyA_pol. {ECO:0000259|Pfam:PF01743}. FT DOMAIN 205 252 PolyA_pol_RNAbd. FT {ECO:0000259|Pfam:PF12627}. FT DOMAIN 318 440 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 452 AA; 51407 MW; 74173E3C89DE1F23 CRC64; MLKKWLNKML PSGRSSKKAE SKTVIPAERH NISAEMLSFA AENVIRRLKG AGFQAYVVGG AVRDLLLGIE PKDFDVATDA TPEQVHKLFR RSRIIGRRFQ IVHVMNGAEI IEVTTFRGGA KVHQNAHGRI MKDNTYGSIE EDAMRRDFTC NALYYDPEKE EILDFHNGIA DVAARRLVMI GNAAERYQED PVRILRAIRL SGKLGFELSE ETAAPIAESI CRLKHEPVAR LFDEIMKLLF SGHARECLKR LNGFDIPDIH PLLNALRVSD GIAGKMTALA LKNTDERLRA DKSVSVGFVL AALMWPELDR HWKSNLQQGL KPTPALSDAI NTMRETVERG WGVPQRFSAT MREIWMFQPQ FENRKGARPH KLFAQARFRA AYDFLLLRAE TGNADRALAE WWTAFQTASA EQRTEMTKNE AAARHEKNEG QAKKRRRRRR KPKPKVVGTD WE // ID Q5F9M6_NEIG1 Unreviewed; 459 AA. AC Q5F9M6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=DNA repair protein radA {ECO:0000256|RuleBase:RU003555}; GN ORFNames=NGO_0367 {ECO:0000313|EMBL:AAW89111.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89111.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89111.1; -; Genomic_DNA. DR RefSeq; WP_003690821.1; NC_002946.2. DR RefSeq; YP_207523.1; NC_002946.2. DR ProteinModelPortal; Q5F9M6; -. DR MEROPS; S16.A04; -. DR EnsemblBacteria; AAW89111; AAW89111; NGO_0367. DR GeneID; 3283025; -. DR KEGG; ngo:NGO0367; -. DR PATRIC; 20333729; VBINeiGon24812_0442. DR HOGENOM; HOG000218329; -. DR KO; K04485; -. DR OMA; FEGERGH; -. DR OrthoDB; EOG6DRPHC; -. DR BioCyc; NGON242231:GI2G-346-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 49507 MW; B84F45F8AF36CFDE CRC64; MAKTLKTLYQ CTECGGTSPK WQGKCPHCGE WNTLQESFAA PEPKNARFQS WAADASTVQS LSAVTAAEVP RNPTGMGELD RVLGGGLVDG AVILLGGDPG IGKSTLLLQT IAKMAQSRKV LYVSGEESAQ QVALRSQRLE LHAEGVNLLA EIRMEAIQAA LKQHQPEVVV IDSIQTMYSD QITSAPGSVS QVRECAAQLT RMAKQMGIAM ILVGHVTKDG AIAGPRVLEH MVDTVLYFEG DQHSNYRMIR AIKNRFGAAN ELGVFAMTEN GLKGVSNPSA IFLASYRDDT PGSCVLVTQE GSRPLLVEIQ ALVDDAHGFT PKRLSVGLEQ NRLAMLLAVL NRHGGIACFD QDVFLNAVGG VKIGEPAADL AVILAMLSSF RNRPMPEKTV VFGEIGLSGE VRPVARGQER LKEAEKLGFK RAIVPKANMP RNAKEFPNLK IHGVSSLQEA IDICRDSRE // ID Q5F7Y3_NEIG1 Unreviewed; 659 AA. AC Q5F7Y3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996}; DE EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996}; GN ORFNames=NGO_1028 {ECO:0000313|EMBL:AAW89704.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89704.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89704.1; -; Genomic_DNA. DR RefSeq; WP_003688227.1; NC_002946.2. DR RefSeq; YP_208116.1; NC_002946.2. DR ProteinModelPortal; Q5F7Y3; -. DR SMR; Q5F7Y3; 3-659. DR EnsemblBacteria; AAW89704; AAW89704; NGO_1028. DR GeneID; 3282211; -. DR KEGG; ngo:NGO1028; -. DR PATRIC; 20335272; VBINeiGon24812_1202. DR HOGENOM; HOG000225953; -. DR KO; K00615; -. DR OMA; WEVLYVE; -. DR OrthoDB; EOG6N3CRG; -. DR BioCyc; NGON242231:GI2G-949-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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:AAW89704.1}. FT DOMAIN 9 29 TRANSKETOLASE_1. FT {ECO:0000259|PROSITE:PS00801}. SQ SEQUENCE 659 AA; 71575 MW; C34C7E89B37D6A36 CRC64; MSQLANVIRF LSADAVQKAN SGHPGAPMGM AEMAETLWTK FLNHNPANPK FYNRDRFVLS NGHASMLLYS LLHLTGYNLS IEDLKNFRQL HSKTPGHPEY GYTDGVETTT GPLGQGIANA VGMALAEKIL AAEFNKDGLN IVDHYTYVFM GDGCLMEGVS HEACSLAGTL GLGKLIVLYD DNNISIDGKV DGWFTENIPQ RFESYGWHVV PNVNGHDTAA IQTAIEAARA ETGKPSIICC KTLIGKGSAN KEGSHKTHGA PLGADEIEAT RKHLGWAYPA FEIPQEIYDA WNAKEKGAKL EAGWNELFAQ YQAKYPAEAA EFVRRMDKKL PENFDEYVQT ALKEVCAKAE TVATRKASQN SIEILAKELP ELVGGSADLT PSNLTDWSNS VSVTRDKGGN YIHYGVREFG MGAIMNGLVL HGGVKPFGAT FLMFSEYERN ALRMAALMKI NPVFVFTHDS IGLGEDGPTH QPIEQTATLR LIPNMDVWRP CDTAESLVAW AEAAKAEDHP SCLIFSRQNL KFQARSEQQL NDIKRGAYVI SEAQGNAQAV IIATGSEVGL AVEAQKVLAG QGIAVRVVSM PSTSVFDRQD AAYQAAVLPE GLPRIAVEAG HTNGWYKYVG LNGAVVGINR FGESAPADLL FKAFGFTVDN VVDTVKSVL // ID A0A0H4IRZ5_NEIG1 Unreviewed; 177 AA. AC A0A0H4IRZ5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Pseudouridine synthase {ECO:0000313|EMBL:AKO63696.1}; GN ORFNames=NGO_06200 {ECO:0000313|EMBL:AKO63696.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63696.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63696.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63696; AKO63696; NGO_06200. DR Proteomes; UP000000535; 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; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR01621; RluA-like; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 10 153 PseudoU_synth_2. FT {ECO:0000259|Pfam:PF00849}. SQ SEQUENCE 177 AA; 20072 MW; 7817D086D54314C1 CRC64; MWEILFRHQD FVAINKPQGI SVHRSGGEVS LTATLAAQLG VEKVWLLHRL DKQAGGILLF ALNSQSAAVL AAQFAERKMK KSYLALSDRK PSKKQGWIKG GMEKSRRGMW KLTRNMENIA VTRFFSIRIS EKMRLFILEP HTGKTHQLRV VMKSLGSSIF GDSLYRGTES ETMFLYA // ID Q5FA40_NEIG1 Unreviewed; 374 AA. AC Q5FA40; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 102. DE RecName: Full=Polyamine-transporting ATPase {ECO:0000256|SAAS:SAAS00083160}; DE EC=3.6.3.31 {ECO:0000256|SAAS:SAAS00083160}; GN ORFNames=NGO_0192 {ECO:0000313|EMBL:AAW88947.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88947.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88947.2; -; Genomic_DNA. DR RefSeq; WP_010356995.1; NC_002946.2. DR RefSeq; YP_207359.2; NC_002946.2. DR ProteinModelPortal; Q5FA40; -. DR EnsemblBacteria; AAW88947; AAW88947; NGO_0192. DR GeneID; 3281640; -. DR KEGG; ngo:NGO0192; -. DR PATRIC; 20333313; VBINeiGon24812_0239. DR KO; K11076; -. DR OMA; YVGHGIS; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-177-MONOMER; -. DR Proteomes; UP000000535; 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}; KW Cell membrane {ECO:0000256|SAAS:SAAS00458580}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00458628}; KW Membrane {ECO:0000256|SAAS:SAAS00458580}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000256|SAAS:SAAS00452173}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transport {ECO:0000256|SAAS:SAAS00452289}. FT DOMAIN 13 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 374 AA; 42160 MW; 72254F8E874C504F CRC64; MTATTASSAK PYLQIQGLVK KFGDNYAVDN IDLDIYQNEI FALLGSSGSG KSTLLRMLAG MESPNQGKII LDGQDITKLA PYDRPINMMF QSYALFPHMT VEQNIAFGLK QDKMPKGEID ARVEEMLRLV QMTKFAKRKP HQLSGGQQQR IALARSLAKR PKILLLDEPL GALDKKLRQQ TQLELVNTLE QVGVTCIMVT HDQEEAMTMA TRIAIMSDGQ LQQVGTPSDV YDYPNSRFTA EFIGETNIFD GVVIENHADY AVIECEGLEN HVRIDHGLGG PSEQDLWVSI RPEDIDLYKE KPEYLGDYNW AKGTVKEIAY LGSFAIYHIK LANGRVVKSQ VPAPYWYVRN ITPPTWDETV YISWPENQPT PLFR // ID Q5F703_NEIG1 Unreviewed; 234 AA. AC Q5F703; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 48. DE SubName: Full=Pretoxin HINT domain protein {ECO:0000313|EMBL:AAW90034.1}; GN ORFNames=NGO_1386 {ECO:0000313|EMBL:AAW90034.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90034.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90034.1; -; Genomic_DNA. DR RefSeq; WP_003705817.1; NC_002946.2. DR RefSeq; YP_208446.1; NC_002946.2. DR ProteinModelPortal; Q5F703; -. DR EnsemblBacteria; AAW90034; AAW90034; NGO_1386. DR GeneID; 3281277; -. DR KEGG; ngo:NGO1386; -. DR PATRIC; 20336165; VBINeiGon24812_1631. DR HOGENOM; HOG000219103; -. DR OMA; RNQINRY; -. DR OrthoDB; EOG6QCD9V; -. DR BioCyc; NGON242231:GI2G-1299-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 234 AA; 25830 MW; 01B8270EC5C54681 CRC64; MVKTADGYKA IAHIQAGDRV LSKDEASGET GYKPVTARYG NPYQETVYIE VSDGIGNSQT LISNRIHPFY SDGKWIKAED LKAGSRLFAE SGKTQTVRNI IVKPTPLKAY NLTVADWHTY FVKGSQAETE GVWVHNDCPY GNLSDNKSVG EGKKFTPAQK KAIIQENMNR NGGVVKSDQS GEVLVRPKKS QKGITPPSNE WQIDHVQAKS KGGSNSYKNA QVLSRRENIK KSNK // ID A0A0H4IUX8_NEIG1 Unreviewed; 110 AA. AC A0A0H4IUX8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63585.1}; GN ORFNames=NGO_00280 {ECO:0000313|EMBL:AKO63585.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63585.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63585.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63585; AKO63585; NGO_00280. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 10907 MW; A9A785C6B8E8DBDB CRC64; MLRGIPSAAG APQTAGFGKP PDPAPAGLPV AKPPSPGCQR GMFAKVTRPS DGVQCIGLPH HSPCALIHGT AVFGNPQPFA RPAIAACAAM AGRGGGIFQV AATFPNNLTA // ID A0A0H4J5G1_NEIG1 Unreviewed; 182 AA. AC A0A0H4J5G1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63637.1}; GN ORFNames=NGO_03650 {ECO:0000313|EMBL:AKO63637.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63637.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63637.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63637; AKO63637; NGO_03650. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 182 AA; 20088 MW; A7AA3DB411B6AF12 CRC64; MELITTGEGA DGDLLVNGSY GIRSFADLKL EYKPELSVRS NHDIIFNNDF QSVDVQPYSG NIHLDVKGKI QFNLNVADKV TDPTTHQEKL VNDNALVRYV NNITPSDEND KGSISFHSKT GNLFNMNVNV HKGTHHFGIH NLRNTNVNLT AEDGDNVVAI KGKLAEPMPA GKVESTSFFK GY // ID A0A0H4IS41_NEIG1 Unreviewed; 59 AA. AC A0A0H4IS41; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63721.1}; GN ORFNames=NGO_07440 {ECO:0000313|EMBL:AKO63721.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63721.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63721.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63721; AKO63721; NGO_07440. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6703 MW; A35895FCDBF7D1CD CRC64; MGFSFCIEKH QSALAGDEAQ ADNINNNNKL PKFAFIGNNN SLKPAFRRLN SNKCRLNRY // ID A0A0H4IRV7_NEIG1 Unreviewed; 94 AA. AC A0A0H4IRV7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63656.1}; GN ORFNames=NGO_03985 {ECO:0000313|EMBL:AKO63656.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63656.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63656.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63656; AKO63656; NGO_03985. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 77 DDE_Tnp_IS1595. FT {ECO:0000259|Pfam:PF12762}. SQ SEQUENCE 94 AA; 10832 MW; 4E18E6187C4E3444 CRC64; MPDGIVYADS PGSRGKLDAG GFTRCRINRS KEFADRRNHI NGIGNFWNQA KRALRKYNGI DRKPFPPLLR ECEFRLNFGT PPRQLKILRD RCGI // ID A0A0H4IWF0_NEIG1 Unreviewed; 113 AA. AC A0A0H4IWF0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Glyoxalase I {ECO:0000313|EMBL:AKO63758.1}; DE EC=4.4.1.5 {ECO:0000313|EMBL:AKO63758.1}; GN ORFNames=NGO_08805 {ECO:0000313|EMBL:AKO63758.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63758.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63758.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63758; AKO63758; NGO_08805. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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 Pfam; PF00903; Glyoxalase; 1. DR SUPFAM; SSF54593; SSF54593; 1. DR TIGRFAMs; TIGR00068; glyox_I; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lyase {ECO:0000313|EMBL:AKO63758.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 98 Glyoxalase. {ECO:0000259|Pfam:PF00903}. SQ SEQUENCE 113 AA; 12666 MW; D1C0726778437097 CRC64; MKLLRRKDYP EGRFTLAFVG YGDETDSTVL ELTHNWDTKR YDLGDAYGHI AVEVDDAYEA CERVKRQGGN VVREAGLMKH GTTVIAFVED PDGCKIEFVQ KKSGDDSVAY ANT // ID Q5F603_NEIG1 Unreviewed; 415 AA. AC Q5F603; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. 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 ORFNames=NGO_1763 {ECO:0000313|EMBL:AAW90384.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90384.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90384.1; -; Genomic_DNA. DR RefSeq; WP_003689969.1; NC_002946.2. DR RefSeq; YP_208796.1; NC_002946.2. DR ProteinModelPortal; Q5F603; -. DR SMR; Q5F603; 3-413. DR EnsemblBacteria; AAW90384; AAW90384; NGO_1763. DR GeneID; 3281094; -. DR KEGG; ngo:NGO1763; -. DR PATRIC; 20337140; VBINeiGon24812_2110. DR HOGENOM; HOG000060165; -. DR KO; K09458; -. DR OMA; METFEQQ; -. DR OrthoDB; EOG6DG2SR; -. DR BioCyc; NGON242231:GI2G-1659-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000535; 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:AAW90384.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR000447, KW ECO:0000313|EMBL:AAW90384.1}. FT ACT_SITE 165 165 {ECO:0000256|PIRSR:PIRSR000447-1}. SQ SEQUENCE 415 AA; 43042 MW; 491D3AA2989CBA1E CRC64; MSQRRVVITG LGQVSPVGNT AAEAWDNLLA GKSGIGAITR FDASDINSRV AGEVRGFDIG QYISAKEARR MDVFIHYGIA AALQAIADSG LDDVENLDKD RIGVNIGSGI GGLPSIEATG KAVIEGGARK INPFFIPGSL INLISGHVTI LKGYRGPSYG MVSACTTGAH AIGDSARLIK YGDADIMVAG GAEGAISTLG VGGFAAMKAL STRNDDPATA SRPWDKGRDG FVIGEGAGIL VLEELEHAKK RGAKIYAEIV GFGMSSDAYH ITAPNEEGPA LAVTRALKDA GINPEDVDYV NAHGTSTPLG DANETKALKR AFGEHACKTV ISSTKSMTGH LLGAAGGVEA VYSILAIHDG KIPPTINIFE QDVEAGCDLD YCANEARDAE IDVAISNSFG FGGTNGTLVF KRFKG // ID Q5FAF8_NEIG1 Unreviewed; 624 AA. AC Q5FAF8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AAW88829.1}; GN ORFNames=NGO_0065 {ECO:0000313|EMBL:AAW88829.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88829.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88829.1; -; Genomic_DNA. DR RefSeq; WP_003687310.1; NC_002946.2. DR RefSeq; YP_207241.1; NC_002946.2. DR EnsemblBacteria; AAW88829; AAW88829; NGO_0065. DR GeneID; 3282317; -. DR KEGG; ngo:NGO0065; -. DR PATRIC; 20332982; VBINeiGon24812_0075. DR HOGENOM; HOG000218768; -. DR OMA; LFSYHCI; -. DR OrthoDB; EOG6HB9KQ; -. DR BioCyc; NGON242231:GI2G-58-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88829.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 55 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 101 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 224 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 269 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 281 299 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 336 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 370 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 9 331 Acyl_transf_3. FT {ECO:0000259|Pfam:PF01757}. SQ SEQUENCE 624 AA; 70751 MW; C068EE3ABC861F30 CRC64; MSQALPYRPD IDTLRAAAVL SVIVFHIEKD WLPGGFLGVD IFFVISGFLM TAILLREMSG GRFFLKTFYI RRIKRILPAF FAVLAATLAG GFFLFTKDDF FLLWKSALTA LGFASNLYFA RGKDYFDPAQ EEKPLLHIWS LSVEEQFYFV FPILLLLVAR KSLRVQFGFL AALCALSLAA SFMPSALDKY YLPHLRACEM LVGSLTAVRM RYRQQRNPAV GKRYAAVGAL FSACILSACL FAYSEQTAYF PGPAALIPCL AVAALIYFNH YEHPLKKFFQ WKITVAAGLI SYSLYLWHWP ILAFMRYIGP DNLPPYSPAA AIVLTLAFSL ISYHCIEKPF KKWKGSFAQS VLWIYALPML VLGAGSFFAM RLPFMAQYDR LGLTRSNTSC HNNTGKQCLW GDTEKQPELL VLGDSHADHY KTFFDAVGKK EKWSATMVSA DACAYVEGYA SRVFQNWAAC RAVYRYAEEH LPRYPKVVLA MRWGSQMPEN SRSLAYDAGF FQKFDRMLHK LSSEKQAVYL MADNLASSYN VQRAYILSSR IPGCRQTLRP DDESTLKANA RIRELAAKYP NVYIIDAAAY IPADFQIGGL PVYSDKDHIN PYGGTELAKR FSEKQRFLDT RHNH // ID Q5F8Q3_NEIG1 Unreviewed; 611 AA. AC Q5F8Q3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 66. DE SubName: Full=Phosphogluconate dehydratase {ECO:0000313|EMBL:AAW89434.1}; GN ORFNames=NGO_0714 {ECO:0000313|EMBL:AAW89434.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89434.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89434.1; -; Genomic_DNA. DR RefSeq; WP_003691226.1; NC_002946.2. DR RefSeq; YP_207846.1; NC_002946.2. DR ProteinModelPortal; Q5F8Q3; -. DR SMR; Q5F8Q3; 6-607. DR EnsemblBacteria; AAW89434; AAW89434; NGO_0714. DR GeneID; 3282884; -. DR KEGG; ngo:NGO0714; -. DR PATRIC; 20334554; VBINeiGon24812_0849. DR HOGENOM; HOG000173157; -. DR KO; K01690; -. DR OMA; KVDVRQK; -. DR OrthoDB; EOG61ZTBF; -. DR BioCyc; NGON242231:GI2G-674-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004456; F:phosphogluconate dehydratase activity; IEA:InterPro. 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:UP000000535}; KW Lyase {ECO:0000256|SAAS:SAAS00427188}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 611 AA; 66239 MW; C397C3FA9AA98A7E CRC64; MNHTPIHPKL AEITGRIIER SRPTREKYLA KIRSAKQMGR LERNQLGCSN LAHGYAAMPK SIKIEMLQET VPNLGIITAY NDMVSAHQPF KDFPDQIKDE AQKNGATAQV AGGTPAMCDG ITQGYAGMEL SLFSRDVIAM STAVGLSHQM FDGSLFMGVC DKIVPGLMIG ALSFGHIPGI FVPAGPMSSG IGNKEKARTR QLFAEGKVGR DELLKSEMGS YHSPGTCTFY GTANSNQMMM EMMGVHLPAA AFVHPYTDLR EALTRYAAGH LARGIKNGTI KPLGEMLTEK SFINALIGLM ATGGSTNHTM HLVAMARAAG VILNWDDFDE ISSIIPLLIR VYPNGKADVN HFTAAGGLPF VIRELLDAGL LHDDVDTVVG HGMRHYTKEP FLIDGKLEWR EAPETSGNDD ILRKADNPFS PDGGLRLMKG NIGRGVVKVS AVREGCRIIE APAIVFNDQR EVLAAFERGE LERDFICVVR YQGPRANGMP ELHKLTPPLG ILQDRGFKVA LLTDGRMSGA SGKVPASIHM TPEALMGGNI AKIRTGDLIR FDSVTGELNV LINEAEWNVR EVERIDLGAN QQGCGRELFA GFRSMTSSAE TGAMSFGGEF A // ID A0A0H4ISI6_NEIG1 Unreviewed; 75 AA. AC A0A0H4ISI6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AKO63589.1}; GN ORFNames=NGO_00395 {ECO:0000313|EMBL:AKO63589.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63589.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63589.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63589; AKO63589; NGO_00395. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Receptor {ECO:0000313|EMBL:AKO63589.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 75 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206645. SQ SEQUENCE 75 AA; 7890 MW; 8E37438CB70C9835 CRC64; MGQFMSVFRI NMTAATVLAA LSSPVFAAQT ADLETVHIKG QRSYNAIATE KNGDYSSLKA AIWMTASIPA SPPAA // ID Q5F7C9_NEIG1 Unreviewed; 111 AA. AC Q5F7C9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE RecName: Full=Alkyl hydroperoxide reductase AhpD {ECO:0000256|SAAS:SAAS00088523}; DE EC=1.11.1.15 {ECO:0000256|SAAS:SAAS00088503}; GN ORFNames=NGO_1249 {ECO:0000313|EMBL:AAW89908.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89908.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89908.1; -; Genomic_DNA. DR RefSeq; WP_003699221.1; NC_002946.2. DR RefSeq; YP_208320.1; NC_002946.2. DR ProteinModelPortal; Q5F7C9; -. DR EnsemblBacteria; AAW89908; AAW89908; NGO_1249. DR GeneID; 3282483; -. DR KEGG; ngo:NGO1249; -. DR PATRIC; 20335829; VBINeiGon24812_1469. DR HOGENOM; HOG000252431; -. DR OMA; QWCIALH; -. DR BioCyc; NGON242231:GI2G-1166-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. FT DOMAIN 24 106 CMD. {ECO:0000259|Pfam:PF02627}. SQ SEQUENCE 111 AA; 11485 MW; FC78ED7BDB2371B7 CRC64; MFKDWKEHTA LVKKSFGELG KAHPKILQAY GALEQAAAAE ALDAKTRELI AIAVAITTRC ESCISVHAAA AAKAGATDSE IAGALATAIA LNAGAAYTYA LRALEAVETQ K // ID A0A0H4ISM8_NEIG1 Unreviewed; 246 AA. AC A0A0H4ISM8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Sugar transporter {ECO:0000313|EMBL:AKO63624.1}; GN ORFNames=NGO_02825 {ECO:0000313|EMBL:AKO63624.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63624.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63624.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63624; AKO63624; NGO_02825. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sugar transport {ECO:0000313|EMBL:AKO63624.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000313|EMBL:AKO63624.1}. FT TRANSMEM 30 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 213 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 246 AA; 25622 MW; 2CE1FAAFFF2F3DC8 CRC64; MGIVLTHAVF WSITASLAVR IAPVGKGNQA LGLLSTGTVM AMVAGIPLGR MVGQYLGWQA SFLLIGLCSA AVMAVLAKSL PRLPSVNTGS LSSLPLLLKR KKLMLLYAVT VPVITAHFTA YSYIEPFVIQ IGGFSARQVT VVPGLYGLAG FAASYLFGKW FAKHPRAFLA GAVSLIALSS GLLLPLAHFP AAIYALVFVW GTAIVVVSLG MVAKVLDFAS DAADLANSIY SELYNVGIGG GALLGH // ID Q5F5W9_NEIG1 Unreviewed; 446 AA. AC Q5F5W9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031}; GN ORFNames=NGO_1800 {ECO:0000313|EMBL:AAW90418.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90418.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU362031}; CC -!- SIMILARITY: Belongs to the peptidase M50B family. CC {ECO:0000256|RuleBase:RU362031, ECO:0000256|SAAS:SAAS00563376}. CC -!- SIMILARITY: Contains 2 PDZ (DHR) domains. CC {ECO:0000256|RuleBase:RU362031}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90418.1; -; Genomic_DNA. DR RefSeq; WP_003690033.1; NC_002946.2. DR RefSeq; YP_208830.1; NC_002946.2. DR ProteinModelPortal; Q5F5W9; -. DR EnsemblBacteria; AAW90418; AAW90418; NGO_1800. DR GeneID; 3282359; -. DR KEGG; ngo:NGO1800; -. DR PATRIC; 20337250; VBINeiGon24812_2160. DR HOGENOM; HOG000006281; -. DR KO; K11749; -. DR OMA; YVKMYGE; -. DR OrthoDB; EOG66F07W; -. DR BioCyc; NGON242231:GI2G-1698-MONOMER; -. DR Proteomes; UP000000535; 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: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. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00462286}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069945, ECO:0000313|EMBL:AAW90418.1}; KW Membrane {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069864, ECO:0000256|SAAS:SAAS00462286}; KW Metal-binding {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00451012}; KW Metalloprotease {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069945, ECO:0000313|EMBL:AAW90418.1}; KW Protease {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069945, ECO:0000313|EMBL:AAW90418.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069864}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362031, KW ECO:0000256|SAAS:SAAS00069864}; KW Zinc {ECO:0000256|RuleBase:RU362031, ECO:0000256|SAAS:SAAS00450985}. FT TRANSMEM 93 113 Helical. {ECO:0000256|RuleBase:RU362031}. FT TRANSMEM 373 394 Helical. {ECO:0000256|RuleBase:RU362031}. FT TRANSMEM 420 438 Helical. {ECO:0000256|RuleBase:RU362031}. FT DOMAIN 111 181 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 446 AA; 48118 MW; 75DA23C309266E47 CRC64; MQTLLAFIFA ILILVSLHEF GHYIVARLCG VKVVRFSVGF GKPFFTRKRG DTEWCLAPIP LGGYVKMVDT REGEVSEADL PYAFDKQHPA KRIAIVAAGP LTNLALAVLL YGLSFSFGVT ELRPYVGTVE PDTIAARTGF QSGDKIQSVN GVSVQDWSSA QTEIVLNLEA GKVAVGVQTA SGAQTVRTID AAGTPEAGKI AKNQGYIGLM PFKITTVAGG VEKGSPAEKA GLKPGDRLTA ADGKPIASWQ EWANLTRQSP GKKITLTYER AGQTHTADIR PDTVEQPDHT LIGRVGLRPQ PDRAWDAQIR RSYRPSVVRA FGMGWEKTVS HSWTTLKFFG KLISGNASVS HISGPLTIAD IAGQSAELGL QSYLEFLALV SISLGVLNLL PVPVLDGGHL VFYTVEWIRG KPLGERVQNI GLRFGLALMM LMMAAAFFND VTRLIG // ID Q5FAB4_NEIG1 Unreviewed; 497 AA. AC Q5FAB4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 65. DE SubName: Full=Ribonuclease G {ECO:0000313|EMBL:AAW88873.1}; GN ORFNames=NGO_0113 {ECO:0000313|EMBL:AAW88873.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88873.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88873.1; -; Genomic_DNA. DR RefSeq; WP_003704899.1; NC_002946.2. DR RefSeq; YP_207285.1; NC_002946.2. DR ProteinModelPortal; Q5FAB4; -. DR EnsemblBacteria; AAW88873; AAW88873; NGO_0113. DR GeneID; 3282417; -. DR KEGG; ngo:NGO0113; -. DR PATRIC; 20333127; VBINeiGon24812_0147. DR HOGENOM; HOG000258025; -. DR KO; K08301; -. DR OMA; WHPRIAG; -. DR OrthoDB; EOG6PCPTH; -. DR BioCyc; NGON242231:GI2G-102-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 52 128 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 497 AA; 56593 MW; C0B968E8B01F7B19 CRC64; MLSGLPIPKD IARPPETILV NITPQETRVA VLEENNICEL HIERNSGHSL VGNIYLGVVR RVLPGMQSAF IDIGLERAAF LHIVDVLEQR RNPEETQRIE HMLFEGQSVL VQVIKDPINT KGARLSTQIS LAGRFLVHLP QEDHIGVSQR IEDDAERSSL RERLDKLLPE NACRGYIIRT NAENATDEQL QSDIDYLTKV WEHIQEQAKI RPPETLLYQD LPLSLRVLRD MVGCDTQKIL VDSTVNHGRM TRFAEQYVHG ALGRIELFKG ERPLFETHNI EQEISRALQP RVNLNFGSYL IIESTEAMTT IDVNTGGFVG ARNFDETIFR TNLEACHTIA RELRLRNLGG IIIIDFIDMA QESHREAVLQ ELAKALAFDR TRVTLHDFTS LGLVELTRKR SRENLNQVLC EPCPSCQGRG RLKTPQTVCY EIQREIVREA RRYDAESFRI LAAPNVIDLF LDEESQSLAM LIDFIGKPIS LAVETAYTQE QYDIVLM // ID Q5F9S1_NEIG1 Unreviewed; 539 AA. AC Q5F9S1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|SAAS:SAAS00035571}; GN ORFNames=NGO_0319 {ECO:0000313|EMBL:AAW89066.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89066.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89066.1; -; Genomic_DNA. DR RefSeq; WP_003687708.1; NC_002946.2. DR RefSeq; YP_207478.1; NC_002946.2. DR ProteinModelPortal; Q5F9S1; -. DR EnsemblBacteria; AAW89066; AAW89066; NGO_0319. DR GeneID; 3281723; -. DR KEGG; ngo:NGO0319; -. DR PATRIC; 20333625; VBINeiGon24812_0390. DR HOGENOM; HOG000218856; -. DR OMA; HPSCGLY; -. DR OrthoDB; EOG61P6QH; -. DR BioCyc; NGON242231:GI2G-301-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; KW S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00433924}; KW Transferase {ECO:0000256|SAAS:SAAS00433928}; KW tRNA processing {ECO:0000256|SAAS:SAAS00433926}. FT DOMAIN 131 503 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 539 AA; 59455 MW; F70AD3EE82E3E8FC CRC64; MDNLVWDGIP DIRTLDQTIR KHAHPLNLIV CLPDNQIPDF QTAQDASDSE CRLKHRLDQA TQCLQFDSIN LIEHILPDVR FWLVPPSRTR RLHEHFHHIS WQTEAIPQTE SKSDKPWFAL PQTSERKKPE HVLVIGAGIA GASTAHALAS HGISVTVLEA RKAAQAASGN RQGLLYAKIS PHDTGQTELL LAGYGYTKRL LGHILPDSDT WGGNGIIHLN YSRTEQQRNH ELGLQKHHNH LYRSITSAEA EKIAGIPLNT PYAEPLCGLY WQHGVWLNPP AFVRTLLSHP LIELYENTTL TGISHDGEKW IASTPNGTFT ATHIIYCTGA HSPCLPETNL AALPLRQIRG QTGLTPSTPF SEQLRCAVSG ESYISPSWHG LHCYGASFIP NSSNTGWNEA EEASNRQALA HLNPALAESL FAANPNPQKH QGHAAIRCDS PDHLPVVGAL GDIAAMRQTY AKLALDKNYR IDTTCPYLPN AYTNTAHGTR GLATAPICAA AVAAEILGLP HLFSQRLRHA LHPNRTVIRA IVRRQNLIP // ID A0A0H4IWG5_NEIG1 Unreviewed; 65 AA. AC A0A0H4IWG5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63773.1}; GN ORFNames=NGO_09430 {ECO:0000313|EMBL:AKO63773.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63773.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63773.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63773; AKO63773; NGO_09430. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7883 MW; 0B4407559AA1E9E5 CRC64; MITVFCLIRL KMPVFRLNQI IFAETLKNLP YLPDRHQDFV VVTEKNILKV RIPNQSLKYR NHIRF // ID Q5F5I8_NEIG1 Unreviewed; 311 AA. AC Q5F5I8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Electron transfer flavoprotein subunit beta {ECO:0000313|EMBL:AAW90549.1}; GN ORFNames=NGO_1936 {ECO:0000313|EMBL:AAW90549.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90549.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90549.1; -; Genomic_DNA. DR RefSeq; WP_003688098.1; NC_002946.2. DR RefSeq; YP_208961.1; NC_002946.2. DR ProteinModelPortal; Q5F5I8; -. DR SMR; Q5F5I8; 2-309. DR EnsemblBacteria; AAW90549; AAW90549; NGO_1936. DR GeneID; 3282683; -. DR KEGG; ngo:NGO1936; -. DR PATRIC; 20337612; VBINeiGon24812_2333. DR HOGENOM; HOG000247865; -. DR KO; K03522; -. DR OMA; QIGSDVH; -. DR OrthoDB; EOG6M6JV6; -. DR BioCyc; NGON242231:GI2G-1839-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 181 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 311 AA; 32592 MW; 1BF25D807613AAD3 CRC64; MSVLIIAEHD NKQLNPATLH AVAAAAKLGK VDLLVVGNGA SSVVEFAKQV AGVEKVLVAD AAHYAEGLAE ELAPLVVKLA ADYRYVAATA TTFGKNLLPR VAALLDVPQI SDLTEIVDNT TFVRPIYAGN AFETVQADSE KLVLTFRVTA FDAVAAQGGN AEVINVKTTP AQNLSRFVNR QLSHSDRPEL TQAKVIVSGG RALGSVEKFS EVLTPLADVL GAAIGASRAA VDAEYAPNDA QVGQTGKVVA PQLYFAIGIS GAIQHVAGMQ DSKVIVAINK DADAPIFNVA DYGLVGDLFE IVPQLIELLK N // ID Q5F5B7_NEIG1 Unreviewed; 222 AA. AC Q5F5B7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. DE SubName: Full=Amino acid ABC transporter permease {ECO:0000313|EMBL:AAW90620.1}; GN ORFNames=NGO_2012 {ECO:0000313|EMBL:AAW90620.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90620.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90620.1; -; Genomic_DNA. DR RefSeq; WP_003692001.1; NC_002946.2. DR RefSeq; YP_209032.1; NC_002946.2. DR ProteinModelPortal; Q5F5B7; -. DR EnsemblBacteria; AAW90620; AAW90620; NGO_2012. DR GeneID; 3282700; -. DR KEGG; ngo:NGO2012; -. DR PATRIC; 20337805; VBINeiGon24812_2426. DR HOGENOM; HOG000267552; -. DR KO; K02029; -. DR OMA; LECIRII; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NGON242231:GI2G-1913-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00450258, ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 20 45 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 57 78 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 84 102 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 192 214 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 19 213 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 222 AA; 25010 MW; C14149A638AD8F60 CRC64; MAFEWLFEGK NAARLGEGLL LTAQISLISV AASCVLGTLF GLVLRSRNRL VRFVGRFYLE TIRIVPILVW LFGLYFGLSV WTGIHIGGFW VCVWVFSLWG VAEMGDLVRG ALESIEKHQV ESGLAPGLSR GQVFRCIELP QSIRRVLPGA VNLFTRMIKT SSLAWLIGVI EVVKVGQQII ENSLLTQPNA SFWVYGLIFM LYFFCCWPLS LLAAKLEQKW EH // ID Q5F793_NEIG1 Unreviewed; 472 AA. AC Q5F793; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 59. DE SubName: Full=Alanine glycine permease {ECO:0000313|EMBL:AAW89944.1}; GN ORFNames=NGO_1290 {ECO:0000313|EMBL:AAW89944.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89944.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89944.1; -; Genomic_DNA. DR RefSeq; WP_010951233.1; NC_002946.2. DR RefSeq; YP_208356.1; NC_002946.2. DR EnsemblBacteria; AAW89944; AAW89944; NGO_1290. DR GeneID; 3282100; -. DR KEGG; ngo:NGO1290; -. DR PATRIC; 20335923; VBINeiGon24812_1516. DR HOGENOM; HOG000255106; -. DR KO; K03310; -. DR OMA; WMWLSAV; -. DR OrthoDB; EOG6D2KVD; -. DR BioCyc; NGON242231:GI2G-1202-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363064}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 15 36 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 311 332 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; 50634 MW; 487B2AC7EEF4E31A CRC64; MENILSVLVG TVNRFLWGYL LIYALLGIGL FFTLYLGAPQ ITKLGAGFKS VFGGLFAKGD KDDKSLSQFQ ALAVAISAQI GTGNVAGVAT AITAGGPGAI FWMWLSAVLG MSTIFAEALL AQKYRVVSHG KYIGGPAFYI THGLTPKIGR GAARFLSGFF SIALIVALGF IGNATQANSI ASAVTIAFDV PSLAVGIVFA VLAGMVVIGG VNRIANIARF VVPFMAVVYI LCAVVILFEF SDHIVPMFNH IFTAAFNPEA VLGGAAGIGM REAIRFGVAR GLFSNEAGMG STPHAHATAD VKHPVQQGMT AFVGVFIDTI LVCTATALII LLTDANLSGE QGAAVTQFAF NKAFPGFGSQ LLAMCLTFFA FTTIIGWYYF GESNIRFLFR GRHLGIYRAL VLLAIVLGTL GKVDLVWSLS DMFNGFMVIP NLIALFLLRK EIRAIYDDYL MQKKAGQDLS YQYEFHEFHD KQ // ID A0A0H4IS62_NEIG1 Unreviewed; 60 AA. AC A0A0H4IS62; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63751.1}; GN ORFNames=NGO_08380 {ECO:0000313|EMBL:AKO63751.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63751.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63751.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63751; AKO63751; NGO_08380. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 60 AA; 6901 MW; 25FDF0F8A84FB9E3 CRC64; MECAGLCLMH NLFCRDMLFG ILVSERSDTK VMICRRLFLK TLILGSKMPS EKAFQTAFVR // ID A0A0H4ITA5_NEIG1 Unreviewed; 160 AA. AC A0A0H4ITA5; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Fimbrial protein {ECO:0000313|EMBL:AKO63804.1}; GN ORFNames=NGO_10995 {ECO:0000313|EMBL:AKO63804.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63804.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63804.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63804; AKO63804; NGO_10995. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 160 AA; 16958 MW; 6F0963E389A2C772 CRC64; MASASDIKGK YVESVTVEKG VVTAKMLSSG VNKEIQGKKL SLWAKREAGS VKWFCGQPVK RNDAANDDVT DDAGTDNGGK GKIDTKHLPS TCRDKSTAVC TKHHAPISNT SKKSAVAGYY PNHGKWPEDN TSAGVASPPP TSKANMFKAL RSQTASLPPK // ID A0A0H4IVE8_NEIG1 Unreviewed; 90 AA. AC A0A0H4IVE8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63715.1}; GN ORFNames=NGO_07320 {ECO:0000313|EMBL:AKO63715.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63715.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63715.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63715; AKO63715; NGO_07320. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 90 AA; 10333 MW; 4D66FF3D5FDE3B93 CRC64; MQWKFEDPQN TAVITTRRIL SKKNGILEVW HDADDGMWQF LDGNEIHEGD AVIVSLKEIV TIDSSVNLLS NLPLGGYAWR NTISEKWNFD // ID A0A0H4IS08_NEIG1 Unreviewed; 221 AA. AC A0A0H4IS08; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=3-ketoacyl-ACP reductase {ECO:0000313|EMBL:AKO63711.1}; DE EC=1.1.1.100 {ECO:0000313|EMBL:AKO63711.1}; GN Name=fabG {ECO:0000313|EMBL:AKO63711.1}; GN ORFNames=NGO_07125 {ECO:0000313|EMBL:AKO63711.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63711.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63711.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63711; AKO63711; NGO_07125. DR Proteomes; UP000000535; 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 PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01831; fabG_rel; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AKO63711.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 221 AA; 23882 MW; C4A6FCF41064DF12 CRC64; MADDGFDIAV HCRSRRDEAE AVAEEIRALG RNARVLQFDV SDREACREIL TADIEANGAY YGVVLNAGLT RDNAFPAFSD DDWDVVPRTN LDGFYNVLHP LVMPMIRRRK AGRIVCMASV SGLTGNRGQV NYSASKAGII GAAKALAVEL AKRKITVNCV APGLMDTDII DENVPVGEIL KAVPAARMGL PEEVAHAVHF LMDEKAAYIT RQVIAVNGGL C // ID Q5F9D7_NEIG1 Unreviewed; 398 AA. AC Q5F9D7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Integrase {ECO:0000313|EMBL:AAW89200.1}; GN ORFNames=NGO_0462 {ECO:0000313|EMBL:AAW89200.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89200.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000256|SAAS:SAAS00541913}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89200.1; -; Genomic_DNA. DR RefSeq; WP_010951050.1; NC_002946.2. DR RefSeq; YP_207612.1; NC_002946.2. DR ProteinModelPortal; Q5F9D7; -. DR DNASU; 3282983; -. DR EnsemblBacteria; AAW89200; AAW89200; NGO_0462. DR GeneID; 3282983; -. DR KEGG; ngo:NGO0462; -. DR PATRIC; 20333962; VBINeiGon24812_0553. DR HOGENOM; HOG000263105; -. DR OMA; DHAKDIW; -. DR OrthoDB; EOG6X3W2Z; -. DR BioCyc; NGON242231:GI2G-440-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.150.130; -; 1. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR025166; DUF4102. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR023109; Integrase_recombinase_N. DR Pfam; PF13356; DUF4102; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 91 DUF4102. {ECO:0000259|Pfam:PF13356}. FT DOMAIN 205 372 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. SQ SEQUENCE 398 AA; 45877 MW; 8545F94545B5FCDB CRC64; MAKIITPLSA NQVKNAKPGD KLYKLSDGGG LALWVYPTGR RSWKLSFMQD GRQQTISLGR YPDFSLAEAR EWREEVRRKR AHGENVVNKK VRADFAFEKV ARDWFVRWSK GRSEKYAGQV MRNFERWVFP AIGNLDIRQV RTADVVGCLR VMEARGIVDT LRKTKNSLKM VFAFAVGSGM MEINPVAQIG SGVFERVKTK NMTALSPSEL PRLIDFLEQR NEFAVYAGRV HIHPVTRFCI YWLLLTMTRI REAALMEWSE LDGEVWRIPA ERKKERRGHD VPLSRAMRWV LDQARGLNVN GRFVFESVNF QGHINKESPH VAMRRSGLDT TAHGLRSLAR TYLREVLKVY NDVAEKLLAH SLGTRTQTAY NRSELWEERK DAPERWGNDV LRLADNGK // ID A0A0H4IW29_NEIG1 Unreviewed; 45 AA. AC A0A0H4IW29; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AKO63638.1}; GN ORFNames=NGO_03690 {ECO:0000313|EMBL:AKO63638.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63638.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63638.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63638; AKO63638; NGO_03690. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 5042 MW; 01FB14ED20B043DA CRC64; MKPVKLKMPS ESLSDGILFG LENTYAVLSP KERIQKTKAT GIHRK // ID Q5F7N0_NEIG1 Unreviewed; 507 AA. AC Q5F7N0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=TspB {ECO:0000313|EMBL:AAW89807.1}; GN ORFNames=NGO_1140 {ECO:0000313|EMBL:AAW89807.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89807.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89807.1; -; Genomic_DNA. DR RefSeq; WP_010951201.1; NC_002946.2. DR RefSeq; YP_208219.1; NC_002946.2. DR RefSeq; YP_208336.1; NC_002946.2. DR EnsemblBacteria; AAW89807; AAW89807; NGO_1140. DR GeneID; 3282070; -. DR GeneID; 3282213; -. DR KEGG; ngo:NGO1140; -. DR KEGG; ngo:NGO1265; -. DR PATRIC; 20335540; VBINeiGon24812_1335. DR HOGENOM; HOG000218809; -. DR OrthoDB; EOG62NX16; -. DR BioCyc; NGON242231:GI2G-1053-MONOMER; -. DR BioCyc; NGON242231:GI2G-1182-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 484 504 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 507 AA; 56038 MW; EC03DBC617309E3A CRC64; MMYSFEANAN AVKISETLSV DTGQGAKVHK FVPKSSNIYS SDLTKAVDLT HIPTGAKARI NAKITASVSR AGVLSGVGKL VRQGAKFGTR AVPYVGTALL AHDVYETFKE DIQARGCRYD PETDKFVKGY EYANCLWYED ERRINRTYGC YGVDSSIMRL MPDRSRFPEV KQLMESQMYR LARPFWNWRK EELNKLSSLD WNNFVLNRCT FDWNGGGCAV NKGDDFRAGA SFSLGRNPKY KEEMDAKKPE EILSLKVDAD PDKYIEATGY PGYSEKVEVA PGTKVNMGPV TDRNGNPVQV AATFGRDAQG NTTADVQVIP RPDLTPASAE APHAQPLPEV SPAENPANNP DPDENPGTRP NPEPDPDLNP DANPDTDGQP GTSPDSPAVP DRPNGRHRKE RKEGEDGGLS CDYFPEILAC QEMGKPSDRM FHDISIPQVT DDKTWSSHNF LPSNGVCPQP KTFHVFGRQY RASYEPLCVF AEKIRFAVLL AFIIMSAFVV FGSLGGE // ID Q5F5Q7_NEIG1 Unreviewed; 83 AA. AC Q5F5Q7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAW90480.1}; GN ORFNames=NGO_1859 {ECO:0000313|EMBL:AAW90480.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90480.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90480.1; -; Genomic_DNA. DR RefSeq; WP_002215364.1; NC_002946.2. DR RefSeq; YP_208892.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q7; -. DR SMR; Q5F5Q7; 2-79. DR EnsemblBacteria; AAW90480; AAW90480; NGO_1859. DR GeneID; 3282322; -. DR KEGG; ngo:NGO1859; -. DR PATRIC; 20337406; VBINeiGon24812_2234. DR HOGENOM; HOG000044615; -. DR OMA; CPVECII; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; NGON242231:GI2G-1764-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. 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 A0A0H4IRN9_NEIG1 Unreviewed; 67 AA. AC A0A0H4IRN9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63621.1}; GN ORFNames=NGO_02290 {ECO:0000313|EMBL:AKO63621.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63621.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63621.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63621; AKO63621; NGO_02290. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7544 MW; 1C2032F097FC23C1 CRC64; MGGQYSSLEN FALSVLREKI INNTVSSDEK LLIINDFLSG FLEFDPETGE PVGETLKIEQ MIDFFLV // ID Q5FA56_NEIG1 Unreviewed; 468 AA. AC Q5FA56; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 84. DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:AAW88931.1}; GN ORFNames=NGO_0176 {ECO:0000313|EMBL:AAW88931.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88931.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88931.1; -; Genomic_DNA. DR RefSeq; WP_003687478.1; NC_002946.2. DR RefSeq; YP_207343.1; NC_002946.2. DR ProteinModelPortal; Q5FA56; -. DR EnsemblBacteria; AAW88931; AAW88931; NGO_0176. DR GeneID; 3281293; -. DR KEGG; ngo:NGO0176; -. DR PATRIC; 20333279; VBINeiGon24812_0222. DR HOGENOM; HOG000218823; -. DR KO; K02484; -. DR OMA; YANIDEM; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NGON242231:GI2G-161-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Kinase {ECO:0000256|RuleBase:RU003568, ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAW88931.1}; 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:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAW88931.1}; 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; 52980 MW; D10D79EC55B096F0 CRC64; MKLFQRIFAT FCAVIVCAIF VASFSFWLVQ NTLAENQFNQ RRTIETTLMG SIISAFKTRG DNGAREILTE WKNSPVSSAV YVIQGDEKKD ILNRYIDNYT IERARLFAAN NPHSNLVRIE YDRFGEEYLF FIKGWDNHQA QRLPSPLFIP GLPLAPIWHE FIILSFIIIV GLLMAYILAG NIAKPIRILG NGMDRVANGE LETRISQQVD DRDDELSHLA IQFDKMAEKL EKLVAKERYL LHHVSHEMRS PLARMQAIVG LIQAQPQKRE QYLKRLEGEL TRMDTLAGEL LTLSRLETSN MALEKESLKL LPFLGNLVED NQSIAQKNGQ TVALSADGKI PENTTILANE SYLYRAFDNV IRNAVNYSPE GSTILINIGQ DHKHWIIDVT DNGPGVDEMQ LPHIFTAFYR ADSSANKPGT GLGLALTQHI IEQHCGKIIA ENIKPNGLRM RFILPKKKTG FKTEKSAN // ID A0A0H4J5V3_NEIG1 Unreviewed; 34 AA. AC A0A0H4J5V3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63737.1}; GN ORFNames=NGO_08070 {ECO:0000313|EMBL:AKO63737.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63737.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63737.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63737; AKO63737; NGO_08070. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 34 AA; 3953 MW; 95381943218B2D07 CRC64; MKPIQMFFPF LNNPLVFFLS AVLPHNSERS AVFL // ID Q5F890_NEIG1 Unreviewed; 158 AA. AC Q5F890; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Transcription elongation factor GreA {ECO:0000256|HAMAP-Rule:MF_00105, ECO:0000256|SAAS:SAAS00018706}; DE AltName: Full=Transcript cleavage factor GreA {ECO:0000256|HAMAP-Rule:MF_00105}; GN Name=greA {ECO:0000256|HAMAP-Rule:MF_00105}; GN ORFNames=NGO_0899 {ECO:0000313|EMBL:AAW89597.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89597.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00105, CC ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS00338401}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000256|HAMAP- CC Rule:MF_00105, ECO:0000256|RuleBase:RU000556, CC ECO:0000256|SAAS:SAAS00541981}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89597.1; -; Genomic_DNA. DR RefSeq; WP_003688476.1; NC_002946.2. DR RefSeq; YP_208009.1; NC_002946.2. DR ProteinModelPortal; Q5F890; -. DR SMR; Q5F890; 2-137. DR EnsemblBacteria; AAW89597; AAW89597; NGO_0899. DR GeneID; 3281103; -. DR KEGG; ngo:NGO0899; -. DR PATRIC; 20334975; VBINeiGon24812_1057. DR HOGENOM; HOG000241145; -. DR KO; K03624; -. DR OMA; HNEGRIA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; NGON242231:GI2G-839-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00105, KW ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS00416876}; KW Elongation factor {ECO:0000313|EMBL:AAW89597.1}; KW Protein biosynthesis {ECO:0000313|EMBL:AAW89597.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00105, KW ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS00425054}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00105, KW ECO:0000256|RuleBase:RU000556, ECO:0000256|SAAS:SAAS00425054}. FT DOMAIN 4 74 GreA_GreB_N. {ECO:0000259|Pfam:PF03449}. FT DOMAIN 83 157 GreA_GreB. {ECO:0000259|Pfam:PF01272}. SQ SEQUENCE 158 AA; 17473 MW; FEF3ADD1D48810DF CRC64; MQKIPLTVRG AELLKQELQQ LKSVARPEVI EAIAEARSHG DLSENAEYEA AKERQGFIEG RISELEHKLS VAHIINPAEI HAEGKIVFGT TVTLEDLETE EHVTYQIVGE DEADIKQGKI YVGSPIARAL IGKEEGDTAE VQAPGGVREY DIIEVRYI // ID Q5F5K3_NEIG1 Unreviewed; 305 AA. AC Q5F5K3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE RecName: Full=Cell division protein FtsX {ECO:0000256|PIRNR:PIRNR003097}; GN ORFNames=NGO_1921 {ECO:0000313|EMBL:AAW90534.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90534.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90534.1; -; Genomic_DNA. DR RefSeq; WP_003688074.1; NC_002946.2. DR RefSeq; YP_208946.1; NC_002946.2. DR EnsemblBacteria; AAW90534; AAW90534; NGO_1921. DR GeneID; 3282849; -. DR KEGG; ngo:NGO1921; -. DR PATRIC; 20337578; VBINeiGon24812_2316. DR HOGENOM; HOG000270397; -. DR KO; K09811; -. DR OMA; ITIFARR; -. DR OrthoDB; EOG60W7WW; -. DR BioCyc; NGON242231:GI2G-1824-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90534.1}; KW Cell division {ECO:0000256|PIRNR:PIRNR003097, KW ECO:0000313|EMBL:AAW90534.1}; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR003097}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR003097}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|PIRNR:PIRNR003097, KW ECO:0000256|SAAS:SAAS00573714, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 34213 MW; 9C780DF78A410AEF CRC64; MSIIHYFSLH VESARSALKQ LLRQPFGTLL TLIMLAVAMT LPLFMYLGIQ SGQSVLGKLN ESPQITVYME TAAAQSDSDT VRSLLTRDKR LDNIRFIGKE DGLAELQSNL DQNLISMLDG NPLPDVFIVT PDPATTPAQM QAIYRDITKL PMVESASMDT EWVQTLYQIN EFIRKILWFL SLTLGMAFVL VAHNTIRLQI LSRKEEIEIT KLLGAPASFI RRPFLYQAMW QSIFSAAVSL GLCGWLLSAV RPLVDAIFKP YGLNIGWRFF YVGELGLVFG FVIALGVFGA WLATTQHLLC FKAKK // ID A0A0H4IVY1_NEIG1 Unreviewed; 122 AA. AC A0A0H4IVY1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63583.1}; GN ORFNames=NGO_00200 {ECO:0000313|EMBL:AKO63583.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63583.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63583.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63583; AKO63583; NGO_00200. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR002622; Transposase_14. DR Pfam; PF01710; HTH_Tnp_IS630; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 29 119 HTH_Tnp_IS630. FT {ECO:0000259|Pfam:PF01710}. SQ SEQUENCE 122 AA; 13712 MW; BCC10B6A3A8E7979 CRC64; MVPFEPGRGN AVPVFVNPLY YGQCKNTGQT AATFNLSRNT LYLRIRLKKQ TGSLKHQVTG LNAAKSDRQK PARYVGRHPD ACLHEIAKHF DCTAAAVCHA PKQMRMARKK RPPLTKDKTR PK // ID A0A0H4IV38_NEIG1 Unreviewed; 108 AA. AC A0A0H4IV38; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Phage baseplate assembly protein {ECO:0000313|EMBL:AKO63650.1}; GN ORFNames=NGO_03855 {ECO:0000313|EMBL:AKO63650.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63650.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63650.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63650; AKO63650; NGO_03855. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007048; GpW/Gp25/IraD. DR Pfam; PF04965; GPW_gp25; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 108 AA; 11896 MW; 469F9FCD05049085 CRC64; MTDAENGRGQ DTLAHIAQSI RNILFTRIGT RLMREEYGSF IPDLIDMPAG HAAIALIHQA AVTALARWKP RITVRRIQAD TADLAAGKIK LTLDVTLADG GERTYRIK // ID A0A0H4IV57_NEIG1 Unreviewed; 78 AA. AC A0A0H4IV57; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:AKO63665.1}; GN ORFNames=NGO_04725 {ECO:0000313|EMBL:AKO63665.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63665.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63665.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63665; AKO63665; NGO_04725. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63665.1}. SQ SEQUENCE 78 AA; 9521 MW; ACA8F1A347241BBC CRC64; MKLAIVPCRR QTRYVRNKSR KYAGKKILET KNLKKINFRH KKPNSRTLKP KMPNLRFSRR HLHQYNAGCF YLYIYVLP // ID Q5FA83_NEIG1 Unreviewed; 311 AA. AC Q5FA83; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Porphobilinogen deaminase {ECO:0000256|HAMAP-Rule:MF_00260}; DE Short=PBG {ECO:0000256|HAMAP-Rule:MF_00260}; DE EC=2.5.1.61 {ECO:0000256|HAMAP-Rule:MF_00260}; DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|HAMAP-Rule:MF_00260}; DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|HAMAP-Rule:MF_00260}; GN Name=hemC {ECO:0000256|HAMAP-Rule:MF_00260}; GN ORFNames=NGO_0146 {ECO:0000313|EMBL:AAW88904.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88904.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the CC hydroxymethylbilane pre-uroporphyrinogen in several discrete CC steps. {ECO:0000256|HAMAP-Rule:MF_00260, CC ECO:0000256|SAAS:SAAS00018414}. CC -!- CATALYTIC ACTIVITY: 4 porphobilinogen + H(2)O = CC hydroxymethylbilane + 4 NH(3). {ECO:0000256|HAMAP-Rule:MF_00260, CC ECO:0000256|SAAS:SAAS00018417}. CC -!- COFACTOR: CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00260}; CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000256|HAMAP- CC Rule:MF_00260}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 2/4. {ECO:0000256|HAMAP-Rule:MF_00260, CC ECO:0000256|SAAS:SAAS00018329}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00260}. CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the CC dipyrromethane group. {ECO:0000256|HAMAP-Rule:MF_00260}. CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000256|HAMAP- CC Rule:MF_00260, ECO:0000256|SAAS:SAAS00542451}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88904.1; -; Genomic_DNA. DR RefSeq; WP_003687436.1; NC_002946.2. DR RefSeq; YP_207316.1; NC_002946.2. DR ProteinModelPortal; Q5FA83; -. DR SMR; Q5FA83; 4-308. DR EnsemblBacteria; AAW88904; AAW88904; NGO_0146. DR GeneID; 3281294; -. DR KEGG; ngo:NGO0146; -. DR PATRIC; 20333205; VBINeiGon24812_0185. DR HOGENOM; HOG000228587; -. DR KO; K01749; -. DR OMA; GAICIES; -. DR OrthoDB; EOG6HB9Z6; -. DR BioCyc; NGON242231:GI2G-134-MONOMER; -. DR UniPathway; UPA00251; UER00319. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00260, KW ECO:0000256|SAAS:SAAS00425415}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00260, KW ECO:0000256|SAAS:SAAS00425344}. FT DOMAIN 6 212 Porphobil_deam. FT {ECO:0000259|Pfam:PF01379}. FT DOMAIN 226 295 Porphobil_deamC. FT {ECO:0000259|Pfam:PF03900}. FT MOD_RES 242 242 S-(dipyrrolylmethanemethyl)cysteine. FT {ECO:0000256|HAMAP-Rule:MF_00260}. SQ SEQUENCE 311 AA; 33614 MW; 41F304C09E2B9F3C CRC64; MNPKKLVIAS RESLLAMWQA KHIQGRLKAL YPDCEVEILG MTTRGDRILD RTLSKVGGKG LFVKELEQSL QDGRADLAVH SIKDVPMDLP EGFALAAISE RANPFDAFVS NRYARLEEMP EGAVVGTSSL RREAQLRARY PHLVIKPLRG NVQTRLSKLD NGEYDAIILA AAGLQRLELD ERIRMILSES DSLPAAGQGA LGIEIATHRE DLYEVLKPLN HDTTHACVTA ERALARALGG SCQVPLAAYC TEENGLLILR GLVGHPDGSI VLQADAQAPA GYADALGRAV AKKLADDGAQ ELIGAVLNTE N // ID Q5F552_NEIG1 Unreviewed; 227 AA. AC Q5F552; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 63. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90685.1}; GN ORFNames=NGO_2084 {ECO:0000313|EMBL:AAW90685.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90685.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90685.1; -; Genomic_DNA. DR RefSeq; WP_010951401.1; NC_002946.2. DR RefSeq; YP_209097.1; NC_002946.2. DR EnsemblBacteria; AAW90685; AAW90685; NGO_2084. DR GeneID; 3282833; -. DR KEGG; ngo:NGO2084; -. DR PATRIC; 20338001; VBINeiGon24812_2523. DR HOGENOM; HOG000060391; -. DR KO; K19416; -. DR OMA; NIFLAIP; -. DR OrthoDB; EOG6PZXBH; -. DR BioCyc; NGON242231:GI2G-1979-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 25 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 55 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 104 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 187 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 221 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 227 AA; 24432 MW; 6931B2213AB73BC8 CRC64; MQHDVYDYTA HTVSKNTVLQ KTYRLLGFSF IPAAAGAALA ANAGFNFYAA FGSRWIGFAV VLAFFYGMIH FIEKNRYSNT GVTLLMVFTF GMGVLIGPVL QYALHIADGA KIVGIAAAMT AAVFLTMSAL ARRTRLDMNA LGRFLTVGAV ILMVAVVANL FLGIPALALT ISAGFVLFSS LIIMWQVRTV IDGGEDSYIS AALTLFISLY NIFSSLLNIL LSLNGDD // ID A0A0H4IV00_NEIG1 Unreviewed; 74 AA. AC A0A0H4IV00; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63610.1}; GN ORFNames=NGO_01355 {ECO:0000313|EMBL:AKO63610.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63610.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0033 family. CC {ECO:0000256|SAAS:SAAS00585298}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AKO63610.1; -; Genomic_DNA. DR RefSeq; WP_003690730.1; NC_002946.2. DR RefSeq; YP_008914848.1; NC_002946.2. DR EnsemblBacteria; AKO63610; AKO63610; NGO_01355. DR GeneID; 19592991; -. DR KEGG; ngo:NGO0250a; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 30 UPF0033. {ECO:0000259|PROSITE:PS01148}. SQ SEQUENCE 74 AA; 7954 MW; FA34F54072FDF5F9 CRC64; MNSETLDVTG LKCPLPILRA KKALAQMRQG EVLTVLATDG GAPGDFEAFC RQTGHVLLDS SEQDGVFTLV VKHK // ID Q5FA07_NEIG1 Unreviewed; 81 AA. AC Q5FA07; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 46. DE SubName: Full=A nuclease of the HNH/endo VII superwith conserved WHH family protein {ECO:0000313|EMBL:AAW88980.1}; GN ORFNames=NGO_0227 {ECO:0000313|EMBL:AAW88980.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88980.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88980.1; -; Genomic_DNA. DR RefSeq; WP_002237787.1; NC_002946.2. DR RefSeq; YP_207392.1; NC_002946.2. DR EnsemblBacteria; AAW88980; AAW88980; NGO_0227. DR GeneID; 3281474; -. DR KEGG; ngo:NGO0227; -. DR PATRIC; 20333397; VBINeiGon24812_0280. DR HOGENOM; HOG000218829; -. DR OMA; IPNYTWH; -. DR OrthoDB; EOG63JR5W; -. DR BioCyc; NGON242231:GI2G-211-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 73 Colicin-DNase. FT {ECO:0000259|Pfam:PF12639}. SQ SEQUENCE 81 AA; 9046 MW; 693627367E9E38BA CRC64; MKDSTGQMRL ATKDLAEAIK RGEVRSSAFT TKQLKAIEKG KDKIPSYTWH HHQDTGRMQL VPEWEHSKTG HIGGTAMGKG K // ID Q5F7U2_NEIG1 Unreviewed; 148 AA. AC Q5F7U2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Acyl-CoA thioester hydrolase {ECO:0000313|EMBL:AAW89745.1}; GN ORFNames=NGO_1078 {ECO:0000313|EMBL:AAW89745.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89745.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89745.1; -; Genomic_DNA. DR RefSeq; WP_002230436.1; NC_002946.2. DR RefSeq; YP_208157.1; NC_002946.2. DR ProteinModelPortal; Q5F7U2; -. DR SMR; Q5F7U2; 7-145. DR EnsemblBacteria; AAW89745; AAW89745; NGO_1078. DR GeneID; 3281110; -. DR KEGG; ngo:NGO1078; -. DR PATRIC; 20335400; VBINeiGon24812_1266. DR HOGENOM; HOG000044841; -. DR KO; K10806; -. DR OMA; VNVEVWV; -. DR OrthoDB; EOG676Z6F; -. DR BioCyc; NGON242231:GI2G-990-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89745.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 11 127 HotDog ACOT-type. FT {ECO:0000259|PROSITE:PS51770}. SQ SEQUENCE 148 AA; 16336 MW; 69E9B40D4AF1F208 CRC64; MQHEEGNRQR PQGELLLRTV AMPRDTNPNQ DIFGGWIMSQ MDLGGGILAA EIARGRIVTV AVQEMNFIRP VKVGNVVCCY GHCVRVGNTS LQLKVEVWVK TLMNDCVTED RHLVTEAVFT YVAIDAEGNP RPIPKEGNPK LSGLLPTP // ID Q5F9Q4_NEIG1 Unreviewed; 283 AA. AC Q5F9Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00316707}; DE Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00316689}; GN Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197}; GN ORFNames=NGO_0338 {ECO:0000313|EMBL:AAW89083.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89083.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00351434}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00316693}. 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:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00316687}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, CC ECO:0000256|SAAS:SAAS00316708}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000256|HAMAP-Rule:MF_00197, ECO:0000256|SAAS:SAAS00583234}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89083.1; -; Genomic_DNA. DR RefSeq; WP_003687738.1; NC_002946.2. DR RefSeq; YP_207495.1; NC_002946.2. DR ProteinModelPortal; Q5F9Q4; -. DR SMR; Q5F9Q4; 4-281. DR EnsemblBacteria; AAW89083; AAW89083; NGO_0338. DR GeneID; 3281778; -. DR KEGG; ngo:NGO0338; -. DR PATRIC; 20333667; VBINeiGon24812_0411. DR HOGENOM; HOG000220466; -. DR KO; K01778; -. DR OMA; RFTKMQG; -. DR OrthoDB; EOG6ND0M5; -. DR BioCyc; NGON242231:GI2G-318-MONOMER; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429562}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429534}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429665}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00475366}; KW Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197, KW ECO:0000256|SAAS:SAAS00429562}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT REGION 11 12 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 76 78 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 215 216 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT REGION 225 226 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT ACT_SITE 76 76 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT ACT_SITE 224 224 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT BINDING 14 14 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT BINDING 47 47 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT BINDING 67 67 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT BINDING 164 164 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT BINDING 197 197 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00197}. FT SITE 166 166 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT SITE 215 215 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_00197}. FT DISULFID 76 224 {ECO:0000256|HAMAP-Rule:MF_00197}. SQ SEQUENCE 283 AA; 30425 MW; 7009DD6B211D7988 CRC64; MKTLKFTKMH GLGNDFMVID AVSQDFTPED VPIAAWADRF RGVGFDQLLV VGCSETEGVD FRYRIFNADG SEVGQCGNGA RCFARFVADK GLTDKKEICV ETAKGIIFPK LSDNGMVTVN MGKPKFMPSE IPFVPESGEG DDACIYGVHL ESGIQPVSCV NMGNPHAVIV VDDVECAPVR ETGSRIEPHR QFPERVNVGF MQVVGRTAIR LRVFERGVGE TQACGTGACA AVVAGIRLGL LDEGKTVEVV LPGGTLYIEW ACGGDVMMTG PAETVFEGEL AYS // ID A0A0H4J5U2_NEIG1 Unreviewed; 96 AA. AC A0A0H4J5U2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=C4-dicarboxylate ABC transporter {ECO:0000313|EMBL:AKO63722.1}; GN ORFNames=NGO_07465 {ECO:0000313|EMBL:AKO63722.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63722.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63722.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63722; AKO63722; NGO_07465. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 11113 MW; 2C99972D12A75190 CRC64; MQIYVKINLF FVFDRLFIKD IYLFVLNKII YQKEHIFPST AIRLPAAFRF GKLVYPDYLL YNQSENFFQK QTGSTVRLCP GGTKPVSLPR AAQGSA // ID A0A0H4J5T7_NEIG1 Unreviewed; 256 AA. AC A0A0H4J5T7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63717.1}; GN ORFNames=NGO_07400 {ECO:0000313|EMBL:AKO63717.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63717.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63717.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63717; AKO63717; NGO_07400. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.160.20.10; -; 1. DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom. 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; 5. DR SUPFAM; SSF51126; SSF51126; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 256 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206336. FT DOMAIN 45 195 CASH. {ECO:0000259|SMART:SM00722}. SQ SEQUENCE 256 AA; 27718 MW; 59EC40D562FC1D24 CRC64; MHTSALRIWL KAVLILAAGS IFQTASAAVV HVSPQDNLAE IFARARAGDT IKLASGVYQT KLYIDKPITI EGPADRSATI EGDKSGRTIA VHAPDVTLRN LTVTRSGMSL PAMDAGIYLE KAAPRALVEH NNIFDNSFGV YLHGSADAMV RENKIVGDAT LRVNERGNGV TVWNAPGAQV VGNDISKGRD GIFSNTSTHN TYKNNRFSDL RFAVHYMYTN DSEVSGNISV GNNMGYVLMF SERLKVFDNI AVGSRD // ID A0A0H4IS43_NEIG1 Unreviewed; 66 AA. AC A0A0H4IS43; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63726.1}; GN ORFNames=NGO_07690 {ECO:0000313|EMBL:AKO63726.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63726.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63726.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63726; AKO63726; NGO_07690. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 56 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 66 AA; 7535 MW; 199A229984C8563C CRC64; MPSFGSNTEN IVRFEHEVLI VCVGRYLDYV TIRAFIKISL PGGILFLKTV GFGFVWGQSR PNWSNR // ID A0A0H4ITB9_NEIG1 Unreviewed; 255 AA. AC A0A0H4ITB9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=AraC family transcriptional regulator {ECO:0000313|EMBL:AKO63819.1}; GN ORFNames=NGO_11415 {ECO:0000313|EMBL:AKO63819.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63819.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63819.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63819; AKO63819; NGO_11415. DR Proteomes; UP000000535; 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 InterPro; IPR018060; HTH_AraC. DR Pfam; PF12833; HTH_18; 1. DR SMART; SM00342; HTH_ARAC; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000700}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|RuleBase:RU000700}; KW Transcription regulation {ECO:0000256|RuleBase:RU000700}. FT DOMAIN 181 255 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 255 AA; 28541 MW; 47849006B3832D5E CRC64; MEGSYRFDTL SNGISIHGGT VTARCDFCSS RLAEPYVSFV LLLEGRLDFG INRRRFRIDA DGGKIVLIAV GEEVLFSRYL YRGGKTVKMT IKGMEQWLPR PEYARFAPLL YREPVRIWDL PPNLRGLAAS CLQTVPKGHL GETLRREADV LRLLSDLWDT VSDGIEPAAG QTAEADAMPS EDFSRTLNAA FDGGAHQVNR LTAALNISER TLQRRMRDHF GITASEWLHH KQMQHALYLL QNGGKNVGET AYLCG // ID A0A0H4IRJ4_NEIG1 Unreviewed; 59 AA. AC A0A0H4IRJ4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63581.1}; GN ORFNames=NGO_00175 {ECO:0000313|EMBL:AKO63581.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63581.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63581.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63581; AKO63581; NGO_00175. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6849 MW; E8BBA12753D8763B CRC64; MPCIGRRHRR RYTDKRNKFP NAQRHTKHRP KAAARTLPAA CGVSIKKPQK QTPFKNAAR // ID Q5F6Z7_NEIG1 Unreviewed; 605 AA. AC Q5F6Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 52. DE SubName: Full=Septum formation inhibitor Maf {ECO:0000313|EMBL:AAW90040.1}; GN ORFNames=NGO_1392 {ECO:0000313|EMBL:AAW90040.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90040.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90040.1; -; Genomic_DNA. DR RefSeq; WP_010951255.1; NC_002946.2. DR RefSeq; YP_208452.1; NC_002946.2. DR ProteinModelPortal; Q5F6Z7; -. DR EnsemblBacteria; AAW90040; AAW90040; NGO_1392. DR GeneID; 3281322; -. DR KEGG; ngo:NGO1392; -. DR PATRIC; 20336175; VBINeiGon24812_1636. DR HOGENOM; HOG000220763; -. DR OMA; KHARESI; -. DR OrthoDB; EOG66F037; -. DR BioCyc; NGON242231:GI2G-1305-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003587; Hint_dom_N. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 605 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256602. SQ SEQUENCE 605 AA; 66230 MW; DC08BE4A806A2B04 CRC64; MKPLRRLTNL LAACAVAAVA LIQPALAADL AQDPFITDNT QRQHYEPGGK YHLFGDPRGS VSDRTGKINV IQDYTHQMGN LLIQQAAIQG NLGYTVRFSG HGHEEHAPFD NHAADSASEE KGNVDDGFTV YRLNWEGHEH HPADAYDGPK GGNYPKPTGA RDEYTYHVNG TARSIKLNPT DTRSIRQRIF DNYNNLGSNF SDRADEANRK MFEHNAKLDR WGNSMEFVNG VAAGALNPFI SAGEALGIGD ILYGTRYAID KAAMRNIAPL PAEGKFAAIG GLGSAAGFEK NTREAVDRWI QENPNAAETV EALVNVLPFA KVKNLTKAAK PGKAAVSGDF SKSYTCSFHG STLVKTADGY KAIAHIQAGD RVLSKDEASG ETGYKPVTAR YGNPYQETVY IEVSDGIGNS QTLISNRIHP FYSDGKWIKA EDLKAGSRLL SESGKTQTVR NIVVKPKPLK AYNLTVADWH TYFVKGDKAE TEGVWVHNDC PTKLKPTERY NRQTHYGGSQ TDGARAQAAR QAGEGKPCPT CGRIQIFGTK TAPSPQHEPP LVKHYYEHGG HSMSNADRAK HARESIKGTQ CLTCQRKEGA MMSRYSREQA KKHGL // ID Q5F7M9_NEIG1 Unreviewed; 105 AA. AC Q5F7M9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89808.2}; GN ORFNames=NGO_1141 {ECO:0000313|EMBL:AAW89808.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89808.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89808.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89808; AAW89808; NGO_1141. DR PATRIC; 20335542; VBINeiGon24812_1336. DR HOGENOM; HOG000218810; -. DR OrthoDB; EOG6H1Q2Q; -. DR BioCyc; NGON242231:GI2G-1054-MONOMER; -. DR BioCyc; NGON242231:GI2G-1183-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR009509; DUF1132. DR Pfam; PF06575; DUF1132; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 105 AA; 12428 MW; AF138AC599DD91F9 CRC64; MNKPFITQAQ LALYKYQPSS EYFGQSMAVI AQSEFVEFAK INKSENVIDC FSFFWNRRIK HDIWLISFPD NSEMVIKESL NDGHKTYKFE FCEIVDNCNF DDVFV // ID Q5F839_NEIG1 Unreviewed; 154 AA. AC Q5F839; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 58. DE RecName: Full=Universal stress protein {ECO:0000256|PIRNR:PIRNR006276}; GN ORFNames=NGO_0959 {ECO:0000313|EMBL:AAW89648.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89648.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89648.1; -; Genomic_DNA. DR RefSeq; WP_003688341.1; NC_002946.2. DR RefSeq; YP_208060.1; NC_002946.2. DR ProteinModelPortal; Q5F839; -. DR EnsemblBacteria; AAW89648; AAW89648; NGO_0959. DR GeneID; 3282570; -. DR KEGG; ngo:NGO0959; -. DR PATRIC; 20335104; VBINeiGon24812_1121. DR HOGENOM; HOG000238897; -. DR OMA; LETEANN; -. DR OrthoDB; EOG65BDRM; -. DR BioCyc; NGON242231:GI2G-890-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006276}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 148 Usp. {ECO:0000259|Pfam:PF00582}. SQ SEQUENCE 154 AA; 16422 MW; CB4C262CB294D064 CRC64; MYKHLVVAVD GSETSINALK HAAELAGVNG ARLTLVHVAN PAEYMALAPE FLQHESYEAA AVAQGNEVLD AAERTARELG VGNTVKHLLV ANKGAREMAQ DLVDYADENG AGLLVLGTHG RTGLMHLLMG SFAETVMRQS HLPLLIIRSK AEEA // ID Q5F562_NEIG1 Unreviewed; 242 AA. AC Q5F562; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472}; DE AltName: Full=2-polyprenyl-6-hydroxyphenol methylase {ECO:0000256|HAMAP-Rule:MF_00472}; DE AltName: Full=3-demethylubiquinone 3-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472}; GN Name=ubiG {ECO:0000256|HAMAP-Rule:MF_00472}; GN ORFNames=NGO_2074 {ECO:0000313|EMBL:AAW90675.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90675.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation CC steps in the ubiquinone biosynthetic pathway. {ECO:0000256|HAMAP- CC Rule:MF_00472, ECO:0000256|SAAS:SAAS00561163}. 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:0000256|HAMAP- CC Rule:MF_00472}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 3- CC demethylubiquinone-n = S-adenosyl-L-homocysteine + ubiquinone-n. CC {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000256|SAAS:SAAS00063541}. CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00472, ECO:0000256|SAAS:SAAS00063519}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC UbiG/COQ3 family. {ECO:0000256|HAMAP-Rule:MF_00472}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90675.1; -; Genomic_DNA. DR RefSeq; WP_010951399.1; NC_002946.2. DR RefSeq; YP_209087.1; NC_002946.2. DR ProteinModelPortal; Q5F562; -. DR EnsemblBacteria; AAW90675; AAW90675; NGO_2074. DR GeneID; 3282843; -. DR KEGG; ngo:NGO2074; -. DR PATRIC; 20337979; VBINeiGon24812_2512. DR HOGENOM; HOG000278065; -. DR KO; K00568; -. DR OMA; HDWEKFV; -. DR OrthoDB; EOG6D5G4H; -. DR BioCyc; NGON242231:GI2G-1969-MONOMER; -. DR UniPathway; UPA00232; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro. DR GO; GO:0061542; F:3-demethylubiquinone-n 3-O-methyltransferase activity; IEA:UniProtKB-HAMAP. 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 {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00472, KW ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:AAW90675.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00472, KW ECO:0000256|SAAS:SAAS00448117}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00472, KW ECO:0000256|SAAS:SAAS00448101, ECO:0000313|EMBL:AAW90675.1}; KW Ubiquinone {ECO:0000313|EMBL:AAW90675.1}; KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00472, KW ECO:0000256|SAAS:SAAS00448108}. FT BINDING 44 44 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00472}. FT BINDING 63 63 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00472}. FT BINDING 85 85 S-adenosyl-L-methionine. FT {ECO:0000256|HAMAP-Rule:MF_00472}. FT BINDING 130 130 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00472}. SQ SEQUENCE 242 AA; 26958 MW; CD51E6C0A93243F8 CRC64; MGGKMSDKKY NVDEGEIAKF SRIADKWWDK SGEFKTLHDI NPLRLDYIDG HADLRGKRVL DVGCGGGILA ESMARRGAAF VKGIDMAEQS LETARLHAAL NNVADIEYEC VRVEDLAGAE PHSFDVVTCM EMMEHVPDPA AIVRACAKLV RPDSMVFFST INKNPKSYLH LIVAAEYLLK FVPKGTHDWK KFISPAELAR MCRQAGLDVA DTKGMTYHVL SQTYALCDST DVNYMFACRP AF // ID Q5F9Z1_NEIG1 Unreviewed; 177 AA. AC Q5F9Z1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88996.1}; GN ORFNames=NGO_0243 {ECO:0000313|EMBL:AAW88996.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88996.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88996.1; -; Genomic_DNA. DR RefSeq; WP_010357100.1; NC_002946.2. DR RefSeq; YP_207408.1; NC_002946.2. DR DNASU; 3281497; -. DR EnsemblBacteria; AAW88996; AAW88996; NGO_0243. DR GeneID; 3281497; -. DR KEGG; ngo:NGO0243; -. DR PATRIC; 20333437; VBINeiGon24812_0300. DR HOGENOM; HOG000218833; -. DR KO; K09924; -. DR OMA; RIICGGI; -. DR OrthoDB; EOG6CZQK7; -. DR BioCyc; NGON242231:GI2G-227-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018637; DUF2059. DR Pfam; PF09832; DUF2059; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 177 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256636. FT DOMAIN 102 146 DUF2059. {ECO:0000259|Pfam:PF09832}. SQ SEQUENCE 177 AA; 19710 MW; 1A8F192EA8DCA935 CRC64; MKLKTLLLPF AALALCANAF AAPPGDASLA RWLDTQNFDR DIEKNMIEGF NAGFKPYADK ALAEMPEAKK DQAAEAFNRY RENVLKDLIT PEVKQAVRNT LLKNAREIYT QEEIDGMIAF YGSPVGQSVV AKNPRLIKKS MSEIAVSWTA LSGKIARHHL PEFTEELRRI ICGGIVD // ID A0A0H4IWD6_NEIG1 Unreviewed; 59 AA. AC A0A0H4IWD6; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63733.1}; GN ORFNames=NGO_07895 {ECO:0000313|EMBL:AKO63733.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63733.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63733.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63733; AKO63733; NGO_07895. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6588 MW; FAC5BBB89CD819A2 CRC64; MPQLEKCPLP NPPPQGRERV AADFAVAGSL KSRLDKQPLI TGRLKNKKQP AQAIFFFLE // ID Q5F971_NEIG1 Unreviewed; 217 AA. AC Q5F971; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 47. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89266.1}; GN ORFNames=NGO_0528 {ECO:0000313|EMBL:AAW89266.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89266.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89266.1; -; Genomic_DNA. DR RefSeq; WP_010951075.1; NC_002946.2. DR RefSeq; YP_207678.1; NC_002946.2. DR DNASU; 3282920; -. DR EnsemblBacteria; AAW89266; AAW89266; NGO_0528. DR GeneID; 3282920; -. DR KEGG; ngo:NGO0528; -. DR PATRIC; 20334102; VBINeiGon24812_0623. DR HOGENOM; HOG000218644; -. DR OMA; PECSASR; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-506-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24192 MW; 86F68FD93616C253 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFECPAGPG ASCFGVRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAEDDA EPETLPPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP LLRECEFRFN FGTPSRQLKI LRDRCGI // ID A0A0H4IST3_NEIG1 Unreviewed; 67 AA. AC A0A0H4IST3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63669.1}; GN ORFNames=NGO_04905 {ECO:0000313|EMBL:AKO63669.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63669.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63669.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63669; AKO63669; NGO_04905. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 6803 MW; 54BE8A8D73932D76 CRC64; MKNKTSSLPL WLAAIMLAAR SPSKEDKTKE NGASAASSSA SSASSQTDLQ PAASAPDNVK QAESAPL // ID A0A0H4IWK3_NEIG1 Unreviewed; 331 AA. AC A0A0H4IWK3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 6. DE SubName: Full=Hemoglobin-haptoglobin-utilization protein {ECO:0000313|EMBL:AKO63818.1}; GN ORFNames=NGO_11390 {ECO:0000313|EMBL:AKO63818.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63818.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:5EE2} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 176-331. RX PubMed=26671256; DOI=10.1038/ncomms10172; RA Wong C.T., Xu Y., Gupta A., Garnett J.A., Matthews S.J., Hare S.A.; RT "Structural analysis of haemoglobin binding by HpuA from the RT Neisseriaceae family."; RL Nat. Commun. 6:10172-10172(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; AE004969; AKO63818.1; -; Genomic_DNA. DR PDB; 5EE2; X-ray; 1.95 A; A=176-331. DR PDBsum; 5EE2; -. DR EnsemblBacteria; AKO63818; AKO63818; NGO_11390. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR InterPro; IPR031586; HpuA. DR InterPro; IPR011250; OMP/PagP_b-brl. DR Pfam; PF16960; HpuA; 2. DR SUPFAM; SSF56925; SSF56925; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5EE2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 331 AA; 35062 MW; 8A8648C02A316334 CRC64; MSIPTATPLP AGEVTLSSDN GNIENINTAG AGSASDAPSR SRRSLDAAPQ NTSGISIRQR EVEKDYFGYK SKETSFIFKT PGGAQYALSS YADPITVSYS SPDFKIPDRH AGQRLADGSR IFICCSDSGA TSYAEITKQD YMKFGAWIGP NGEIDLFAGG FPVGKTPPPA FSYGSSTPET ALSKGKITYQ VWGIRVRNGQ FVTSSYTPPK SGSYYGTLAN TPVLSFITAN FNSNTLAGKI LGNSDYGPDV DIQNATITGP TFSGDATSGG KSGKLEGKFF GKFASTRSSE VSIGGKITFD GDRSLDTVFG GVSYEKKLDD TSQDTNHLTK Q // ID Q5F9Q8_NEIG1 Unreviewed; 287 AA. AC Q5F9Q8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 88. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000256|HAMAP-Rule:MF_00137, ECO:0000256|SAAS:SAAS00194445}; DE EC=6.3.2.6 {ECO:0000256|HAMAP-Rule:MF_00137, ECO:0000256|SAAS:SAAS00194458}; DE AltName: Full=SAICAR synthetase {ECO:0000256|HAMAP-Rule:MF_00137}; GN Name=purC {ECO:0000256|HAMAP-Rule:MF_00137}; GN ORFNames=NGO_0333 {ECO:0000313|EMBL:AAW89079.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89079.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00137, CC ECO:0000256|SAAS:SAAS00194441}. 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:0000256|HAMAP-Rule:MF_00137, ECO:0000256|SAAS:SAAS00194440}. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC {ECO:0000256|HAMAP-Rule:MF_00137, ECO:0000256|SAAS:SAAS00535425}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89079.2; -; Genomic_DNA. DR RefSeq; WP_020996787.1; NC_002946.2. DR RefSeq; YP_207491.2; NC_002946.2. DR ProteinModelPortal; Q5F9Q8; -. DR EnsemblBacteria; AAW89079; AAW89079; NGO_0333. DR GeneID; 3281760; -. DR KEGG; ngo:NGO0333; -. DR PATRIC; 20333659; VBINeiGon24812_0407. DR HOGENOM; HOG000230360; -. DR KO; K01923; -. DR OMA; WNKQPPA; -. DR OrthoDB; EOG69SKD1; -. DR BioCyc; NGON242231:GI2G-314-MONOMER; -. DR UniPathway; UPA00074; UER00131. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00137, KW ECO:0000256|SAAS:SAAS00416489}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00137, KW ECO:0000256|SAAS:SAAS00416508, ECO:0000313|EMBL:AAW89079.2}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00137, KW ECO:0000256|SAAS:SAAS00416489}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00137, KW ECO:0000256|SAAS:SAAS00416526}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 262 SAICAR_synt. {ECO:0000259|Pfam:PF01259}. SQ SEQUENCE 287 AA; 32252 MW; 6D328E0FD197E7BD CRC64; MSEIGLVKIY SGKVRDLYEI DDKRMLMVAS DRLSAFDVIL DAPIPGKGEI LTQISNFWFK KLAHIMPNHF TGDTVYDVLP ENEAKALEKR AVVAKKLTPV KVEAIVRGYL AGSGWKDYQK TGSVCGIRLP EGMREAQQLP EVIFTPSTKA AVGDHDENIS FEECGRIIGK ELAEEVRDKA VRLYTEAAEY AKSRGIIICD TKFEFGLDEE GTLTLMDEVL TPDSSRFWPA DQYEVGTNPP SFDKQFVRDW LEQSGWNKKA PAPKVPADVI RKTVEKYQEA LTLLTQD // ID Q5F8E1_NEIG1 Unreviewed; 222 AA. AC Q5F8E1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=DnaA regulatory inactivator Hda {ECO:0000313|EMBL:AAW89546.1}; GN ORFNames=NGO_0841 {ECO:0000313|EMBL:AAW89546.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89546.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89546.1; -; Genomic_DNA. DR RefSeq; WP_003688563.1; NC_002946.2. DR RefSeq; YP_207958.1; NC_002946.2. DR ProteinModelPortal; Q5F8E1; -. DR EnsemblBacteria; AAW89546; AAW89546; NGO_0841. DR GeneID; 3282156; -. DR KEGG; ngo:NGO0841; -. DR PATRIC; 20334848; VBINeiGon24812_0994. DR HOGENOM; HOG000256538; -. DR KO; K10763; -. DR OMA; GWGLVYQ; -. DR OrthoDB; EOG6038W4; -. DR BioCyc; NGON242231:GI2G-788-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 34 198 Bac_DnaA. {ECO:0000259|Pfam:PF00308}. SQ SEQUENCE 222 AA; 25453 MW; FDFF8C64E8813C86 CRC64; MNQLIFDFAA HDYPSFDKFL GTENAELVYV LQHKHDPFIY VWGEEGAGKS HLLQAWVAQA LEAGKNAAYI DAASMPLTDA AFEAEYLAVD QVEKLGNEEQ ALLFSIFNRF RNSGKGFLLL GSEYTPQQLV IREDLRTRMA YCLVYEVKPL TDQEKIDALA NMAAARQVTV DSEIFEYLLK HWRRDMDSLM MMLDTLDNYA VTMGKRITLP LLRQLLKQQE TQ // ID Q5F851_NEIG1 Unreviewed; 239 AA. AC Q5F851; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. 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 ORFNames=NGO_0941 {ECO:0000313|EMBL:AAW89636.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89636.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89636.1; -; Genomic_DNA. DR RefSeq; WP_003693308.1; NC_002946.2. DR RefSeq; YP_208048.1; NC_002946.2. DR ProteinModelPortal; Q5F851; -. DR EnsemblBacteria; AAW89636; AAW89636; NGO_0941. DR GeneID; 3281595; -. DR KEGG; ngo:NGO0941; -. DR PATRIC; 20335067; VBINeiGon24812_1103. DR HOGENOM; HOG000085050; -. DR OMA; IMHAEIM; -. DR OrthoDB; EOG64FKGZ; -. DR BioCyc; NGON242231:GI2G-878-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00972}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00972}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 25918 MW; 2AD2D080D2413839 CRC64; MLATPPLAPK TVAALHRLGI RTLEELRQNG SVKAFLLLKA SGLTLTKSTL WQLESLLNGT PPQEMSQAHK DCLLAELKNH PPVAAFPPQE EMGYFMREAL RQAEQSAADG EIPVGAVIVS DGKIITSAHN TCIADCNVSR HAEINALAQA GSEMQNYRLD GCDIYITLEP CAMCASALIQ ARIRRVIYGA AEPKTGAAGS IVNLFADKRL NTHTAIRGGI LQEECRAVLS RFFQNKRKG // ID Q5F9H5_NEIG1 Unreviewed; 195 AA. AC Q5F9H5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 48. DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:AAW89162.1}; GN ORFNames=NGO_0419 {ECO:0000313|EMBL:AAW89162.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89162.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89162.1; -; Genomic_DNA. DR RefSeq; WP_010951039.1; NC_002946.2. DR RefSeq; YP_207574.1; NC_002946.2. DR ProteinModelPortal; Q5F9H5; -. DR EnsemblBacteria; AAW89162; AAW89162; NGO_0419. DR GeneID; 3282997; -. DR KEGG; ngo:NGO0419; -. DR PATRIC; 20333849; VBINeiGon24812_0502. DR HOGENOM; HOG000137693; -. DR OrthoDB; EOG6W19KN; -. DR BioCyc; NGON242231:GI2G-397-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89162.1}. SQ SEQUENCE 195 AA; 22562 MW; 2424886E236870CB CRC64; MVSTIRTGCG RNIFPKSSTD PPTQRHQNRH PRPHVPLSAE RNSKHPDRSL RFCPIPAKRF GHLRMAQHVF LPRFPFIDID RIRWVRAGLK AFKHYIRENG LPDLIHAHCM NYAGILAQKI SEKYGIPYVL TEHSSTITRG LIRHHQWQPM EKAAAPASAR LAVSRHFAHV LQHKYGCEWQ YLPNIPGGIF KQTFE // ID Q5F912_NEIG1 Unreviewed; 253 AA. AC Q5F912; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE SubName: Full=Pilus assembly protein PilW {ECO:0000313|EMBL:AAW89325.1}; GN ORFNames=NGO_0595 {ECO:0000313|EMBL:AAW89325.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89325.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89325.1; -; Genomic_DNA. DR RefSeq; WP_003688950.1; NC_002946.2. DR RefSeq; YP_207737.1; NC_002946.2. DR ProteinModelPortal; Q5F912; -. DR SMR; Q5F912; 32-251. DR EnsemblBacteria; AAW89325; AAW89325; NGO_0595. DR GeneID; 3281181; -. DR KEGG; ngo:NGO0595; -. DR PATRIC; 20334264; VBINeiGon24812_0704. DR HOGENOM; HOG000218990; -. DR KO; K02656; -. DR OMA; RAQFYIR; -. DR OrthoDB; EOG6Q2SH3; -. DR BioCyc; NGON242231:GI2G-565-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 36 174 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 253 AA; 28451 MW; E72B1DE64D799A3E CRC64; MPFKPSKRIS LLLVLALGAC STSYRPSRAE KANQVSNIKT QLAMEYMRGQ DYRQATASIE DALKSNPKNE LAWLVRAEIY QYLKVNDKAQ ESFRQALSIK PDSAEINNNY GWFLCGRLNR PAESMAYFDK ALADPTYPTP YIANLNKGIC SAKQGQFGLA EAYLKRSLAA QPQFPPAFKE LARTKMLAGQ LGDADYYFKK YQSRVEVLQA DDLLLGWKIA KALGNVQAAY EYEAQLQANF PYSEELQTVL TGQ // ID A0A0H4ISL2_NEIG1 Unreviewed; 38 AA. AC A0A0H4ISL2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63609.1}; GN ORFNames=NGO_01330 {ECO:0000313|EMBL:AKO63609.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63609.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63609.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63609; AKO63609; NGO_01330. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 38 AA; 4400 MW; 9AA9CA9CAE6F7083 CRC64; MHKSILLEDV AVRNISIQEE KKCLIGYNQG KSYFISED // ID Q5F5Q0_NEIG1 Unreviewed; 706 AA. AC Q5F5Q0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 88. DE SubName: Full=ATPase {ECO:0000313|EMBL:AAW90487.1}; GN ORFNames=NGO_1867 {ECO:0000313|EMBL:AAW90487.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90487.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90487.1; -; Genomic_DNA. DR RefSeq; WP_003690126.1; NC_002946.2. DR RefSeq; YP_208899.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q0; -. DR EnsemblBacteria; AAW90487; AAW90487; NGO_1867. DR GeneID; 3282362; -. DR KEGG; ngo:NGO1867; -. DR PATRIC; 20337428; VBINeiGon24812_2245. DR HOGENOM; HOG000266158; -. DR OMA; VVSYQFV; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NGON242231:GI2G-1771-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 76721 MW; CF1D0B5FD4E1AECC CRC64; MRRFLPIAAI CAVVLLYGLT AATGSTSSLA DYFWWIVSFS AMLLLVLSAV LARYVILLLK DRRNGVFGSQ IAKRLSGMFT LVAVLPGLFL FGISAQFING TINSWFGNDT HEALERSLNL SKSALDLAAD NAVSNAVPVQ IDLIGTASLS GNMGSVLEHY AGSGFAQLAL YNAASGKIEK SINPHQFDQP LPDKEHWEQI QQTGSVRSLE SIGGVLYAQG WLSAGTHNGR DYALFFRQPI PENVAQDAVL IEKARAKYAE LSYSKKGLQT FFLVTLLIAS LLSIFLALVM ALYFARRFVE PILSLAEGAK AVAQGDFSQT RPVLRNDEFG RLTKLFNHMT EQLSIAKEAD ERNRRREEAA RHYLECVLDG LTTGVVVFDE KGRLKTFNKA AEQILGMPLA PLWGSSRHGW HGVSAQQSLL AEVFAAIGAA AGTDKPVQVE YAAPDDAKIL LGKATVLPED NGNGVVMVID DITVLIRAQK EAAWGEVAKR LAHEIRNPLT PIQLSAERLA WKLGGKLDDQ DAQILTRSTD TIIKQVAALK EMVEAFRNYA RAPSLKLENQ DLNALIGDVL ALYEAGPCRF EAELAGEPLM MAADTTAMRQ VLHNIFKNAA EAAEEADMPE VRVKSETGQD GRIVLTVCDN GKGFGKEMLH NAFEPYVTDK PAGTGLGLPV VKKIIGEHGG RISLSNQDAG GACVRIILPK TVETYA // ID Q5F6P5_NEIG1 Unreviewed; 380 AA. AC Q5F6P5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 69. DE SubName: Full=DNA methylase {ECO:0000313|EMBL:AAW90142.1}; GN ORFNames=NGO_1504 {ECO:0000313|EMBL:AAW90142.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90142.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000256|SAAS:SAAS00572311}. CC -!- SIMILARITY: Contains THUMP domain. CC {ECO:0000256|SAAS:SAAS00512137}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90142.1; -; Genomic_DNA. DR RefSeq; WP_004465704.1; NC_002946.2. DR RefSeq; YP_208554.1; NC_002946.2. DR ProteinModelPortal; Q5F6P5; -. DR DNASU; 3281364; -. DR EnsemblBacteria; AAW90142; AAW90142; NGO_1504. DR GeneID; 3281364; -. DR KEGG; ngo:NGO1504; -. DR PATRIC; 20336482; VBINeiGon24812_1789. DR HOGENOM; HOG000040915; -. DR KO; K07444; -. DR OMA; GFMYKAN; -. DR OrthoDB; EOG6HJ238; -. DR BioCyc; NGON242231:GI2G-1408-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 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; PS00092; N6_MTASE; 1. DR PROSITE; PS51165; THUMP; 1. DR PROSITE; PS01261; UPF0020; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00572314, KW ECO:0000313|EMBL:AAW90142.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00572314, KW ECO:0000313|EMBL:AAW90142.1}. FT DOMAIN 46 157 THUMP. {ECO:0000259|PROSITE:PS51165}. SQ SEQUENCE 380 AA; 42294 MW; 5096B0AD4CFBC77F CRC64; MNTLYTLFAT CPRGLETVLS QELGSLGCTD VQAFDGGVSC RGGLEQAYAA NLHSRTAGRI LLRLTKGTYR TERDIYKLAK NINWFNWFTL QQTFKVKIEA KRANVKSLQF AGLTVKDAVC DAFRDIYDAR PSVDKAAPDV RIHAFLDERN VEIFIDTSGE ALFKRGYRLD TGEAPLRENL AAGLLLSAGY DGTQPFQDPF CGSGTIAIEA AWIAAGRAPG MMRRFGFEKL QNFDKTLWAD LRRRAEAQTR PVRAPIAGSD NGRRIVQTAL DNAHNAGADD IVSFSVAGAQ SVRPNGENGI MVSNPPYGVR LEEVRALQAL YPQLGTWLKK HYAGWRVGMF TGDREMPKFM RLLPKRKIPL YNGNIDCRLF LIDMVQGSNR // ID A0A0H4IV51_NEIG1 Unreviewed; 59 AA. AC A0A0H4IV51; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=SbmA protein {ECO:0000313|EMBL:AKO63660.1}; GN ORFNames=NGO_04425 {ECO:0000313|EMBL:AKO63660.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63660.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63660.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63660; AKO63660; NGO_04425. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 50 ABC transporter. FT {ECO:0000259|Pfam:PF00005}. SQ SEQUENCE 59 AA; 6521 MW; 848FFA6D6CC6DE7C CRC64; MNTCRLGYLI DKLDKTDGWQ HKLSPGELQR VAFVRALLSK PKIVLLDEAA AALDEPAEA // ID Q5F4Z5_NEIG1 Unreviewed; 78 AA. AC Q5F4Z5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=ATP synthase subunit c {ECO:0000256|SAAS:SAAS00242779}; GN ORFNames=NGO_2145 {ECO:0000313|EMBL:AAW90742.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90742.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90742.1; -; Genomic_DNA. DR RefSeq; WP_002214801.1; NC_002946.2. DR RefSeq; YP_209154.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z5; -. DR EnsemblBacteria; AAW90742; AAW90742; NGO_2145. DR GeneID; 3282776; -. DR KEGG; ngo:NGO2145; -. DR PATRIC; 20338143; VBINeiGon24812_2594. DR HOGENOM; HOG000235244; -. DR KO; K02110; -. DR OMA; WGLICSK; -. DR OrthoDB; EOG68H8G3; -. DR BioCyc; NGON242231:GI2G-2036-MONOMER; -. DR Proteomes; UP000000535; 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: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:UP000000535}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU003372}; KW Ion transport {ECO:0000256|RuleBase:RU003372}; KW Membrane {ECO:0000256|SAAS:SAAS00499070, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F4W7_NEIG1 Unreviewed; 237 AA. AC Q5F4W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 63. DE SubName: Full=Tetrapyrrole methylase {ECO:0000313|EMBL:AAW90770.2}; GN ORFNames=NGO_2177 {ECO:0000313|EMBL:AAW90770.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90770.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90770.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F4W7; -. DR EnsemblBacteria; AAW90770; AAW90770; NGO_2177. DR PATRIC; 20338216; VBINeiGon24812_2630. DR HOGENOM; HOG000258038; -. DR OMA; ETPYRNR; -. DR OrthoDB; EOG61308G; -. DR BioCyc; NGON242231:GI2G-2064-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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 PIRSF; PIRSF005917; MTase_YraL; 1. DR SUPFAM; SSF53790; SSF53790; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW90770.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90770.2}. SQ SEQUENCE 237 AA; 26066 MW; 91A9E3045EA7D6A2 CRC64; MMSPVLYLIP TPLGTPDTPC LLQHEQRAVV GLTDFVVEAE KTARAHLKHL GITTPIRELN LQTLNEHTDL KTLPELLKPL QEGRSMGIVS EAGCPAVADP GANLVALAHK HGFEVRPLVG PSSLLLALMA SGANGQNFAF NGYLPSEKNE RIQSLNALEQ RSRQCGETQI FIETPYRNDA LLADAVENLH PETRLCTATD LTLPTQLVVS KTVADWRRMK EMPNLKKRPT IFVMYAG // ID Q5F6M8_NEIG1 Unreviewed; 399 AA. AC Q5F6M8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020}; DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020}; DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020}; GN Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020}; GN ORFNames=NGO_1521 {ECO:0000313|EMBL:AAW90159.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90159.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate CC and ATP. Can also catalyze the reverse reaction. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020}; CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP- CC Rule:MF_00020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020, CC ECO:0000256|SAAS:SAAS00314496}. CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP- CC Rule:MF_00020, ECO:0000256|RuleBase:RU003835, CC ECO:0000256|SAAS:SAAS00589723}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90159.1; -; Genomic_DNA. DR RefSeq; WP_004465718.1; NC_002946.2. DR RefSeq; YP_208571.1; NC_002946.2. DR ProteinModelPortal; Q5F6M8; -. DR EnsemblBacteria; AAW90159; AAW90159; NGO_1521. DR GeneID; 3281543; -. DR KEGG; ngo:NGO1521; -. DR PATRIC; 20336526; VBINeiGon24812_1811. DR HOGENOM; HOG000288398; -. DR KO; K00925; -. DR OMA; NEYVLVI; -. DR OrthoDB; EOG69975F; -. DR BioCyc; NGON242231:GI2G-1425-MONOMER; -. DR UniPathway; UPA00340; UER00458. DR Proteomes; UP000000535; 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; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00589711}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00421397}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00589699, KW ECO:0000313|EMBL:AAW90159.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00539098}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00539034}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|SAAS:SAAS00589711}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00020, KW ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00589699, KW ECO:0000313|EMBL:AAW90159.1}. FT NP_BIND 206 210 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT NP_BIND 281 283 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT NP_BIND 329 333 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT ACT_SITE 146 146 Proton donor/acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00020}. FT METAL 10 10 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT METAL 384 384 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT BINDING 17 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}. FT BINDING 89 89 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00020}. FT SITE 178 178 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00020}. FT SITE 239 239 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_00020}. SQ SEQUENCE 399 AA; 42970 MW; 3D6451212818C4D0 CRC64; MSDQLILVLN CVSSSLKGAV IDRKSGSVVL SCLGERLTTP EAVITFNKDG NKRQVPLSGR NCHAGAVGML LNELEKHGLH DRIKAIGRRI AHGGEKYHES VLIDQDVLDE LKACIPFAPL HNPANISGIL AAQEHFPGLP NVGVMDTSFH QTMPERAYTY AVPRELRKKY AFRRYGFHGT GMRYVAPEAA RILGKPLEDI RMIIAHLGNG ASITAVKNGK SVDTGMGFTP IEGLVMGTRC GDTDPGVYSY PTFHAGMDVA QVDEMLNEKS GFPGISELPN DCRTLEIAAD EGREGARLAL EVMTCRLAKY IASMAVACGS VDALVFTGGI GENSRNIRAK TVSYLDFLGL HIDTKANMEK RYGNSGIISP TDSSPAVLVV PTNEELMIAC DTAELAGIL // ID Q5FA43_NEIG1 Unreviewed; 617 AA. AC Q5FA43; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 72. DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463}; GN ORFNames=NGO_0189 {ECO:0000313|EMBL:AAW88944.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88944.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88944.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FA43; -. DR EnsemblBacteria; AAW88944; AAW88944; NGO_0189. DR PATRIC; 20333307; VBINeiGon24812_0236. DR HOGENOM; HOG000018637; -. DR OMA; AAPMEII; -. DR OrthoDB; EOG6N0HJT; -. DR BioCyc; NGON242231:GI2G-174-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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 9 29 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 437 457 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 461 481 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 490 510 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 547 567 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 570 590 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01463}. FT DOMAIN 1 103 SecD-TM1. {ECO:0000259|Pfam:PF13721}. SQ SEQUENCE 617 AA; 66746 MW; 9645EE17A6234FA5 CRC64; MNRYPLWKYL LIVFTIAVAA VYSLPNLFGE TPAVQVSTNR QAIIINEQTQ SKVDAALKNA GIQTDGMFVV DNSLKVRFKD TETQLKARDV IENTLGEGYI TALNLLADSP EWMAKIKANP MFLGLDLRGG VHFTMQVDMK AAMQKTFERY SGDIRRELRR EKIRSGTVRQ AENSLTVPLQ DAGDVQKALP QLLKLFPEAT LNSEGSNIVL TLSEEAVNKV RSDAVKQNIT TLHNRVNELG VAEPIIQQSG LDRIVVQLPG VQDTAKAKDI IGRTATLEVR MVEDDPAKLR EALEGNVPSG YELLSSGGEH PETLLISKQV ELTGDNINDA QPSFDQMGAP AVSLSLDSAG GSIFGELTAA NVGKRMAMVL IDQGKSEVVT APVIRTAITG GRVEISGSMT TAEANDTSLL LRAGSLAAPM QIVEERTIGP SLGKENIEKG FHSTLWGFAI VAAFMVVYYR LMGFFSTIAL SANILFLIGI LSAMQATLTL PGMAALALTL GMAIDSNVLI NERIREELRA GVPPQQAINL GFQHAWATIV DSNLTSLIAG IALLVFGSGP VRGFAVVHCL GILTSMYSSV VVFRALVNLW YGRRRKLQNI SIGAVWKPEA ETAAGKE // ID Q5F9C0_NEIG1 Unreviewed; 238 AA. AC Q5F9C0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Cro/Cl family transcriptional regulator {ECO:0000313|EMBL:AAW89217.1}; GN ORFNames=NGO_0479 {ECO:0000313|EMBL:AAW89217.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89217.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89217.1; -; Genomic_DNA. DR RefSeq; WP_003687969.1; NC_002946.2. DR RefSeq; YP_207629.1; NC_002946.2. DR ProteinModelPortal; Q5F9C0; -. DR DNASU; 3282967; -. DR EnsemblBacteria; AAW89217; AAW89217; NGO_0479. DR GeneID; 3282967; -. DR KEGG; ngo:NGO0479; -. DR PATRIC; 20333994; VBINeiGon24812_0569. DR HOGENOM; HOG000071249; -. DR OMA; TINDHYI; -. DR OrthoDB; EOG6Q8J1B; -. DR BioCyc; NGON242231:GI2G-457-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; 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 SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 29 84 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 238 AA; 26498 MW; C3FE6529972C3477 CRC64; MPFIIDYQCL CAINSEIKMF SGEQLGQAIS EAIKRKNVSQ KEVADHFGVK QPSVSGWIKN GRIDKKHLDK LIDYFSDVVT PSHFGIETFR VLKSNEQSSI RFPRLNAEAT CGAGTINDHY IEVVDYVTVA AAWAREKLGG NLNKIQVITA RGDSMEPTIE NGDVMFVDTA VEAFDGDGLY LLWYIDGLKA KRLQSTVGGG LMIISDNSSY RTETVRGEDL NAVRIIGRIR GAWRLSQF // ID A0A0H4IWG0_NEIG1 Unreviewed; 60 AA. AC A0A0H4IWG0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63768.1}; GN ORFNames=NGO_09365 {ECO:0000313|EMBL:AKO63768.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63768.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63768.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63768; AKO63768; NGO_09365. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 56 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 60 AA; 5930 MW; 538BBECED45F7562 CRC64; MGYEKGDVEA AGEKAQVQQD VAWGFEGGFD CFSEALSVCG LGVLGVGGVV AAVVAAGKPP // ID A0A0H4J605_NEIG1 Unreviewed; 120 AA. AC A0A0H4J605; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63802.1}; GN ORFNames=NGO_10980 {ECO:0000313|EMBL:AKO63802.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63802.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63802.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63802; AKO63802; NGO_10980. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 120 AA; 12872 MW; CF00AA3A70EBED7E CRC64; MAEGQKSAVT EYYLNHGIWP KDNTSAGVAN PTDIKGKYVE SVTVTNGVVT AKMLSSGVNK EIQGKRLSLW AKREAGSVKW FCGQPVKRTE ANADAAGKDT TNGINTKHLP STCRDPFSAS // ID Q5F6L7_NEIG1 Unreviewed; 423 AA. AC Q5F6L7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 64. 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 ORFNames=NGO_1534 {ECO:0000313|EMBL:AAW90170.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90170.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90170.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90170; AAW90170; NGO_1534. DR PATRIC; 20336564; VBINeiGon24812_1830. DR HOGENOM; HOG000282689; -. DR OMA; NIGWIRI; -. DR OrthoDB; EOG68M4JQ; -. DR BioCyc; NGON242231:GI2G-1436-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90170.2}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00913, KW ECO:0000313|EMBL:AAW90170.2}; 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:UP000000535}; 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:UP000000535}; 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; 47332 MW; 32B6FF882C817836 CRC64; MGDGVHTLLL DRPIVRDGRK FDAPLLWMVV LMTAFGLLMI YSASVYLASK EGGDQFFYLT RQAGFVVAGL IASGFLWFLC RMRTWRRLVP WIFALSGLLL VAVLIAGREI NGATRWIPLG PLNFQPTELF KLAVILYLAS LFTRREEVLR SMESLGWQSI WRGTANLIMS ATNPQARRET LEMYGRFRAI ILPIMLVAFG LVLIMVQPDF GSFVVITVIT VGMLFLAGLP WKYFFVLVGS VLGGMVLMIT AAPYRVQRVV AFLDPWKDPQ GAGYQLTHSL MAIGRGEWFG MGLGASLSKR GFLPEAHTDF IFAIIAEEFG FFGMCVLIFC YGWLVVRAFS IGKQSRDLGL TFNAYIASGI GIWIGIQSFF NIGVNIGALP TKGLTLPLMS YGGSSVFFML ISMMLLLRID YENRQKMRGY RVE // ID Q5F599_NEIG1 Unreviewed; 449 AA. AC Q5F599; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU003385}; GN ORFNames=NGO_2030 {ECO:0000313|EMBL:AAW90638.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90638.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90638.1; -; Genomic_DNA. DR RefSeq; WP_002215003.1; NC_002946.2. DR RefSeq; YP_209050.1; NC_002946.2. DR ProteinModelPortal; Q5F599; -. DR EnsemblBacteria; AAW90638; AAW90638; NGO_2030. DR GeneID; 3282717; -. DR KEGG; ngo:NGO2030; -. DR PATRIC; 20337843; VBINeiGon24812_2445. DR HOGENOM; HOG000255206; -. DR KO; K00412; -. DR OMA; PGGIPFF; -. DR OrthoDB; EOG6P3338; -. DR BioCyc; NGON242231:GI2G-1931-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 106 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 260 277 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 358 382 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; 50301 MW; 46E6F95B9C23BEF1 CRC64; MANQTNSKAK ALLGWMDARF PLSKMWNEHL AQYYAPKNFN FWYYFGSLAL LVLVIQIVSG IFLTMNYKPD GNLNAYHLPA AFTAVEYIMR DVSGGWIIRY MHSTGASFFF IVVYLHMFRG LIYGSYKKPR ELVWIFGSLI FLALMAEAFM GYLLPWGQMS FWGAQVIINL FSAIPVIGPD LSTWIRGDFN VSDVTLNRFF ALHVIAVPLV LLGLVVAHII ALHEVGSNNP DGVEIKKNKD ENGIPRDGIP FHPYYTVKDI LGVVVFLIVF CAVLFFAPEG GGYFLEAPNF DAANALKTPP HIAPVWYFTP FYAILRAIPS FLGTQVWGVI GMGAAVVLIA LLPWLDRGEV KSVRYRGPIF KTALVLFIIS FIGLGILGAM VATDTRTLVA RILSFVYFAF FLGMPFYTKL DKNKPVPERV TMSTAKQKIM FFVYVGITAV GAYLFATNI // ID Q5F9F1_NEIG1 Unreviewed; 358 AA. AC Q5F9F1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Sulfate/thiosulfate import ATP-binding protein CysA {ECO:0000256|HAMAP-Rule:MF_01701}; DE EC=3.6.3.25 {ECO:0000256|HAMAP-Rule:MF_01701}; DE AltName: Full=Sulfate-transporting ATPase {ECO:0000256|HAMAP-Rule:MF_01701}; GN Name=cysA {ECO:0000256|HAMAP-Rule:MF_01701}; GN ORFNames=NGO_0445 {ECO:0000313|EMBL:AAW89186.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89186.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01701, CC ECO:0000256|SAAS:SAAS00043414}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + sulfate(Out) = ADP + phosphate + CC sulfate(In). {ECO:0000256|HAMAP-Rule:MF_01701, CC ECO:0000256|SAAS:SAAS00043421}. 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:0000256|HAMAP-Rule:MF_01701, CC ECO:0000256|SAAS:SAAS00043407}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01701}; Peripheral membrane protein {ECO:0000256|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:0000256|HAMAP-Rule:MF_01701, ECO:0000256|SAAS:SAAS00552311}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000256|HAMAP- CC Rule:MF_01701, 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; AE004969; AAW89186.1; -; Genomic_DNA. DR RefSeq; WP_003701047.1; NC_002946.2. DR RefSeq; YP_207598.1; NC_002946.2. DR ProteinModelPortal; Q5F9F1; -. DR EnsemblBacteria; AAW89186; AAW89186; NGO_0445. DR GeneID; 3281417; -. DR KEGG; ngo:NGO0445; -. DR PATRIC; 20333916; VBINeiGon24812_0532. DR KO; K02045; -. DR OMA; PLTVVMR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-424-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_01701, KW ECO:0000256|RuleBase:RU363033, ECO:0000256|SAAS:SAAS00452173, KW ECO:0000313|EMBL:AAW89186.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01701}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01701}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01701, KW ECO:0000256|SAAS:SAAS00437633}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01701}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01701, KW ECO:0000256|RuleBase:RU363033, ECO:0000256|SAAS:SAAS00452173, KW ECO:0000313|EMBL:AAW89186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sulfate transport {ECO:0000256|HAMAP-Rule:MF_01701, KW ECO:0000256|SAAS:SAAS00437635}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01701, KW ECO:0000256|SAAS:SAAS00437635}. FT DOMAIN 3 238 ABC transporter. {ECO:0000256|HAMAP- FT Rule:MF_01701, FT ECO:0000259|PROSITE:PS50893}. FT DOMAIN 198 344 CYSA. {ECO:0000259|PROSITE:PS51237}. FT NP_BIND 36 43 ATP. {ECO:0000256|HAMAP-Rule:MF_01701}. SQ SEQUENCE 358 AA; 40182 MW; A3B06CCFBA42A618 CRC64; MSITIQNLNK KRFGNFHALK NINLNVPAGK LVSLLGPSGG GKTTLLRIIA GLENADGGQI LFDGQDVTAK HVRERKVGFV FQHYALFRHM NVFDNVAFGL TVLPKPERPS KGQIRAKVEE LLKLVQLSHL AKSYPHQLSG GQRQRIALAR ALAVEPKLLL LDEPFGALDA KVRKELRTWL RDIHHNLGVT SILVTHDQEE ALEVSDEIVV MNHGKIEQTG SAEAIYRKPE NAFVTEFLGE ADAFEGRIEK GIWHYNGFAW KLDAQYKWQE QTATGYIRPH EWQIAAEHET PMIRAEIEKI HAVGALTHVL VKHGKQDVHI TLAGSDAARY PIAEGKKLNL IPKQVYVFSQ NELIEYSI // ID A0A0H4IV10_NEIG1 Unreviewed; 111 AA. AC A0A0H4IV10; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Sugar transporter {ECO:0000313|EMBL:AKO63625.1}; GN ORFNames=NGO_02830 {ECO:0000313|EMBL:AKO63625.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63625.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63625.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63625; AKO63625; NGO_02830. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR InterPro; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sugar transport {ECO:0000313|EMBL:AKO63625.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000313|EMBL:AKO63625.1}. FT TRANSMEM 7 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 69 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 111 AA; 11731 MW; E896123664EB63E5 CRC64; MNASHKPWLS IVALAIGAFI FNTAEYIPIA LLSDIGRSFG MAATETGVMI TVYAWIVALT SLALPLMLLT RNYGTARPAA GPVCAVLLSA TSCRLPRGVL KSYSQAAWGL C // ID Q5F8J8_NEIG1 Unreviewed; 820 AA. AC Q5F8J8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 99. 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 ORFNames=NGO_0775 {ECO:0000313|EMBL:AAW89489.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89489.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89489.1; -; Genomic_DNA. DR RefSeq; WP_003688644.1; NC_002946.2. DR RefSeq; YP_207901.1; NC_002946.2. DR ProteinModelPortal; Q5F8J8; -. DR SMR; Q5F8J8; 610-790. DR MEROPS; S16.001; -. DR EnsemblBacteria; AAW89489; AAW89489; NGO_0775. DR GeneID; 3281944; -. DR KEGG; ngo:NGO0775; -. DR PATRIC; 20334698; VBINeiGon24812_0921. DR HOGENOM; HOG000261410; -. DR KO; K01338; -. DR OMA; GIKKAGM; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; NGON242231:GI2G-729-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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 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; 90783 MW; CC59D7E0346F6862 CRC64; MTQKEKHFEE YAALATLPLR DVVVYPHMVL PLFVGRPKSI AALENAITRE EPVFLLAQTD AAVEEPVATD LYQTGTVAQV LQVLKLPDGT VKVLVEGLYR GRVLTIEDTG GLFVSHIEAV VEEDTGGNTD LEAVRRTLLA QFEQYAKLNK KIPAEIIGSI NGIAENSRLT DTVAAHLQLK LAQRQQILEI PEIGKRMEFL LAKLESELDI MQAEKRIRGR VKRQMEKSQR EYYLNEQIKA IHKELGEEDE NGELDALEAG IKKAGMTKEA EEKCLSELKK LKMMPPMSAE STVVRNYIDT LLGLPWKKKS RVSKDIAKAG LVLDADHYGL EKVKERILEY LAVQKRMDKL KGPILCLVGP PGVGKTSLGE SIAKATGRKY VRMALGGVRD ESEIRGHRRT YIGSMPGKIL QNMAKAGVRN PLFLLDEIDK LGSDFRGDPA SALLEVLDHE QNNKFADHYA EVDYDLSDVM FIATSNSLNI PTPLLDRMEI IRLSGYTEDE KINIAMQYLV PKQMKRNGVK EGELVVEESA VRDIIRYYTR EAGVRSLDRE IAKICRKVVM QITLNEDKKR LSETKKTSKA KPRAVKVNEK NLHDYLGVRR FDYGVAESEN RIGQVTGLAW TEVGGELLTV EAAALPGKGM IQCTGQLGDV MKESVSAAWS VVRSRAESVG LAPDFYEKKD IHVHVPEGAT PKDGPSAGIA MTLAMVSAFT KIPVRADVAM TGEITLRGEV LPIGGLKEKL LAALRGGIKH VLIPKDNVKD LEEIPENVKT GLTIHPVKWI DEVLALGLES RPESWAEPSA AEAAAESASK PKPRSRAIKH // ID A0A0H4IVH7_NEIG1 Unreviewed; 98 AA. AC A0A0H4IVH7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63750.1}; GN ORFNames=NGO_08350 {ECO:0000313|EMBL:AKO63750.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63750.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63750.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63750; AKO63750; NGO_08350. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 98 AA; 11117 MW; D9536A3C69C8595D CRC64; MDGIVPDVCG TVCRIWFYHH PFSVETPPVA AIEPNRWRKL PLCIRGGVQC GALICRLCVE TGWSVHTGTV WLKLKVKYAE TLNEPLYCLY DLCCFAMI // ID Q5F561_NEIG1 Unreviewed; 305 AA. AC Q5F561; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000256|SAAS:SAAS00085804}; DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00301}; DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00301}; DE EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00301}; GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00301}; GN ORFNames=NGO_2075 {ECO:0000313|EMBL:AAW90676.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90676.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. {ECO:0000256|HAMAP-Rule:MF_00301, CC ECO:0000256|SAAS:SAAS00085813}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. {ECO:0000256|HAMAP- CC Rule:MF_00301, ECO:0000256|SAAS:SAAS00085805}. CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family. CC {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000256|SAAS:SAAS00570425}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90676.1; -; Genomic_DNA. DR RefSeq; WP_003692348.1; NC_002946.2. DR RefSeq; YP_209088.1; NC_002946.2. DR ProteinModelPortal; Q5F561; -. DR EnsemblBacteria; AAW90676; AAW90676; NGO_2075. DR GeneID; 3282842; -. DR KEGG; ngo:NGO2075; -. DR PATRIC; 20337981; VBINeiGon24812_2513. DR HOGENOM; HOG000004810; -. DR KO; K02204; -. DR OMA; AGALRFW; -. DR OrthoDB; EOG6BW4W1; -. DR BioCyc; NGON242231:GI2G-1970-MONOMER; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459726}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459717}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459716, ECO:0000313|EMBL:AAW90676.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459717}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459726}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00301, KW ECO:0000256|SAAS:SAAS00459716, ECO:0000313|EMBL:AAW90676.1}. FT DOMAIN 28 253 APH. {ECO:0000259|Pfam:PF01636}. SQ SEQUENCE 305 AA; 33592 MW; 87E9CFBF94CF61EB CRC64; MSVYTSVSDD EMRGFLSGYD LGEFVSLQGI AQGITNSNYF LTTTSGRYVL TVFEVLKQEE LPFFLELNRH LSMKGVAVAA PVARKDGRLD SVLAGKPACL VACLKGSDTA LPTAEQCFHT GAMLAKMHLA AADFPLEMEN PRYDAWWTEA CARLLPVLSQ DDAALLCSEI DALKDNLGNH LPSGIIHADL FKDNVLLDGG QVSGFIDFYY ACRGNFMYDL AIAVNDWART ADNKLDEALK KAFVGGYEGV RPLSAGEKAY FPTAQRAGCI RFWVSRLLDF HFPQAGEMTF IKDPNAFRNL LLSLD // ID A0A0H4IVP0_NEIG1 Unreviewed; 96 AA. AC A0A0H4IVP0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63825.1}; GN ORFNames=NGO_11685 {ECO:0000313|EMBL:AKO63825.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63825.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63825.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63825; AKO63825; NGO_11685. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 10912 MW; 79763F8CA2F07377 CRC64; MIRMKTSTVV FGGFFMADNG ERIQIPVLEN PDIREINRFF SVSNFEKKAG VLVFRIIPEP EFGNTELTVY FEKGYYSGLT KTGTALPRLS SKRTIP // ID Q5FA09_NEIG1 Unreviewed; 628 AA. AC Q5FA09; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 46. DE SubName: Full=Septum formation inhibitor Maf {ECO:0000313|EMBL:AAW88978.1}; GN ORFNames=NGO_0225 {ECO:0000313|EMBL:AAW88978.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88978.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88978.1; -; Genomic_DNA. DR RefSeq; WP_003704451.1; NC_002946.2. DR RefSeq; YP_207390.1; NC_002946.2. DR EnsemblBacteria; AAW88978; AAW88978; NGO_0225. DR GeneID; 3281479; -. DR KEGG; ngo:NGO0225; -. DR PATRIC; 20333391; VBINeiGon24812_0277. DR HOGENOM; HOG000220700; -. DR OMA; TQREWEN; -. DR OrthoDB; EOG64R617; -. DR BioCyc; NGON242231:GI2G-209-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR InterPro; IPR029501; EndoU_bac. DR Pfam; PF06255; DUF1020; 1. DR Pfam; PF14436; EndoU_bacteria; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 628 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256637. FT DOMAIN 505 626 EndoU_bacteria. FT {ECO:0000259|Pfam:PF14436}. SQ SEQUENCE 628 AA; 68756 MW; C55230AA00AD8E80 CRC64; MGISRKISLI LSILAVCLPM HAHASDLAND PFIRQVLDRQ HFEPDGKYHL FGSRGELAER SGHIGLGNIQ SHQLGNLMIQ QAAIKGNIGY IVRFSDHGHE VHSPFDNHAS HSDSDEAGSP VDGFSLYRIH WDGYEHHPAD GYDGPQGGGY PAPKGARDIY SYDIKGVAQN IRLNLTDNRS TGQRLADRFH NAGAMLTQGV GDGFKRATRY SPELDRSGNA AEAFNGTADI VKNIIGAAGE IVGAGDAVQG ISEGSNIAVM HGLGLLSTEN KMARINDLAD MAQLKDYAAA AIRDWAVQNP NAAQGIEAVS NIFMAAIPIK GIGAVRGKYG LGGITAHPVK RSQMGAIALP KGKSAVSDNF ADAAYAKYPS PYHSRNIRSN LEQRYGKENI TSSTVPPSNG KNVKLADQRH PKTGVPFDGK GFPNFEKHVK YDTKLDIQEL SGGGIPKAKP VFDAKPRWEV DRKLNKLTTR EQVEKNVQET RRRSQSSQFK AHAQREWENK TGLDFNHFIG GDINKKGTVT GGHSLTRGDV RVIQQTSAPD KHGVYQATVE IKKPDGSWEV KTKKGGKVMT KHTMFPKDWD EARIRAEVTS AWESRIMLKD NKWQGTSKSG IKIEGFTEPN RTAYPIYE // ID Q5F8X9_NEIG1 Unreviewed; 117 AA. AC Q5F8X9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Putative chaperone protein HscB {ECO:0000313|EMBL:AAW89358.1}; GN ORFNames=NGO_0630 {ECO:0000313|EMBL:AAW89358.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89358.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|SAAS:SAAS00371420}. CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity. CC {ECO:0000256|SAAS:SAAS00371431}. CC -!- SIMILARITY: Belongs to the HscB family. CC {ECO:0000256|SAAS:SAAS00561535}. CC -!- SIMILARITY: Contains J domain. {ECO:0000256|SAAS:SAAS00065102}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89358.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F8X9; -. DR EnsemblBacteria; AAW89358; AAW89358; NGO_0630. DR PATRIC; 20334344; VBINeiGon24812_0744. DR HOGENOM; HOG000262077; -. DR OrthoDB; EOG66F07J; -. DR BioCyc; NGON242231:GI2G-598-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0051259; P:protein oligomerization; IEA:InterPro. DR Gene3D; 1.10.287.110; -; 1. DR Gene3D; 1.20.1280.20; -; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR004640; HscB. DR InterPro; IPR009073; HscB_oligo_C. DR PANTHER; PTHR14021; PTHR14021; 1. DR Pfam; PF07743; HSCB_C; 1. DR SUPFAM; SSF47144; SSF47144; 1. DR TIGRFAMs; TIGR00714; hscB; 1. PE 3: Inferred from homology; KW Chaperone {ECO:0000256|SAAS:SAAS00448706}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 41 113 HSCB_C. {ECO:0000259|Pfam:PF07743}. SQ SEQUENCE 117 AA; 13368 MW; 0EB2B6C01524DAC2 CRC64; MMSSTINDAY RTLKNPIDRA AYLLKTSGID ADAPEHTSFA PDFLMQQMEW RETLMEARAG NNLESLKNLD NEIRAEQEKL FCGLKQSFAR QDCDTAAQQV RQGRFLDKLR HEISSAL // ID Q5F5Q2_NEIG1 Unreviewed; 395 AA. AC Q5F5Q2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=DNA processing protein DprA {ECO:0000313|EMBL:AAW90485.1}; GN ORFNames=NGO_1865 {ECO:0000313|EMBL:AAW90485.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90485.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90485.1; -; Genomic_DNA. DR RefSeq; WP_003705341.1; NC_002946.2. DR RefSeq; YP_208897.1; NC_002946.2. DR ProteinModelPortal; Q5F5Q2; -. DR EnsemblBacteria; AAW90485; AAW90485; NGO_1865. DR GeneID; 3282392; -. DR KEGG; ngo:NGO1865; -. DR PATRIC; 20337424; VBINeiGon24812_2243. DR HOGENOM; HOG000003904; -. DR KO; K04096; -. DR OMA; YPKENKR; -. DR OrthoDB; EOG6DG2TK; -. DR BioCyc; NGON242231:GI2G-1769-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 395 AA; 41853 MW; 6D9B134A17ABF0F5 CRC64; MTEDERFAWL QLAFTPYIGA ESFLLLMRSF GSAQNALSAP AEQVAPAVRH KHALEAWRNA EKRALARQAA EAALEWEMRD GCRLMLLQDE DFPEMLTQGL TAPPVLFLRG NVRLLHKPSA AIVGSRHATP QAMRIAKDFG RALGGKGIPT VSGMASGIDT AAHQGALEAE GGTVAVWGTG IDRIYPPANK NLAYEIAEKG LIVSEFPIGT RPYAGNFPRR NRLIAALSQV TLVVEAALES GSLITAGLAA EMGREVMAVP GSIDNPHSKG CHKLIKDGAK LTECLDDILN ECPGLLQNTG ASSYSINKDT PDTGRRAVQT AYAPPPAAKM PSEGAAGGTA VGGILDKMGF DPVHPDVLAG QLAMPAADLY AALLELELDG SVAAMPGGRY QRIRT // ID A0A0H4IWC8_NEIG1 Unreviewed; 118 AA. AC A0A0H4IWC8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63718.1}; GN ORFNames=NGO_07405 {ECO:0000313|EMBL:AKO63718.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63718.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63718.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63718; AKO63718; NGO_07405. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR028096; EfeO_Cupredoxin. DR Pfam; PF13473; Cupredoxin_1; 1. DR SUPFAM; SSF49503; SSF49503; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 115 Cupredoxin_1. {ECO:0000259|Pfam:PF13473}. SQ SEQUENCE 118 AA; 13164 MW; BC4492A2CF857C50 CRC64; MEQAKKDGVE LEKAAKAVRE GNKVRVYMTA VAPAYSIPQF EVNQGDEVTV YVTNVETIED LTHGFTLEGC GIAMEIGPQA TSSVTFKAVR PGVHWYYCQW FCHALHMEMS GQMIVHPK // ID Q5F7F9_NEIG1 Unreviewed; 257 AA. AC Q5F7F9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 80. DE SubName: Full=DeoR faimly transcriptional regulator {ECO:0000313|EMBL:AAW89878.1}; GN ORFNames=NGO_1219 {ECO:0000313|EMBL:AAW89878.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89878.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89878.1; -; Genomic_DNA. DR RefSeq; WP_003700931.1; NC_002946.2. DR RefSeq; YP_208290.1; NC_002946.2. DR ProteinModelPortal; Q5F7F9; -. DR DNASU; 3281982; -. DR EnsemblBacteria; AAW89878; AAW89878; NGO_1219. DR GeneID; 3281982; -. DR KEGG; ngo:NGO1219; -. DR PATRIC; 20335749; VBINeiGon24812_1433. DR HOGENOM; HOG000224685; -. DR KO; K02444; -. DR OMA; ADRQTRC; -. DR OrthoDB; EOG6XSZXW; -. DR BioCyc; NGON242231:GI2G-1130-MONOMER; -. DR Proteomes; UP000000535; 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; 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; PS51000; HTH_DEOR_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000712, KW ECO:0000256|SAAS:SAAS00589027}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 27961 MW; 895FD8170503E3C9 CRC64; MKPKIQRHGE ILSLVRRHQF MSVDELAAAL DVTPQTIRCD IRELEEGGSL KRHHGGASSG GNLPEGLPAD RQTRCQNEKN AIARLIAEHI PDGSSLFVSI GTTMEAAASE LVKRRSSLRI ITNNIHVASV VSARTDYTVI ITSGVVRPLD GGITGVATVD FINQFKVDYA VMSTHGVESD GSLLDYDYKE VSVMQAMIAN ARVRFLGVDH SKFRSNALVR LGGITAFDKV FTDRLPDTAM QKMLKEAGVE CLIADAV // ID A0A0H4IT43_NEIG1 Unreviewed; 92 AA. AC A0A0H4IT43; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63734.1}; GN ORFNames=NGO_07985 {ECO:0000313|EMBL:AKO63734.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63734.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63734.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63734; AKO63734; NGO_07985. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 74 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 92 AA; 9801 MW; 1907FB6DA7EADEE1 CRC64; MPSEAVSGGI SFGFAPPSDM LNLRPCRPSF ATVSLFDLNG KTMSPPLPPM SGKLMAVLMA VLVALMPFSI DAYLPAIPEM AQPLNADIHR IE // ID Q5F778_NEIG1 Unreviewed; 394 AA. AC Q5F778; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Flavoprotein {ECO:0000313|EMBL:AAW89959.1}; GN ORFNames=NGO_1307 {ECO:0000313|EMBL:AAW89959.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89959.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89959.1; -; Genomic_DNA. DR RefSeq; WP_003691630.1; NC_002946.2. DR RefSeq; YP_208371.1; NC_002946.2. DR ProteinModelPortal; Q5F778; -. DR EnsemblBacteria; AAW89959; AAW89959; NGO_1307. DR GeneID; 3281866; -. DR KEGG; ngo:NGO1307; -. DR PATRIC; 20335975; VBINeiGon24812_1538. DR HOGENOM; HOG000037525; -. DR KO; K13038; -. DR OMA; VRFIGNH; -. DR OrthoDB; EOG6FFSBB; -. DR BioCyc; NGON242231:GI2G-1222-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 130 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 182 364 DFP. {ECO:0000259|Pfam:PF04127}. SQ SEQUENCE 394 AA; 42456 MW; 0FA494E69C26EE6F CRC64; MGKHILLGVT GSIAAYKSCE LVRLLKKQGH SVTVVMSRSA TEFVSPLTFQ ALSGNPVLTD THGGNGSNGM EHINLTRNAD VFLIAPASMN TVAKICNGVA DNLLTNLAAA RKCPLAIAPA MNVEMWLNPA NQRNIAQLVS DGITVYMPGL GEQACRENGM GRMPEPAELL DLLPDLWTPK ILRDKKILIT AGATFEAIDP VRGITNTSSG KMGVALARAC RAAGAEISLI HGQLQTTLPF GISDTVQAVS AEDMHRAVHR LIEKQDAFIS VAAVSDYKVK NRSTQKFKKD KNAKPLSIEL DENPDTLASI ASLPNPPFCI GFAAETENVM AYAREKRIKK KIPVIVANDV SIAMGKTTNQ IVIIDDDAEL SFPETSKDEA AMRIVERLAV YLNK // ID A0A0H4IWJ0_NEIG1 Unreviewed; 141 AA. AC A0A0H4IWJ0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63803.1}; GN ORFNames=NGO_10985 {ECO:0000313|EMBL:AKO63803.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63803.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63803.1; -; Genomic_DNA. DR RefSeq; WP_039080665.1; NC_002946.2. DR RefSeq; YP_009115490.1; NC_002946.2. DR EnsemblBacteria; AKO63803; AKO63803; NGO_10985. DR GeneID; 22847897; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 141 AA; 14983 MW; 1CA9BDD7E279B624 CRC64; MPTDPDSRLR GNDEAILLAE GQKSAVTGYY LNNGKWPADN GAAGVASPAT DIKGKYVKEV KVENGVVTAQ MASTGVNNEI KGKKLSLWAK RQDGSVKWFC GQPVKRDAGA KTGADDVKAD GNNGINTKHL PSTCRDKHDA K // ID Q5F5I6_NEIG1 Unreviewed; 423 AA. AC Q5F5I6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000256|HAMAP-Rule:MF_00138}; GN ORFNames=NGO_1939 {ECO:0000313|EMBL:AAW90551.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90551.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000256|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00138}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00138}; CC Note=Binds 1 magnesium or manganese ion per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00138}; 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:0000256|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|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; AE004969; AAW90551.1; -; Genomic_DNA. DR RefSeq; WP_003705171.1; NC_002946.2. DR RefSeq; YP_208963.1; NC_002946.2. DR ProteinModelPortal; Q5F5I6; -. DR SMR; Q5F5I6; 1-423. DR EnsemblBacteria; AAW90551; AAW90551; NGO_1939. DR GeneID; 3282681; -. DR KEGG; ngo:NGO1939; -. DR PATRIC; 20337621; VBINeiGon24812_2337. DR HOGENOM; HOG000033463; -. DR KO; K01945; -. DR OMA; DYQNFTE; -. DR OrthoDB; EOG69SKD1; -. DR BioCyc; NGON242231:GI2G-1841-MONOMER; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00138}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AAW90551.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00138}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00138}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00138}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00138}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 107 314 ATP-grasp. {ECO:0000256|HAMAP- FT Rule:MF_00138, FT ECO:0000259|PROSITE:PS50975}. FT NP_BIND 133 194 ATP. {ECO:0000256|HAMAP-Rule:MF_00138}. FT METAL 284 284 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00138}. FT METAL 286 286 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00138}. SQ SEQUENCE 423 AA; 45177 MW; 628B4BD89BDDFAB4 CRC64; MKLLVIGNGG REHALAWKLA QSPKVETVFV APGNAGTAIE SKLQNIALTA YQDLIEFCRK ENIVFTVVGP EAPLAAGIVD DFRAAGLKIF GPTQYAAQLE SSKDFAKAFM VKYNIPTAQY QTFENADAAH DYVNQKGAPI VIKADGLVAG KGVIVAMTLD EAHAAIDDML LGNKMGNAGE RVVIEDFLQG EEASFIVMVD GNHVLPMATS QDHKRLLDGD KGPNTGGMGA YSPAPVVTPA VYERAMNEII LPTVAGMKAE GHEFTGFLYA GLMIDQSGAP YTIEFNCRFG DPETQPIMSR LNSDLADLVE AAIDGRLDSV KAEWNPQTAV GVVLAAQNYP ETPKKGDVIS GLDDVNRIGK VFHAGTTVNE KGDVLTNGGR ILCVVGLGDD VAQAKAKAYG ALEKISFDGM QYRKDIADKA INR // ID Q5F967_NEIG1 Unreviewed; 397 AA. AC Q5F967; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=GDSL-like lipase/acylhydrolase family protein {ECO:0000313|EMBL:AAW89270.1}; GN ORFNames=NGO_0532 {ECO:0000313|EMBL:AAW89270.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89270.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89270.1; -; Genomic_DNA. DR RefSeq; WP_003691388.1; NC_002946.2. DR RefSeq; YP_207682.1; NC_002946.2. DR ProteinModelPortal; Q5F967; -. DR EnsemblBacteria; AAW89270; AAW89270; NGO_0532. DR GeneID; 3282916; -. DR KEGG; ngo:NGO0532; -. DR PATRIC; 20334110; VBINeiGon24812_0627. DR HOGENOM; HOG000218984; -. DR OMA; KEQYERR; -. DR OrthoDB; EOG69SK6T; -. DR BioCyc; NGON242231:GI2G-510-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR Gene3D; 3.40.50.1110; -; 2. DR InterPro; IPR013830; SGNH_hydro. DR InterPro; IPR010916; TonB_box_CS. DR Pfam; PF13472; Lipase_GDSL_2; 1. DR SUPFAM; SSF52266; SSF52266; 2. DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89270.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 397 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256081. SQ SEQUENCE 397 AA; 42591 MW; DC281C05F84B9A47 CRC64; MNPKHFIAFS ALFAATQAEA LPVASVSPDT VTVSPSAPYT DTNGLLTDYG NAAASPWMKK LRSVAQGSGE AFRILQIGDS HTAGDFFTDA LRKRLQKTWG DGGIGWVYPA NVKGQRMAAV RHSGNWQSFT SRNNTGDFPL GGILAQTGSG GGMTLTASDG KTGKQRVSLF AKPLLAEQTL TVNGNTVSAN GGGWQVLDTG AALPLAIQTE MPWDIGFINI ENPAGGITVS AMGINGAQLT QWSKWRADRM NDLAQTGADL VILSYGTNEA FNNNIDIADT EQKWLDTVRQ IRDSLPAAGI LIIGAPESLK NTLGVCGTRP VLLTEVQQMQ RRVARQGQTM FWSWQNAMGG ICSMKNWLNQ GWAAKDGVHF SAQGYRRAAE MLADSLEELV RAAAIRQ // ID Q5F5Z3_NEIG1 Unreviewed; 279 AA. AC Q5F5Z3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 91. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAW90394.1}; GN ORFNames=NGO_1775 {ECO:0000313|EMBL:AAW90394.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90394.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90394.1; -; Genomic_DNA. DR RefSeq; WP_003690341.1; NC_002946.2. DR RefSeq; YP_208806.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z3; -. DR EnsemblBacteria; AAW90394; AAW90394; NGO_1775. DR GeneID; 3282533; -. DR KEGG; ngo:NGO1775; -. DR PATRIC; 20337192; VBINeiGon24812_2132. DR HOGENOM; HOG000262939; -. DR OMA; LPNRCPP; -. DR OrthoDB; EOG60SCM3; -. DR BioCyc; NGON242231:GI2G-1673-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 30329 MW; 14DCB77D80BB8EFB CRC64; MTATAADLDR LLPQTQCREC GYEGCLPYAR AMLRGEAHNL CAPGGATVVR DLAALLGKPL VAPAKTQAKA LARIDETACI GCTACIRACP ADAIMGAGKL MHTVITDECT GCGLCVAPCP VDCIHMQPVA DTVLPRARRF SLSDDSRFAA AEHARARYLK RNERKQREAD ERKAMLAERE AAVRNARPQT PDTPEKPAFN PADLIAKAMA KAQTQQDRLA AADNRQGYQA KQIAEARERA ELRRAQRDMK YGSDSEKAAA LEYLKQYKAK QEAAQNTAS // ID Q5F9I0_NEIG1 Unreviewed; 566 AA. AC Q5F9I0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 57. DE SubName: Full=Single-stranded DNA exonuclease {ECO:0000313|EMBL:AAW89157.1}; GN ORFNames=NGO_0414 {ECO:0000313|EMBL:AAW89157.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89157.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89157.1; -; Genomic_DNA. DR RefSeq; WP_003694944.1; NC_002946.2. DR RefSeq; YP_207569.1; NC_002946.2. DR ProteinModelPortal; Q5F9I0; -. DR EnsemblBacteria; AAW89157; AAW89157; NGO_0414. DR GeneID; 3283002; -. DR KEGG; ngo:NGO0414; -. DR PATRIC; 20333839; VBINeiGon24812_0497. DR HOGENOM; HOG000018414; -. DR KO; K07462; -. DR OMA; GKHKKAW; -. DR OrthoDB; EOG63C0P5; -. DR BioCyc; NGON242231:GI2G-392-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Exonuclease {ECO:0000313|EMBL:AAW89157.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89157.1}; KW Nuclease {ECO:0000313|EMBL:AAW89157.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 61927 MW; F2946F9A780996CE CRC64; MSVKIQTRPV NTDVFNHLLA AGADPLIARL CASRGVQSPA ELDDKLASLL PYQSLTNCEA AAGRLADAVE RKEKILIVAD YDADGATACA VGLDGLAAMG AKVDFLVPNR FEHGYGLTPE LAEIAAAQGV DLLITVDNGI ASIAGVARAQ ALGLDVIVTD HHLPADTVPD CIIVNPNQKG CGFPSKSLAG VGVIFYVLTA LRAELRRRNY FSDGIKEPNL GGLLDLVALG TVADVVPLDH NNRILVSQGL KRMRSGKMRP GIRALFEVAR RDWRKAQPFD MGFALGPRIN AAGRLDDMSV GIACLLARDD SEAQELAARL NNLNIERREI EQSMLRDALN AFPETLPSGQ TTLVAYRDDF HQGVVGIVAS RLKDRFYRPT IVFAPADNGE VRGSGRSIPN LHLRDALDLV SKRHPDLILK FGGHAMAAGL SILEHNIPAF QTAFEEAVRE MVCEDDLSQT YITDGSLPAC DITLEQAQNL ACHVWGQGFA PPSFTDEFHV VRQQPLGAEG KHKKAWLQKD GCEFEAMFWR CSEDIPEYIR TVYRPVANEW RNNLELQLYI DYWEAA // ID A0A0H4J614_NEIG1 Unreviewed; 97 AA. AC A0A0H4J614; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63812.1}; GN ORFNames=NGO_11145 {ECO:0000313|EMBL:AKO63812.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63812.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63812.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63812; AKO63812; NGO_11145. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 97 AA; 11194 MW; 46D590D80C0A387D CRC64; MLIRYKDRRA SFRRHSRAGG SPDRLFGKWG GGLRACQIKT VFKRVAMRYM QGLEAQSIYY FHRNGRPRPP CKPLKDKPPG LIRAAVGNHL PLDLFKI // ID Q5F805_NEIG1 Unreviewed; 642 AA. AC Q5F805; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. 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 ORFNames=NGO_0999 {ECO:0000313|EMBL:AAW89682.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89682.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89682.1; -; Genomic_DNA. DR RefSeq; WP_003699819.1; NC_002946.2. DR RefSeq; YP_208094.1; NC_002946.2. DR ProteinModelPortal; Q5F805; -. DR SMR; Q5F805; 394-531, 570-636. DR EnsemblBacteria; AAW89682; AAW89682; NGO_0999. DR GeneID; 3282596; -. DR KEGG; ngo:NGO0999; -. DR PATRIC; 20335200; VBINeiGon24812_1168. DR HOGENOM; HOG000270272; -. DR KO; K03086; -. DR OMA; RDAKKEM; -. DR OrthoDB; EOG6XHC70; -. DR BioCyc; NGON242231:GI2G-925-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 73680 MW; 2485F6ADFC3921F9 CRC64; MSKNQNHEEY QDDARPLTIE EQRARLRQLI IMGKERGYIT YSEINDALPD DMSDADQIDN IVSMISGLGI QVTEHAPDAE DILLSDNAAV TDDDAVEEAE AALSSADSEF GRTTDPVRMY MREMGQVDLL TREDEIIIAK KIENALKNMV QAISACPGSI AEILELIEKI CKDEIRVDEV VEAIIDPNEV LLNELGLGHL ETTAPEKPSN DNSDENEDDE ESEEDADEIS AANLAELKQK VIGHFAQIEK DYKKMIGCLE KHHSRHKDYL AYRDAIANKL LEVRFATRQI DSLSSSLRGK VENIRKLERE IRDICLDRVH MERDYFIQNF LPEITNLQWI EEEIAKGRVW SNALDRFRHA 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 A0A0H4IWJ4_NEIG1 Unreviewed; 140 AA. AC A0A0H4IWJ4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Pilin {ECO:0000313|EMBL:AKO63808.1}; GN ORFNames=NGO_11115 {ECO:0000313|EMBL:AKO63808.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63808.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63808.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63808; AKO63808; NGO_11115. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 14769 MW; ADAFC6DD754CE820 CRC64; MPTDPDSRLR GNDEAILLAE GQKSAVAGYC PNHGKWPANN GDAGVASSAE IKGKYVKSVT VANGVVTAEM ASSGVNKEIK GKRLSLWARR QDGSVKWFCG QPVTRNDAAD NDDVAKDDAA GNAIETKHLP STCRDEPTAT // ID Q5F5M6_NEIG1 Unreviewed; 757 AA. AC Q5F5M6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 68. DE SubName: Full=Transcription accessory protein {ECO:0000313|EMBL:AAW90511.1}; GN ORFNames=NGO_1895 {ECO:0000313|EMBL:AAW90511.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90511.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90511.1; -; Genomic_DNA. DR RefSeq; WP_003690166.1; NC_002946.2. DR RefSeq; YP_208923.1; NC_002946.2. DR ProteinModelPortal; Q5F5M6; -. DR SMR; Q5F5M6; 4-715. DR EnsemblBacteria; AAW90511; AAW90511; NGO_1895. DR GeneID; 3282286; -. DR KEGG; ngo:NGO1895; -. DR PATRIC; 20337494; VBINeiGon24812_2278. DR HOGENOM; HOG000270497; -. DR KO; K06959; -. DR OMA; GFLRIRD; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NGON242231:GI2G-1795-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 640 709 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 757 AA; 83270 MW; 1406FAF17DABD2EA CRC64; MNITRILSQE LSATTVQINA AIELLDDGAT VPFIARYRKE ATGGLDDTQL RQLAERLQYL RELEERKAVV LKSIEEQGKL SDDLRAQIEA ADNKTALEDL YLPYKPKRRT KAQIAHEHGL QPLADVLLAE QPQDVEAAAQ GYLNENIPDA KAALDGARAI LMEQFAEDAE LIGTLRDKLW NEAEIHTQVV EGKETEGEKF SDYFDRREPV RAMPSHRALA VLRGRNEGVL NIALKYQPDD TPITQQSEYE QIIARRFKVS DGHKWLRDTV RLTWRAKIFL SLELEALNRL KEAADTDAIT VFARNLKDLL LAAPAGRLTT LGLDPGYRNG VKCAVVDDTG KLLDTVIVYL HQENNMLATL SRLIKQHGVK LIAIGNGTAS RETDKIAGEL VRGMPESSLH KIVVSEAGAS IYSASELAAR EFPDLDVSLR GAVSIARRLQ DPLAELVKID PKSIGVGQYQ HDVNQSRLAK SLDAVVEDCV NAVGVDANTA SAPLLARISG LNQTLAQNIV AYRDENGAFD SRKKLLKVPR LGEKTFEQAA GFLRINGGKE PLDASAVHPE AYPVVAKMLA QQGITAAELI GNRERVKQIK ASDFTDERFG LPTILDILSE LEKPGRDPRG AFQTASFAEG IHEISDLQVG MILEGVVSNV ANFGAFVDIG VHQDGLVHIS ALSNKFVQDP REVVKAGDVV KVKVLEVDAA RKRIALTMRL DDEPGGAKHK MPSENRSRER TAGRKPQRND RAPTNSAMAD AFAKLKR // ID Q5F6G7_NEIG1 Unreviewed; 245 AA. AC Q5F6G7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 62. DE SubName: Full=Pretoxin HINT domain protein {ECO:0000313|EMBL:AAW90220.1}; GN ORFNames=NGO_1592 {ECO:0000313|EMBL:AAW90220.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90220.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90220.1; -; Genomic_DNA. DR RefSeq; WP_003705657.1; NC_002946.2. DR RefSeq; YP_208632.1; NC_002946.2. DR ProteinModelPortal; Q5F6G7; -. DR EnsemblBacteria; AAW90220; AAW90220; NGO_1592. DR GeneID; 3281715; -. DR KEGG; ngo:NGO1592; -. DR PATRIC; 20336710; VBINeiGon24812_1901. DR HOGENOM; HOG000219103; -. DR OMA; ISPTSNE; -. DR OrthoDB; EOG618QQG; -. DR BioCyc; NGON242231:GI2G-1488-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR002711; HNH. DR InterPro; IPR030934; Intein_C. DR Pfam; PF01844; HNH; 1. DR SUPFAM; SSF51294; SSF51294; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 198 245 HNH. {ECO:0000259|Pfam:PF01844}. SQ SEQUENCE 245 AA; 26875 MW; D19BA894D5111578 CRC64; MVRTADGYKA IAHIQAGDRV LSKDEASGKT GYKPVTAQYG NPYQETVYIK VSDGIGNSQT LISNRIHPFY SDGKWIKAED LKAGNRLFAE SGKTQTVRNI VVKPKPLKAY NLTVADWHTY FVKGNQAETE GVWVHNSCPY GGSNNLEKAK LRAERLSKND RAGKDFTKAG KEAVIDLNRI QNNGQVKCAN CGIETIPAKQ SIKNISPTSN ERQVDHVIPK SKGGQGTPKN GQVLCRGCNI KKSNK // ID A0A0H4J5U8_NEIG1 Unreviewed; 45 AA. AC A0A0H4J5U8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:AKO63732.1}; GN ORFNames=NGO_07840 {ECO:0000313|EMBL:AKO63732.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63732.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63732.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63732; AKO63732; NGO_07840. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR SUPFAM; SSF50249; SSF50249; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AKO63732.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AKO63732.1}. SQ SEQUENCE 45 AA; 4791 MW; 362CBF6A874FB708 CRC64; MATETNIAEI SALDYEGRGV AKVGGKTIFI KGALLDCLML GCFRL // ID Q5F8A2_NEIG1 Unreviewed; 360 AA. AC Q5F8A2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AAW89585.1}; GN ORFNames=NGO_0886 {ECO:0000313|EMBL:AAW89585.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89585.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89585.1; -; Genomic_DNA. DR RefSeq; WP_003706300.1; NC_002946.2. DR RefSeq; YP_207997.1; NC_002946.2. DR ProteinModelPortal; Q5F8A2; -. DR EnsemblBacteria; AAW89585; AAW89585; NGO_0886. DR GeneID; 3281450; -. DR KEGG; ngo:NGO0886; -. DR PATRIC; 20334947; VBINeiGon24812_1043. DR HOGENOM; HOG000102082; -. DR KO; K00257; -. DR OMA; WRESAFV; -. DR OrthoDB; EOG6KMB49; -. DR BioCyc; NGON242231:GI2G-827-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 107 Acyl-CoA_dh_N. FT {ECO:0000259|Pfam:PF02771}. SQ SEQUENCE 360 AA; 38272 MW; BF0FF9F15882F997 CRC64; MNAQTLLANV AELVKTKLKP LVDDIDRKGY YPEAFMRELG AIGAVGIEAE GGNGLGLATR IAVLREIGKE CGATSFSAWC QAACAWYLHQ TPNQAVKDKY LADILQGKVL AGTGMSNTVK HLAGIEKHNL QAECVEGGYT VNGALPWVSN IGEDHIWANT AQIGGGYVMF ITGGQREGVS LQNCPEFCAL EGTHTFSLNF KDVFIPDEDI IAAPEQFAGY IQSIKAGFIL LQIGIGAGVI DGSLGIIRLV NVVNAEVNSY LDDGYDSLKA RLDGAWAETE RLAGLAWDNT PDNLATLKLR EAAAVLALAA AQSAALHSGA KGYLMRSPAQ RRVGEAMFVA IVTPAIKHLC KEIAAIEAAK // ID Q5FA18_NEIG1 Unreviewed; 505 AA. AC Q5FA18; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 73. DE SubName: Full=Fe3+ dicitrate ABC transporter permease {ECO:0000313|EMBL:AAW88969.2}; GN ORFNames=NGO_0216 {ECO:0000313|EMBL:AAW88969.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88969.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88969.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FA18; -. DR EnsemblBacteria; AAW88969; AAW88969; NGO_0216. DR PATRIC; 20333371; VBINeiGon24812_0268. DR HOGENOM; HOG000238612; -. DR OMA; SIHYAND; -. DR OrthoDB; EOG6FFS2H; -. DR BioCyc; NGON242231:GI2G-199-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 53 233 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; 55840 MW; EAC367501FA67ECE CRC64; MSPKKIPIWL TGLILLIALP LTLPFLYVAM RSWQVGINRA VELLFRPRMW DLLSNTLTMM AGVTLISIVL GIACALLFQR YRFFGKTFFQ TAITLPLCIP AFVSCFTWIS LTFRVEGFWG TVMIMSLSSF PLAYLPVEAA LKRISLSYEE VSLSLGKSRL QTFFSAILPQ LKPAIGSSVL LIALHMLVEF GAVSILNYPT FTTAIFQEYE MSYNNNTAAL LSAVLTAVCG IVVFGESIFR GKAKIYHSGK GVARPYPVKT LKLPGQIGAI VFLSSLLILG IIIPFGVLIH WMMVGTSGTF ALVSVFDAFI RSLSVSALGA ILTILCALPL VWASVRYRNF LTVWIDRLPF LLHAVPGLVI ALSLVYFSIN YTPAVYQTFI VVILAYFMLY LPMAQTTLRT SLEQLPKGME QVGATLGRGH FFIFRTLVLP SILPGITAAF ALVFLKLMKE LTATLLLTAD DVHTLSTAVW EYTSDAQYAA ATPYALMLVL FSGIPVFLLK KYAFK // ID Q5F528_NEIG1 Unreviewed; 62 AA. AC Q5F528; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90709.1}; GN ORFNames=NGO_2108 {ECO:0000313|EMBL:AAW90709.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90709.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90709.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90709; AAW90709; NGO_2108. DR BioCyc; NGON242231:GI2G-2003-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 7048 MW; 72B68722DBF835B7 CRC64; MPEIQKTKTE RIGFPFLWDN GMFSRTPPQC LRPAYFPMQN LEKITPSRSS AVNSPVISPH AT // ID Q5F6C9_NEIG1 Unreviewed; 251 AA. AC Q5F6C9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Repressor {ECO:0000313|EMBL:AAW90258.1}; GN ORFNames=NGO_1630 {ECO:0000313|EMBL:AAW90258.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90258.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90258.1; -; Genomic_DNA. DR RefSeq; WP_003693472.1; NC_002946.2. DR RefSeq; YP_208670.1; NC_002946.2. DR ProteinModelPortal; Q5F6C9; -. DR EnsemblBacteria; AAW90258; AAW90258; NGO_1630. DR GeneID; 3281384; -. DR KEGG; ngo:NGO1630; -. DR PATRIC; 20336796; VBINeiGon24812_1943. DR OMA; YREWEIN; -. DR OrthoDB; EOG62NX32; -. DR BioCyc; NGON242231:GI2G-1527-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; 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; PF01381; HTH_3; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 75 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 251 AA; 27896 MW; 4C0F598B7FFD8B0A CRC64; MKKRELNEIE TAECAELKRI FNSKKEELKL TQYKLAEAVG VTQSAVNHYL NGTNALNASI ASQFAKILQI PVSDFSLRLA EEISSMSIGI DGDKLLALQA DNLDTNTITL NLYDVSASCG HGVVNPDYPQ LLRSIEIPND ALFELLGTNN LTNVQLMPPD GDSMEPTIPQ KSITLIKTDV SKFQTGGIYL FTFDGYTYIK RLSRGKGGAI HATSDNRHYA KSDFLINPEE ADKFHIHGKF WKVLPLDFLD L // ID Q5F713_NEIG1 Unreviewed; 155 AA. AC Q5F713; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AAW90024.1}; GN ORFNames=NGO_1376 {ECO:0000313|EMBL:AAW90024.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90024.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90024.1; -; Genomic_DNA. DR RefSeq; WP_003705826.1; NC_002946.2. DR RefSeq; YP_208436.1; NC_002946.2. DR ProteinModelPortal; Q5F713; -. DR SMR; Q5F713; 14-154. DR EnsemblBacteria; AAW90024; AAW90024; NGO_1376. DR GeneID; 3281771; -. DR KEGG; ngo:NGO1376; -. DR PATRIC; 20336141; VBINeiGon24812_1619. DR HOGENOM; HOG000145987; -. DR OMA; DEFPRPM; -. DR OrthoDB; EOG6CGCF5; -. DR BioCyc; NGON242231:GI2G-1289-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 155 AA; 17692 MW; B28339D1F6602A6A CRC64; MPSEHQPQSK GNKMAILKLD EHLYISPQLT KADAEQIAQL GIKTVICNRP DREEESQPDF AQIKQWLEQA GVTGFHHQPV TARDIQKHDV ETFRQLIGQA EYPILAYCRT GTRCSLLWGF RRAAEGMPVD EIIRRAQAAG VNLENFRERL DNARV // ID Q5F7D4_NEIG1 Unreviewed; 143 AA. AC Q5F7D4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. DE SubName: Full=MarR family transcriptional regulator {ECO:0000313|EMBL:AAW89903.1}; GN ORFNames=NGO_1244 {ECO:0000313|EMBL:AAW89903.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89903.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89903.1; -; Genomic_DNA. DR RefSeq; WP_003689706.1; NC_002946.2. DR RefSeq; YP_208315.1; NC_002946.2. DR ProteinModelPortal; Q5F7D4; -. DR EnsemblBacteria; AAW89903; AAW89903; NGO_1244. DR GeneID; 3282613; -. DR KEGG; ngo:NGO1244; -. DR PATRIC; 20335807; VBINeiGon24812_1463. DR HOGENOM; HOG000219033; -. DR OMA; KQICDEW; -. DR OrthoDB; EOG6NGVRR; -. DR BioCyc; NGON242231:GI2G-1156-MONOMER; -. DR Proteomes; UP000000535; 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 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 16305 MW; 8D1D3A725355A1B2 CRC64; MNRLDQLGIR INLICNVFDK WIGQQDLNYN LFTVLYTLAT EGSRTQKHIG EEWSLPKQTV SGVCKTLAGQ GLIEWQEGEQ DRRERLLSLT EKGKVHAAPL TENAQEFSDK VFSTFGDKRT TRLFADLDAL AEVMEKTISE NKK // ID Q5F8T8_NEIG1 Unreviewed; 63 AA. AC Q5F8T8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89399.1}; GN ORFNames=NGO_0672 {ECO:0000313|EMBL:AAW89399.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89399.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89399.1; -; Genomic_DNA. DR RefSeq; WP_010951103.1; NC_002946.2. DR RefSeq; YP_207811.1; NC_002946.2. DR EnsemblBacteria; AAW89399; AAW89399; NGO_0672. DR GeneID; 3282033; -. DR KEGG; ngo:NGO0672; -. DR BioCyc; NGON242231:GI2G-639-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 7154 MW; E2C3EED3D07A7C0E CRC64; MPEIAGNGNP YLVKRRTLCN LSLFFQLFKG GLLESKSAVA ENRHRGIKNK GLYQISRYVT LEI // ID Q5F614_NEIG1 Unreviewed; 483 AA. AC Q5F614; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90373.2}; GN ORFNames=NGO_1752 {ECO:0000313|EMBL:AAW90373.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90373.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90373.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F614; -. DR EnsemblBacteria; AAW90373; AAW90373; NGO_1752. DR PATRIC; 20337108; VBINeiGon24812_2094. DR HOGENOM; HOG000218642; -. DR OMA; WTRVIAS; -. DR OrthoDB; EOG6716J0; -. DR BioCyc; NGON242231:GI2G-1648-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 53481 MW; B529873C0BFA22BF CRC64; MLSFLSGLLS LGIEVLWVRM FSFAAQSVPQ AFSFTLACFL TGIAVGAYFG KRICRSRFVD IPFIGQCFLW AGIADFLILG AAWLLTGFSG FVHHAGIFIT LSAVVRGLIF PLVHHVGTDG NKSGRQVSNV YFANVAGSAL GPVLIGFVIL DFLSTQQIYL LICLISAAVP LFCTLFQKSL RLNAVSVAVS LMFGILMFLL PDSVFQNIAG RPDRLIENKH GIVAVYHRDG DKVVYGANVY DGAYNTDIFN SVNGIERAYL LPSLKSGIRR IFVVGLSTGS WARVLSAIPE MQSMIVAEIN PAYRSLIADE PQIAPLLQDK RVEIVLDDGR KWLRRHPDEK FDLILMNSTW YWRAYSTNLL SAEFLKQVQS HLTPDGIVMF NTTHSPHAFA TAVHSIPYAY RYGHMVVGSA TPVVFPNKEL LKQRLSRLIW PESGRHVFDS STVDAAAQKV VSRMLIRMTE PSAGAEVITD DNMIVEYKYG RGI // ID Q5F7W6_NEIG1 Unreviewed; 268 AA. AC Q5F7W6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000313|EMBL:AAW89721.1}; GN ORFNames=NGO_1049 {ECO:0000313|EMBL:AAW89721.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89721.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89721.1; -; Genomic_DNA. DR RefSeq; WP_003695051.1; NC_002946.2. DR RefSeq; YP_208133.1; NC_002946.2. DR EnsemblBacteria; AAW89721; AAW89721; NGO_1049. DR GeneID; 3281113; -. DR KEGG; ngo:NGO1049; -. DR PATRIC; 20335324; VBINeiGon24812_1228. DR HOGENOM; HOG000219017; -. DR OMA; CEQTQMF; -. DR OrthoDB; EOG622PN0; -. DR BioCyc; NGON242231:GI2G-966-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR019613; DUF4198. DR Pfam; PF10670; DUF4198; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000313|EMBL:AAW89721.1}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256609. SQ SEQUENCE 268 AA; 30134 MW; 1E8585B42DCA421E CRC64; MKKTLTLLAV SALFATSAHP HRVWVETAHT HGGEYLKADL GYGEFPELEP IAKDRLHIFS KPMQLVTEKG KENMIQRGTY NYQYRSNRPV KDGSYLVTAE YQPTFRSKNK AGWKQAGIKE MPDASYCEQT RMFGKNIVNV GHESADTAII TKPVGQNLEI VPLDNPANIH VGERFKVRVL FRGEPLPNAT VTATFDGFDT SDRSKTHKTE AQAFSDTTDG KGEVDIIPLR QGFWKASVEY KADFPDQSLC QKQANYTTLT FQIGHSHH // ID Q5FA68_NEIG1 Unreviewed; 125 AA. AC Q5FA68; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88919.1}; GN ORFNames=NGO_0163 {ECO:0000313|EMBL:AAW88919.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88919.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88919.1; -; Genomic_DNA. DR RefSeq; WP_003690617.1; NC_002946.2. DR RefSeq; YP_207331.1; NC_002946.2. DR EnsemblBacteria; AAW88919; AAW88919; NGO_0163. DR GeneID; 3281366; -. DR KEGG; ngo:NGO0163; -. DR PATRIC; 20333249; VBINeiGon24812_0207. DR HOGENOM; HOG000218878; -. DR OMA; FRNIYRI; -. DR OrthoDB; EOG67T5KM; -. DR BioCyc; NGON242231:GI2G-149-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 125 AA; 14825 MW; 776C74CC56F128AD CRC64; MSFGYLIATS QPCELLTKSR GETFSLIMDK MDLWIYFRFC EGNIYTIRKN ETESCLTERG GEWLKHIYEF NRESFIFSDV LLQKGESEEN FSEIVLKSIK NNKILTVEVR SGLHFDLRNI YRIEM // ID Q5F8N6_NEIG1 Unreviewed; 87 AA. AC Q5F8N6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89451.1}; GN ORFNames=NGO_0732 {ECO:0000313|EMBL:AAW89451.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89451.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89451.1; -; Genomic_DNA. DR RefSeq; WP_003688704.1; NC_002946.2. DR RefSeq; YP_207863.1; NC_002946.2. DR EnsemblBacteria; AAW89451; AAW89451; NGO_0732. DR GeneID; 3282073; -. DR KEGG; ngo:NGO0732; -. DR PATRIC; 20334606; VBINeiGon24812_0875. DR HOGENOM; HOG000027800; -. DR OrthoDB; EOG6ZD6G4; -. DR BioCyc; NGON242231:GI2G-691-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 84 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 87 AA; 9671 MW; 2628B804969A5664 CRC64; MADILPSDKR RQPPKTKGNP INIIEQETKR TELRKIDAEI AKIIADAHKI NAESVKIAQE SRWYPMMAAT GLVTAIAAVL ALIFKFA // ID A0A0H4IRM7_NEIG1 Unreviewed; 209 AA. AC A0A0H4IRM7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=DNA glycosylase {ECO:0000313|EMBL:AKO63611.1}; GN ORFNames=NGO_01470 {ECO:0000313|EMBL:AKO63611.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63611.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63611.1; -; Genomic_DNA. DR RefSeq; WP_010357144.1; NC_002946.2. DR RefSeq; YP_009115479.1; NC_002946.2. DR EnsemblBacteria; AKO63611; AKO63611; NGO_01470. DR GeneID; 22847887; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 209 AA; 23152 MW; DB93DFB727D370C3 CRC64; MSENLLEIET HPFDPVLPPK AAVMMMGTFP PKEDKRAMQF HYPNFQNDMW RVYGLVFFND AAHFRMPSHG EAAHSEKAFD AEKIKAFLHE RGIASCPTVL KAAREHGNAS DKFLKVVETV DLAAVLAKIP DCRHICTTGG KATEILLDIQ GGGIKMPKTG ETVPFPFAGR DLTLTRLPST SRAYPLSLAK KAAAYRAFFE MAGLCEKQL // ID Q5F5X8_NEIG1 Unreviewed; 257 AA. AC Q5F5X8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE SubName: Full=Chromosome partitioning protein {ECO:0000313|EMBL:AAW90409.1}; GN ORFNames=NGO_1790 {ECO:0000313|EMBL:AAW90409.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90409.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90409.1; -; Genomic_DNA. DR RefSeq; WP_004466992.1; NC_002946.2. DR RefSeq; YP_208821.1; NC_002946.2. DR ProteinModelPortal; Q5F5X8; -. DR EnsemblBacteria; AAW90409; AAW90409; NGO_1790. DR GeneID; 3282470; -. DR KEGG; ngo:NGO1790; -. DR PATRIC; 20337226; VBINeiGon24812_2149. DR HOGENOM; HOG000019422; -. DR KO; K03496; -. DR OMA; GVIVPMQ; -. DR OrthoDB; EOG6D8BCX; -. DR BioCyc; NGON242231:GI2G-1688-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 257 AA; 27020 MW; 9FD6D50A90320EF0 CRC64; MSANILAIAN QKGGVGKTTT TVNLAASLAS RGKRVLVVDL DPQGNATTGS GIDKAGLQSG VYQVLLGDAD VQSAAVRSKE GGYGVLGANR ALAGAEIELV QEIAREVRLK NALKAVAEDY DFILIDCPPS LTLLTLNGLV AAGGVIVPML CEYYALEGIS DLIATVRKIR QAVNPDLDIT GIVRTMYDSR SRLVAEVSEQ LRSHFGDLLF ETAIPRNIRL AEAPSHGMPV MAYDAQAKGA KAYLALADEL AARVSGK // ID A0A0H4ISS7_NEIG1 Unreviewed; 152 AA. AC A0A0H4ISS7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Transposase {ECO:0000313|EMBL:AKO63664.1}; GN ORFNames=NGO_04640 {ECO:0000313|EMBL:AKO63664.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63664.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63664.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63664; AKO63664; NGO_04640. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR SUPFAM; SSF48295; SSF48295; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 152 AA; 17477 MW; 2D999B9D114921DB CRC64; MIFVNSLYFS ISDSLVRKWV ARYRLHGESG IKRRKHTTKY SVEYKLEAIR PVTGQGMSQK AAADQLNLPD CSVLPQWLRL YRLNGINGLK PKPKGRKPVK KQYPPQTKKA DYLKTKEELF AELAYLKAEA AVLKKLDALK EVRQKERNSS QG // ID Q5F781_NEIG1 Unreviewed; 217 AA. AC Q5F781; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 48. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89956.1}; GN ORFNames=NGO_1302 {ECO:0000313|EMBL:AAW89956.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89956.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89956.1; -; Genomic_DNA. DR RefSeq; WP_010951236.1; NC_002946.2. DR RefSeq; YP_208368.1; NC_002946.2. DR EnsemblBacteria; AAW89956; AAW89956; NGO_1302. DR GeneID; 3281897; -. DR KEGG; ngo:NGO1302; -. DR PATRIC; 20335951; VBINeiGon24812_1530. DR HOGENOM; HOG000218644; -. DR OMA; IREVICY; -. DR OrthoDB; EOG6GJBXZ; -. DR BioCyc; NGON242231:GI2G-1214-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 217 AA; 24064 MW; F78DF0F8D40F2E67 CRC64; MKITHCKLKK EVQKEPLRSF VPEVTARSAA DILGIHPDSA ALFYRKIRTV TNHRLALAAD EVFEGPAGPG ASCFGGRRKG RRGRGAAGKA VVFGIPKRNG RAYTVAADDA EPETLLPAVK KKIMPDGIVY ADSPGSRGKS DAGGFTRCRI NRSKEFADRR NHINGIGNFW NQAKRALRKY NGIDRKPFPP FLKECEFRLN FGTPSRQLKI LRDWCGI // ID A0A0H4J5D1_NEIG1 Unreviewed; 63 AA. AC A0A0H4J5D1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63612.1}; GN ORFNames=NGO_01505 {ECO:0000313|EMBL:AKO63612.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63612.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63612.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63612; AKO63612; NGO_01505. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 6990 MW; 09658ABF1D9F301F CRC64; MLQQGTAHQA PHCVLPERGC PPIRFYRYKQ TGFNRKGMGI KSISDTSRAM PSENQSPLSD GIV // ID A0A0H4IS59_NEIG1 Unreviewed; 383 AA. AC A0A0H4IS59; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63746.1}; GN ORFNames=NGO_08310 {ECO:0000313|EMBL:AKO63746.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63746.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63746.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63746; AKO63746; NGO_08310. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. 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; IPR005195; Glyco_hydro_65_M. DR InterPro; IPR005196; Glyco_hydro_65_N. DR Pfam; PF03632; Glyco_hydro_65m; 1. DR Pfam; PF03636; Glyco_hydro_65N; 1. DR SUPFAM; SSF48208; SSF48208; 1. DR SUPFAM; SSF74650; SSF74650; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 12 256 Glyco_hydro_65N. FT {ECO:0000259|Pfam:PF03636}. FT DOMAIN 313 380 Glyco_hydro_65m. FT {ECO:0000259|Pfam:PF03632}. SQ SEQUENCE 383 AA; 42773 MW; EDDBADAD81535A6C CRC64; MEISPWTLRS AKLEKEHKRL QESLTSLGNG YMGMRGSFEE TYSADSHLGT YIAGVWFPDK TRVGWWKNGY PKYFGKAINA LNFSKVKIFV DGQEVDLAKN DVAGFSVELD MQHGVLRRSF TVFGVRFDVC KFLSVAQKEL ALTRWEAVSV DGKTHQVRID SIIDADVKNE DSNYEEKFWQ VLDKGVSDDR SYIAAQTVAN PFGVEQFIVN AGQTFAGSFK AFGGSQTDWQ VSNSFEAEVG GTPETFEKRV IVTTSRDYQG LEAVKAAGRA LSEKIAGVAF ETLLDAHKAG WQHRWEIADV VIEGSDEAQQ GIRFNLFQLF STYYGEDARL NIGPKGFTGE KYGGATYWDT EAYAVPLYLA LAEPEVTRNL LQYRRNQIAA GAA // ID Q5FA42_NEIG1 Unreviewed; 311 AA. AC Q5FA42; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464}; GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464}; GN ORFNames=NGO_0190 {ECO:0000313|EMBL:AAW88945.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88945.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88945.1; -; Genomic_DNA. DR RefSeq; WP_003687497.1; NC_002946.2. DR RefSeq; YP_207357.1; NC_002946.2. DR ProteinModelPortal; Q5FA42; -. DR EnsemblBacteria; AAW88945; AAW88945; NGO_0190. DR GeneID; 3281564; -. DR KEGG; ngo:NGO0190; -. DR PATRIC; 20333309; VBINeiGon24812_0237. DR HOGENOM; HOG000245914; -. DR KO; K03074; -. DR OMA; IDMNLEV; -. DR OrthoDB; EOG676Z5R; -. DR BioCyc; NGON242231:GI2G-175-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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 16 36 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; 34402 MW; FD77A8EA4BB1C7AC CRC64; MELFKIKRDI PFMSYGKLTT FISLVTFIAA VFFLVARGLN FSVEFTGGTV MEVQYQQGAD VNKMRERLDT LKMGDVQVQA LGTNKHIMIR LPNKEGVTSA QLSNQVMDLL KKDSPDVTLR QVEFIGPQVG EELVNNGLMA LGFVVIGIII YLSMRFEWRF AVSAIIANMH DIVIILGCFA FFQWEFSLTV LAGILAVLGY SVNESVVVFD RIRENFRKPA MRGHTVPEVI DNAITATMSR TIITHGSTEA MVVSMLVFGG AALHGFSMAL TIGIVFGIYS SVLVASPLLL MFGLSRDNIA KEAKQKEEIV V // ID Q5F7F1_NEIG1 Unreviewed; 468 AA. AC Q5F7F1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181}; GN ORFNames=NGO_1227 {ECO:0000313|EMBL:AAW89886.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89886.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Presumably involved in the processing and regular CC turnover of intracellular proteins. Catalyzes the removal of CC unsubstituted N-terminal amino acids from various peptides. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00345238}. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|- CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino CC acid amides and methyl esters are also readily hydrolyzed, but CC rates on arylamides are exceedingly low. {ECO:0000256|HAMAP- CC Rule:MF_00181, ECO:0000256|SAAS:SAAS00015314}. CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, CC preferentially leucine, but not glutamic or aspartic acids. CC {ECO:0000256|HAMAP-Rule:MF_00181}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181, CC ECO:0000256|SAAS:SAAS00373812}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|HAMAP-Rule:MF_00181, ECO:0000256|SAAS:SAAS00590753}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89886.1; -; Genomic_DNA. DR RefSeq; WP_003689678.1; NC_002946.2. DR RefSeq; YP_208298.1; NC_002946.2. DR ProteinModelPortal; Q5F7F1; -. DR EnsemblBacteria; AAW89886; AAW89886; NGO_1227. DR GeneID; 3282045; -. DR KEGG; ngo:NGO1227; -. DR PATRIC; 20335767; VBINeiGon24812_1442. DR HOGENOM; HOG000243129; -. DR KO; K01255; -. DR OMA; IQQMEIC; -. DR OrthoDB; EOG6FV8B3; -. DR BioCyc; NGON242231:GI2G-1138-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00484934, ECO:0000313|EMBL:AAW89886.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00451174}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00484934, ECO:0000313|EMBL:AAW89886.1}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00445711}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00451152}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00181, KW ECO:0000256|SAAS:SAAS00484934, ECO:0000313|EMBL:AAW89886.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 322 329 CYTOSOL_AP. FT {ECO:0000259|PROSITE:PS00631}. FT ACT_SITE 254 254 {ECO:0000256|HAMAP-Rule:MF_00181}. FT ACT_SITE 328 328 {ECO:0000256|HAMAP-Rule:MF_00181}. FT METAL 242 242 Manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 247 247 Manganese 1. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 247 247 Manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 265 265 Manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 324 324 Manganese 1. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 326 326 Manganese 1. {ECO:0000256|HAMAP- FT Rule:MF_00181}. FT METAL 326 326 Manganese 2. {ECO:0000256|HAMAP- FT Rule:MF_00181}. SQ SEQUENCE 468 AA; 50029 MW; 6BB269B1359AC71A CRC64; MEFSTKTEIL QEQQAGAQLF VCADKAPEHN TAAHALFSAL EEGQNFSDTK IPTDNGLQAV AVVRLEKTDR AALNKAAAEA AKWAQNQETV NVDVHAFDEA QAAAVAEAFA IAFGNAAYRF DRYKKEAKPA KFSQAVFHSA HEAAVKEALR VAEAQVYGQS LCRDLGNAAP NECTPEFLAR TAKAEAEKLG AHAKIIEKDY IKENMGSFWS VAKGSVEDPY LVELSYFGAA DKEAAPVVLV GKGITFDTGG ISLKPGLNMD EMKFDMCGAA TVISTFCAAV KLQLPINLIA IVATCENMPS GAANKPGDVV KSMKGLTIEV LNTDAEGRLI LCDALTYAEQ FKPKAVIDVA TLTGACIVAL GHDVSGVMGN NQDLIDSLLA ASYNVDDKAW QLPLFETYKD QLKSNFADIP NIGTPGAGTI TAATFLSYFT EGYPWAHLDI AGTAWKSGAE KGATGRPVPL LMNYLRNL // ID A0A0H4IRL0_NEIG1 Unreviewed; 75 AA. AC A0A0H4IRL0; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63596.1}; GN ORFNames=NGO_00655 {ECO:0000313|EMBL:AKO63596.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63596.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63596.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63596; AKO63596; NGO_00655. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 63 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 75 AA; 9321 MW; F186EE44FBFC067F CRC64; MKNWKQFIFF VILVIACYQV LYFLSDMFLL DYINKYSWNL NFIQGTLNFF SIYLPYVFVS RIFRNTNQEK EYKND // ID Q5F5R9_NEIG1 Unreviewed; 329 AA. AC Q5F5R9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90468.2}; GN ORFNames=NGO_1847 {ECO:0000313|EMBL:AAW90468.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90468.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90468.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90468; AAW90468; NGO_1847. DR PATRIC; 20337370; VBINeiGon24812_2220. DR HOGENOM; HOG000289917; -. DR OMA; WIKSEDS; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NGON242231:GI2G-1748-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 72 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 329 AA; 38426 MW; A925561F37972145 CRC64; MCRRFAMQCR LKFLKARQAA MFEAADLYRE LLSERPDLVY PRFDLGVMLF EDKQYREALV QLHRAEEVLP PDMRQLAREY IRQAEAVQAW HPSFNMNYEQ TDNVNNASLS RDIVINGRKW IKSEDSLPKR ANGIRYELGV DRMFNMAGNH FARLGISGSG VHYWNARDFS EQAFHAEVGY RYRNSRLEWG FRPFVKQNRL GNNRYTANTG IVLDYSRRLN EKWRSTQSFQ YGRKQYHDEY LAKRYNSKTI SVSGTFSYYA MSAWQLYGGI SGMFDNTVEK EQASRRYGVS LGTVKILDGG LGLKLGAGYT KRIFKAPATL IYNFTRRDD // ID Q5F8L4_NEIG1 Unreviewed; 230 AA. AC Q5F8L4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461}; DE EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461}; GN ORFNames=NGO_0758 {ECO:0000313|EMBL:AAW89473.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89473.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89473.1; -; Genomic_DNA. DR RefSeq; WP_010951116.1; NC_002946.2. DR RefSeq; YP_207885.1; NC_002946.2. DR ProteinModelPortal; Q5F8L4; -. DR EnsemblBacteria; AAW89473; AAW89473; NGO_0758. DR GeneID; 3281868; -. DR KEGG; ngo:NGO0758; -. DR PATRIC; 20334664; VBINeiGon24812_0904. DR HOGENOM; HOG000259349; -. DR KO; K01783; -. DR OMA; GANYITF; -. DR OrthoDB; EOG67HK17; -. DR BioCyc; NGON242231:GI2G-713-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|PIRNR:PIRNR001461}; KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 230 AA; 24760 MW; 1E5B0344A62D6258 CRC64; MTAYRIAPSI LSADFARLGE EVANVIAAGA DLIHFDVMDN HYVPNLTFGP MVCAALKPYA SVPIDVHLMV EPVDDLIQSF AKAGASIITF HPEASRHIDR SLSLIRDMGC QAGLVLNPAT PVYVLENVLD RLDMVLLMSV NPGFGGQSFI PHTLEKIRQV RAMLDRYEGK SGRRIAIEVD GGIKTDNIAA VARAGADTFV AGSAIFGKPD YKAVIAAMRA ELEKAARAEP // ID Q5F766_NEIG1 Unreviewed; 553 AA. AC Q5F766; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Paraquat-inducible protein B {ECO:0000313|EMBL:AAW89971.1}; GN ORFNames=NGO_1320 {ECO:0000313|EMBL:AAW89971.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89971.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89971.1; -; Genomic_DNA. DR RefSeq; WP_003693803.1; NC_002946.2. DR RefSeq; YP_208383.1; NC_002946.2. DR EnsemblBacteria; AAW89971; AAW89971; NGO_1320. DR GeneID; 3281932; -. DR KEGG; ngo:NGO1320; -. DR PATRIC; 20336005; VBINeiGon24812_1553. DR HOGENOM; HOG000256423; -. DR KO; K06192; -. DR OMA; HHVEIKA; -. DR OrthoDB; EOG69WFM1; -. DR BioCyc; NGON242231:GI2G-1234-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 60481 MW; C4094E8106174EF1 CRC64; MTDNSPPPNG HAQARVRKNN TFLSAVWLVP LIALIAGGWL WVKEIRNRGP VVTLLMDSAE GIEVNNTVIK VLSIDVGRVT RIKLRDDQKG VEVTAQLNAD VSGLIRSDTQ FWVVKPRIDQ SGVTGLGTLL SGSYIAFTPG KSGEAKDVFQ VQDIPPVTAI GQSGLRLNLI GKNDRILNVN SPVLYENFMV GQIESAHFDP SDQSVHYTIF IQSPNDKLIH SASRFWLESG INIETTGSGI KLNSAPLPAL LSGAISFDSP KTKNSKNVKS EDSFTLYDSR SEIANLPDDR SLYYTAFFKQ SVRGLTVGSP VEYKGLNVGM VSDVPYFDRN DSLHLFENGW IPVRIRIEPS RLEINADEQS KEHWKQQFQT ALNKGLTATI SSNNLLTGGK MIELNDQPSA SPKLRPHTVY AGDTVIATRG GGLDDLQVKL ADLLDKFNNL PLDKTVAELN GSLAELKSAL KSANAALSSI DKLVGNPQTQ NIPNELNQTL KELRITLQGV SPQSPIYGDV QNTLQSLDKT LKDVQPVINT LKEKPNALIF NNSSKDPIPK GSR // ID Q5F4X2_NEIG1 Unreviewed; 175 AA. AC Q5F4X2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE SubName: Full=Phosphoribosyltransferase {ECO:0000313|EMBL:AAW90765.1}; GN ORFNames=NGO_2172 {ECO:0000313|EMBL:AAW90765.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90765.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90765.1; -; Genomic_DNA. DR RefSeq; WP_010951420.1; NC_002946.2. DR RefSeq; YP_209177.1; NC_002946.2. DR ProteinModelPortal; Q5F4X2; -. DR EnsemblBacteria; AAW90765; AAW90765; NGO_2172. DR GeneID; 3282753; -. DR KEGG; ngo:NGO2172; -. DR PATRIC; 20338206; VBINeiGon24812_2625. DR HOGENOM; HOG000170387; -. DR OMA; RTQWLGP; -. DR OrthoDB; EOG6H1Q23; -. DR BioCyc; NGON242231:GI2G-2059-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Glycosyltransferase {ECO:0000313|EMBL:AAW90765.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90765.1}. FT DOMAIN 14 131 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 175 AA; 19952 MW; A2FA8C501F631011 CRC64; MKQKIWYTYD DIHRVIKALA EKIRNAGVKY DAMIAIGGGG FIPARMLRCF LEIPIYAVTT AYYDSDSEGQ VTEEVKKVQW LDPVPEVLRG KNVLVVDEVD DSRVTMEFCL KELLKEDFDT VGVAVLHEKI KAKAGKIPEG IPYFSGITVE DWWINYPWDA LDIDEHNRLA EADRG // ID Q5F7L5_NEIG1 Unreviewed; 284 AA. AC Q5F7L5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89822.1}; GN ORFNames=NGO_1156 {ECO:0000313|EMBL:AAW89822.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89822.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89822.1; -; Genomic_DNA. DR RefSeq; WP_003705520.1; NC_002946.2. DR RefSeq; YP_208234.1; NC_002946.2. DR ProteinModelPortal; Q5F7L5; -. DR EnsemblBacteria; AAW89822; AAW89822; NGO_1156. DR GeneID; 3282207; -. DR KEGG; ngo:NGO1156; -. DR PATRIC; 20335581; VBINeiGon24812_1355. DR HOGENOM; HOG000071329; -. DR OMA; GSEGTHI; -. DR OrthoDB; EOG65QWDB; -. DR BioCyc; NGON242231:GI2G-1068-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 2.160.20.20; -; 1. DR InterPro; IPR012332; P22_tailspike_C-like. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR InterPro; IPR004899; Pertactin_central. DR Pfam; PF03212; Pertactin; 1. DR SUPFAM; SSF51126; SSF51126; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 109 Pertactin. {ECO:0000259|Pfam:PF03212}. SQ SEQUENCE 284 AA; 31433 MW; F3A4A071312CB68E CRC64; MSNGARWTVT NDSMLKELDL SEDAQVEFSD NNKFVKVSVS KLKGDGGVFK MYGDIVKGES DKLITRKGSE GTHIIEYMDD AKAKTTGREY LKLVENKGNQ EDNKASNKAS YKLNVRCTEQ GGWCFALGES GASKKVNIST DGKRDFYLYP DTLTPGASSS VLFGEALYQL NAVSDETLVQ RMGEIHADGM PQEDNNVWIK RVGGKFSGSR SDYRVGGYGN RYWGFAGGFN RTGFGDKWIH YKGLMLRHLQ SSYASEDYVG SGKILRQGGR CLFRLAQPGK QGLL // ID Q5F6Z9_NEIG1 Unreviewed; 117 AA. AC Q5F6Z9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90038.1}; GN ORFNames=NGO_1390 {ECO:0000313|EMBL:AAW90038.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90038.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90038.1; -; Genomic_DNA. DR RefSeq; WP_002216461.1; NC_002946.2. DR RefSeq; YP_208450.1; NC_002946.2. DR EnsemblBacteria; AAW90038; AAW90038; NGO_1390. DR GeneID; 3281310; -. DR KEGG; ngo:NGO1390; -. DR PATRIC; 20336173; VBINeiGon24812_1635. DR HOGENOM; HOG000296623; -. DR OMA; HTRENGS; -. DR OrthoDB; EOG6TN47X; -. DR BioCyc; NGON242231:GI2G-1303-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 117 AA; 13707 MW; 88D3768B99C7DA92 CRC64; MGIKNEQIII CKKYNTEIYP VSDVSKIGVA ENVKQTGLYP INGLRHRPKG DTNGWYIWAG ENFSYDKNFF LPLHTFHLQI WRPEIIPFLT LPPGYRFLIG ENGYEDVWFD ELLLNDN // ID Q5F7Y7_NEIG1 Unreviewed; 391 AA. AC Q5F7Y7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=2-nitropropane dioxygenase {ECO:0000313|EMBL:AAW89700.1}; GN ORFNames=NGO_1024 {ECO:0000313|EMBL:AAW89700.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89700.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89700.1; -; Genomic_DNA. DR RefSeq; WP_003691002.1; NC_002946.2. DR RefSeq; YP_208112.1; NC_002946.2. DR ProteinModelPortal; Q5F7Y7; -. DR EnsemblBacteria; AAW89700; AAW89700; NGO_1024. DR GeneID; 3282094; -. DR KEGG; ngo:NGO1024; -. DR PATRIC; 20335260; VBINeiGon24812_1196. DR HOGENOM; HOG000123286; -. DR KO; K00459; -. DR OMA; SNCVSPC; -. DR OrthoDB; EOG6C013S; -. DR BioCyc; NGON242231:GI2G-945-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Dioxygenase {ECO:0000313|EMBL:AAW89700.1}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89700.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 334 NMO. {ECO:0000259|Pfam:PF03060}. SQ SEQUENCE 391 AA; 41954 MW; 60E30F960196B23B CRC64; MQNIFDPLII RGKSLIPIVQ GGMGVGVSAS GLSSAVAREN GIGTIASVDL RHLHEDLLAE SQINPSEEKY TSLNCTALDR EIQKAKSASE GKGLIAVNVM KAVKDHAAYV RQACESGADA VVMGAGLPLD LPEMTEGYHK DVALLPILSE SRGINIVLKR WMKKGILPDA IVVEHPAHAA GHLGASTVEG VNDAKFDFKR VIEETFEVFK NLGLEGEKIP LILAGGMANF EKVKTALKNW GASAVQIGTA FAVTEEGDAH LNFKKTLASA ETEKVVEFMS VAGLPARGIR TKFLDSYIRR EGKLQANAKA DPRRCTQGLN CLTSCGLRDG LSKAGQFCID IQLAAAFRGE VDKGLFFRGK DQLPFGNAIR TVRETIQYLL TGSEPVATLG R // ID Q5F7X7_NEIG1 Unreviewed; 114 AA. AC Q5F7X7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89710.1}; GN ORFNames=NGO_1034 {ECO:0000313|EMBL:AAW89710.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89710.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89710.1; -; Genomic_DNA. DR RefSeq; WP_003693394.1; NC_002946.2. DR RefSeq; YP_208122.1; NC_002946.2. DR EnsemblBacteria; AAW89710; AAW89710; NGO_1034. DR GeneID; 3281669; -. DR KEGG; ngo:NGO1034; -. DR PATRIC; 20335288; VBINeiGon24812_1210. DR HOGENOM; HOG000071266; -. DR OMA; MIASNAK; -. DR OrthoDB; EOG66XBNP; -. DR BioCyc; NGON242231:GI2G-955-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 114 AA; 12340 MW; BA07C2C1E7107309 CRC64; MIASNAKNRA QNPSAAYRPA LFGQTLILPP SRTLVQTGTD DTARAFPVFT GYPSSGLCSS TISALRFSGG SRRKYSGLNL NRYGVASPCR TGLNLIHYIL RPLQNSLPSR QLKP // ID Q5F5A2_NEIG1 Unreviewed; 309 AA. AC Q5F5A2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 77. DE SubName: Full=LysR family transcriptional regulator {ECO:0000313|EMBL:AAW90635.1}; GN ORFNames=NGO_2027 {ECO:0000313|EMBL:AAW90635.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90635.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90635.1; -; Genomic_DNA. DR RefSeq; WP_003686949.1; NC_002946.2. DR RefSeq; YP_209047.1; NC_002946.2. DR ProteinModelPortal; Q5F5A2; -. DR EnsemblBacteria; AAW90635; AAW90635; NGO_2027. DR GeneID; 3282720; -. DR KEGG; ngo:NGO2027; -. DR PATRIC; 20337837; VBINeiGon24812_2442. DR HOGENOM; HOG000218906; -. DR KO; K03576; -. DR OMA; ACEHLPF; -. DR OrthoDB; EOG64BQ3T; -. DR BioCyc; NGON242231:GI2G-1928-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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}. SQ SEQUENCE 309 AA; 34813 MW; 67370C8890DAF82A CRC64; MDSIIELRHL KTLLALEETG SVSLAAKRVF LTQSALSHQI RMLENHYGTP LFERKSTPLR FTPVGERLLR LAHELIPQVA VAERDLARIT EGEAGELRIA VECHTCFDWL MPAMGEFRPM WPQVELDIVS GFQADPVGLL LQHRADLAIV SEAEKQSSIS FHPLFAYEMV GICAPDHPLA AKNVWTAEDF IGETLITYPV PDEMLDLPKK ILIPKNINPP RRHSELTIAI IQLVASRRGI AALPYWTVMP YLEKGYVVHR QITADGLQSK LYAAIRTEDT DKSYLNNFCQ IIRERGFADL PGLSELEPV // ID Q5F5N8_NEIG1 Unreviewed; 78 AA. AC Q5F5N8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90499.1}; GN ORFNames=NGO_18781 {ECO:0000313|EMBL:AAW90499.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90499.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90499.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90499; AAW90499; NGO_18781. DR PATRIC; 20337454; VBINeiGon24812_2258. DR HOGENOM; HOG000218673; -. DR OrthoDB; EOG6CGCJQ; -. DR BioCyc; NGON242231:GI2G-1783-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 70 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 78 AA; 9205 MW; 53FB1DC159520952 CRC64; MIMGVLIFFL IVPILGFICA TINYFIINKF KLPKYMAYLL PSLSILFIFI HAIKLHMILF FYVSCVYSAY TYYDKKSL // ID Q5F811_NEIG1 Unreviewed; 206 AA. AC Q5F811; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Diadenosine tetraphosphatase {ECO:0000313|EMBL:AAW89676.1}; GN ORFNames=NGO_0992 {ECO:0000313|EMBL:AAW89676.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89676.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89676.1; -; Genomic_DNA. DR RefSeq; WP_003688277.1; NC_002946.2. DR RefSeq; YP_208088.1; NC_002946.2. DR EnsemblBacteria; AAW89676; AAW89676; NGO_0992. DR GeneID; 3281206; -. DR KEGG; ngo:NGO0992; -. DR PATRIC; 20335188; VBINeiGon24812_1162. DR HOGENOM; HOG000219025; -. DR OMA; FCPEDIP; -. DR OrthoDB; EOG6CCH4G; -. DR BioCyc; NGON242231:GI2G-919-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR019722; G6PD_bac. DR Pfam; PF10786; G6PD_bact; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 206 AA; 24442 MW; 5945B026AA8B51E2 CRC64; MLTPKSCDLF NIPFFQFAQL KKYQPESIPQ IKADYKENWQ IWQQLIQQVA ADLSEPFAPP HIERWCNGWQ VRAHFFAYFK YAQYKNSAAI LSILLNRRRL SVSLDWHCYK ADVSPIALPE YNRWLDDFDT EKYAAFDMWH GAESEYDDYR TVAQQSESDR RLQNDEDFFC IGKHIERDDL GKQDVAKWIA ETVEDLLPLY EACHGK // ID Q5F6T0_NEIG1 Unreviewed; 407 AA. AC Q5F6T0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 74. DE SubName: Full=Chloride channel protein {ECO:0000313|EMBL:AAW90107.2}; GN ORFNames=NGO_1467 {ECO:0000313|EMBL:AAW90107.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90107.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90107.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6T0; -. DR EnsemblBacteria; AAW90107; AAW90107; NGO_1467. DR PATRIC; 20336367; VBINeiGon24812_1732. DR HOGENOM; HOG000184895; -. DR OMA; IQHVAYG; -. DR OrthoDB; EOG6F81SB; -. DR BioCyc; NGON242231:GI2G-1372-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00438323, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 98 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 175 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 205 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 236 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 257 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 308 341 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 375 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 400 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 407 AA; 42851 MW; DA30C55AC0647034 CRC64; MGRRKLWFAL AAAGVIGGLV GIVLTELMHF IRHTAYGYDA DGAYISFREG VAQAFGMRRV AMLTLCGAIA GGGWWLLKRF GKPQIEIKAA LKQPLQGLPF LTTVFHVLLQ IITVGLGSPL GREVAPREMT AAFAFAGGRR LGLDEGEMRL LIACASGAGL AAVYNVPLAS TLFILEAMLG VWTQQAVAAA LLTSVIATAV ARIGLGDVQQ YHPANLAVNT SLLWFSAVIG PILGATAAFF RRTAQKFPFI KRDNIKIIPL AVCMFALIGV IAVWFPEILG NGKAGNQLTF GGLTGWQYSL ELTAVKWAVV LMALAAGAYG GLITPSMMLG STISFAAAAA WNSVFPEMPS ESAAVVGAAV FLGVSLKMPL TAIVFVLELT YAPLSLLLPL CIGMAGVLGT SGKMGFK // ID Q5FAJ1_NEIG1 Unreviewed; 367 AA. AC Q5FAJ1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. 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 ORFNames=NGO_0002 {ECO:0000313|EMBL:AAW88775.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88775.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88775.1; -; Genomic_DNA. DR RefSeq; WP_010950967.1; NC_002946.2. DR RefSeq; YP_207187.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ1; -. DR EnsemblBacteria; AAW88775; AAW88775; NGO_0002. DR GeneID; 3283050; -. DR KEGG; ngo:NGO0002; -. DR PATRIC; 20332832; VBINeiGon24812_0002. DR HOGENOM; HOG000071791; -. DR KO; K02338; -. DR OMA; THQIRLK; -. DR OrthoDB; EOG65J53F; -. DR BioCyc; NGON242231:GI2G-2-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 40869 MW; E820FA027B587475 CRC64; MLILQAERDS LLKPLQAFTG IVERLHTLPI LSNVLIEGRG GQTKLLATDL EIQIDTAGPE GGAGDFRITT NAKKFQDILR ALPAGALVSL DWDDNRLTLK AGKSRFALQT LPAADFPMMN VGEDISATFS LGQERFKTML SQVQYSMAVQ DIRYYLNGLL MQVEGSQLRL VATDGHRLAY AACAIDADLP RAEVILPRKT VLELFKLLNN PDDPIQIELL DKQVRFQCNG TTIVSKVIDG KFPDFNRVIP LDNDKIFVLS RAELLGALER VSILANEKFR GARLFLQPGL LSVVCSNNEQ EEAREEIEIA YQGGELEVGF NIGYLMDVLR NIHSDDMQLA FGDANRSTLF TVPNNPNFKY IVMPMRI // ID A0A0H4IVF3_NEIG1 Unreviewed; 395 AA. AC A0A0H4IVF3; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63720.1}; GN ORFNames=NGO_07415 {ECO:0000313|EMBL:AKO63720.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63720.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63720.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63720; AKO63720; NGO_07415. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR Pfam; PF12801; Fer4_5; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 83 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 115 142 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 274 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 298 328 4Fe-4S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51379}. SQ SEQUENCE 395 AA; 45092 MW; CF94B3560F5D51AC CRC64; MVQRVLSVND KAFVTADLDY ELPQAYYVDD PKAPPVEISA PVEAVPAAAS DTASDGIAED ASAENGVSNQ LWKQIWKAKQ GQIVVVGIAL TILLLVFLFQ DWIVRYEKWY DRFRFAFLTF TLFYIGWYAQ AQLSVVNTLT LFSAILTEFH WEFFLMDPIV FILWLFTAAT MLLWNRGTFC GWLCPFGSLQ ELTNRIAKKL GVKQITVPHM LHTRLNVIKY LILFGFLAIS LYDLGTAEKF AEVEPFKTAI ILKFMCDWWF VAFAVALLIA GLFIERFFCR YLCPLGAGIA LPGRFRVFDW LRRYKMCGNP CQICTHECPV QAIAPEGDIH PNECIQCLHC QVMYHHDTRC PQVVAENKKK QKQAAAKSGE LENVSKQPQE QVVRFVKPET AQSEK // ID Q5F900_NEIG1 Unreviewed; 221 AA. AC Q5F900; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 53. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AAW89337.1}; GN ORFNames=NGO_0609 {ECO:0000313|EMBL:AAW89337.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89337.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89337.1; -; Genomic_DNA. DR RefSeq; WP_003688928.1; NC_002946.2. DR RefSeq; YP_207749.1; NC_002946.2. DR ProteinModelPortal; Q5F900; -. DR DNASU; 3281753; -. DR EnsemblBacteria; AAW89337; AAW89337; NGO_0609. DR GeneID; 3281753; -. DR KEGG; ngo:NGO0609; -. DR PATRIC; 20334298; VBINeiGon24812_0721. DR HOGENOM; HOG000258627; -. DR OMA; IGQIRFW; -. DR OrthoDB; EOG67X1R0; -. DR BioCyc; NGON242231:GI2G-577-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89337.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89337.1}. SQ SEQUENCE 221 AA; 24866 MW; 286B5902F572A1DE CRC64; MDAWFEDTAM GRYVAKLEQD FFNRYVASYR FSGMCAVQVG GQWLSLSEDI VCVPRDMSMS AENMALADVF ADMLLLPHTL ECGVPSQILS EAHRILKPSG RLMLTGFNPY SLWGFCRWFD GVRLPEKRFC LPLPELKRQL ADAGFDIEFG KFMVYLPPVS SLGQIRFWRF MEKAGDRWWP QCAAVYGLVL VKRAAGVTPL PAWDGYWGGK ALAAGAARVA D // ID Q5F970_NEIG1 Unreviewed; 675 AA. AC Q5F970; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 61. DE SubName: Full=Transporter {ECO:0000313|EMBL:AAW89267.2}; GN ORFNames=NGO_0529 {ECO:0000313|EMBL:AAW89267.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89267.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89267.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F970; -. DR EnsemblBacteria; AAW89267; AAW89267; NGO_0529. DR PATRIC; 20334104; VBINeiGon24812_0624. DR HOGENOM; HOG000053241; -. DR OMA; DDWLKIN; -. DR OrthoDB; EOG6D8B89; -. DR BioCyc; NGON242231:GI2G-507-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00492880, KW ECO:0000256|SAAS:SAAS00492882, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 76254 MW; E7B37E565E22263F CRC64; MSLSEFIERR TSFNPMVILT TLFFVCVLVV LVLTVPDQVQ MWLDRAKEVI FTEFSWFYVL TFSIFLGFLL ILSVSGLGNI RLGRDEDVPE FGFLSWLAML FAAGMGVGLM FFGVAEPLMH YFSDITVGAP EHRQQQALLH TVFHWGVHAW SVYGTIALAL AYFGFRYKLP LALRSCFYPL LKEKISGRFG DAIDIMALLA TFFGIITTLG FGASQLGAGL QEMGWIAENS FGVQVLIIAA VMSLAVVSAI SGVGKGVKVL SELNLGLAFL LLFFVLAADP TVYLLSAFGD NIGNYLGNLV RLSLKTYAYE REHKPWFESW TVLYWAWWCS WAPFVGLFIA RISKGRTIRE FVFGVLLIPG LFGVLWFTVF GNTAIWLNDG VAGGMLEKMT SSPETLLFKF FNYLPLPELT SIVSLLVISL FFVTSADSGI YVLNNITSRD KGLSAPRWQA VMWGVLMSAV AVLLMRSGGL GNLQSMTLIV SLPFALLMLI MCFSLWKGLS ADKKYFETRV NPTSVFWTGG KWKERLVRIM SQTQEQDILK FLKHTASPAM HELQRELSEE YGLSVRVDKM FHQDEPAIEF VIRKETMRDF MYGIKSVGQD VSDQLINDGK LPHIRHQTTY KPYAYFFDGR VGYDVQYMNK DELIADILKN YERYLMLLDD VGQELMAHEQ VELAE // ID A0A0H4IVN2_NEIG1 Unreviewed; 129 AA. AC A0A0H4IVN2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63815.1}; GN ORFNames=NGO_11165 {ECO:0000313|EMBL:AKO63815.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63815.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63815.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63815; AKO63815; NGO_11165. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 129 AA; 13870 MW; DE164876081D9189 CRC64; MAEGQKSAVT EYYLNHGEWP KDNGSAGVAS ASKIIGKYVK EVKVENGVVT AQMASSNVNK EIKDKKLSLW AKRENGSVKW FCGQPVKRTE ANAKAGTDDV AKDDTAGTKI DTKHLPSTCR DESSLPGIA // ID Q5F932_NEIG1 Unreviewed; 491 AA. AC Q5F932; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 67. DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:AAW89305.1}; GN ORFNames=NGO_0572 {ECO:0000313|EMBL:AAW89305.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89305.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89305.1; -; Genomic_DNA. DR RefSeq; WP_003688980.1; NC_002946.2. DR RefSeq; YP_207717.1; NC_002946.2. DR ProteinModelPortal; Q5F932; -. DR EnsemblBacteria; AAW89305; AAW89305; NGO_0572. DR GeneID; 3282525; -. DR KEGG; ngo:NGO0572; -. DR PATRIC; 20334208; VBINeiGon24812_0676. DR HOGENOM; HOG000038764; -. DR KO; K03797; -. DR OMA; RGEPNTK; -. DR OrthoDB; EOG6PS5W5; -. DR BioCyc; NGON242231:GI2G-545-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU004404}; KW Protease {ECO:0000256|RuleBase:RU004404}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Serine protease {ECO:0000256|RuleBase:RU004404}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 491 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255556. FT DOMAIN 93 161 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 491 AA; 52735 MW; E22583E914F0C49C CRC64; MSKPVFKKIA LYTLGAISGV AVSLAVQGFA AEKDGRDNEV LPVQSIRTMA EVYGQIKANY YHDKPDADLF EGAMKGMVAG LDPHSEYMDK KGYAEIKEST SGEFGGLGME IGQEDGFVKV VSPIEDTPAE RAEVKSGDFI VKIDNVSTRG MTVSEAVKKM RGKPGTKITL TLSRKNADKP IVVNLTRAII KVKSVRHHLI EPDYGYIRVS QFQERTVESV NTAAKELVKE NKGKPLKGLV LDLRDDPGGL LTGAVGVSAA FLPSEAVVVS TKGRDGKDGM VLKAVPEDYV YGMGGDPLAG IPAELKTIPM TVLVNSGSAS ASEIVAGALQ DHKRAVIVGT QSFGKGSVQT LIPLSNGSAV KLTTALYYTP NDRSIQAQGI VPDVEVKDKE RTFESREADL VGHIGNPLGG EDVNSETLAV PLEKDADKPA AKEKGKKKKD EDLSSRRIPN PAKDDQLRKA LDLVKSPEQW QKSLGLAAKK PVSNKDKKDK K // ID A0A0H4J5J1_NEIG1 Unreviewed; 110 AA. AC A0A0H4J5J1; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63662.1}; GN ORFNames=NGO_04530 {ECO:0000313|EMBL:AKO63662.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63662.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63662.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63662; AKO63662; NGO_04530. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 110 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005206333. FT COILED 47 74 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 110 AA; 11718 MW; 8DB1BF87ECECC3CE CRC64; MKNLKNISVV AVCAVLLAAC ASENSVANYA IGDDSAVIKA GRNRAEARIS RAELAQHRRQ RKNVSEELAL EREKRANKHD AIRQGMGTAA GGLMLLNGVV GTVGVMKSVF // ID Q5FA65_NEIG1 Unreviewed; 288 AA. AC Q5FA65; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Meta-pathway of phenol degradation family protein {ECO:0000313|EMBL:AAW88922.1}; GN ORFNames=NGO_0166 {ECO:0000313|EMBL:AAW88922.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88922.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88922.1; -; Genomic_DNA. DR RefSeq; WP_003696729.1; NC_002946.2. DR RefSeq; YP_207334.1; NC_002946.2. DR ProteinModelPortal; Q5FA65; -. DR EnsemblBacteria; AAW88922; AAW88922; NGO_0166. DR GeneID; 3281383; -. DR KEGG; ngo:NGO0166; -. DR PATRIC; 20333255; VBINeiGon24812_0210. DR HOGENOM; HOG000218890; -. DR OMA; KAGNYWM; -. DR OrthoDB; EOG6SNDQS; -. DR BioCyc; NGON242231:GI2G-152-MONOMER; -. DR Proteomes; UP000000535; 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 SUPFAM; SSF56925; SSF56925; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 288 AA; 31431 MW; 97A518A1BD50E792 CRC64; MKNILLVFVS FVPLCVRTDL PLNIEDIMTD KGKWKLETSL TYLNSENSRA ALASPVYIQT GSASFIPVPT EIQENGSNTD MLAGTLGLRY GLTGNTDIYG SGSYLWHEER KLDGNGKTRN KRMSDISAGI SHTFLKDGKN PALIAFLEST VYEKSRNKAS SGKSWLIGAT TYKAIDPIVL SLTAAYRING SKTLSDDVKY KAGNYWMLNP NISFAANDRI SLTGGIQWLG KQPDRIDGKK ESARNTSTYA HFGAGFGFTK TAALNASARF NVSGQSSSEL KLGVQHTF // ID Q5F7F6_NEIG1 Unreviewed; 140 AA. AC Q5F7F6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 57. DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:AAW89881.2}; GN ORFNames=NGO_1222 {ECO:0000313|EMBL:AAW89881.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89881.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89881.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7F6; -. DR EnsemblBacteria; AAW89881; AAW89881; NGO_1222. DR PATRIC; 20335757; VBINeiGon24812_1437. DR HOGENOM; HOG000256281; -. DR OMA; GPRPMEM; -. DR OrthoDB; EOG6R2H4J; -. DR BioCyc; NGON242231:GI2G-1133-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 14935 MW; 24748610588C75CC CRC64; MQVTSKWIDG MCFVGTAEGG HSVVMEGSAA EGAAKRGPSP LEMLLLGVAG CSSIDVVMIA EKQRQKVTDC RATVTAKRAD DAPRVFTEIH IHFKVIGHDL KESAIERAVQ MSAEKYCSAS IMLGKAAKIT HSFEIAGAEK // ID Q5F6F5_NEIG1 Unreviewed; 80 AA. AC Q5F6F5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90232.1}; GN ORFNames=NGO_1604 {ECO:0000313|EMBL:AAW90232.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90232.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90232.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90232; AAW90232; NGO_1604. DR PATRIC; 20336744; VBINeiGon24812_1918. DR HOGENOM; HOG000071214; -. DR OMA; EMPSELR; -. DR OrthoDB; EOG6NKR85; -. DR BioCyc; NGON242231:GI2G-1500-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 8835 MW; FFE561DAA46F931E CRC64; MEMPSELRFG RHMFSGSYSG LNLNRYGVTP PCRTMLYCLR LRRFVLIFVN PLTCPTAAKT MSCMAGICGA GLLPKTAGKK // ID Q5F8X2_NEIG1 Unreviewed; 76 AA. AC Q5F8X2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89365.1}; GN ORFNames=NGO_0638 {ECO:0000313|EMBL:AAW89365.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89365.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89365.1; -; Genomic_DNA. DR RefSeq; WP_003691301.1; NC_002946.2. DR RefSeq; YP_207777.1; NC_002946.2. DR EnsemblBacteria; AAW89365; AAW89365; NGO_0638. DR GeneID; 3281789; -. DR KEGG; ngo:NGO0638; -. DR PATRIC; 20334360; VBINeiGon24812_0752. DR HOGENOM; HOG000027835; -. DR OrthoDB; EOG6G7R75; -. DR BioCyc; NGON242231:GI2G-605-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 56 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 76 AA; 8858 MW; C50891D00702864D CRC64; MVVVARVGFF IVGGIVQYLS VSVKYGGAVA DCLFKWRYSL ILLYLFGFLN QLVMFFEERR LGRFAGKRFQ NDLIYF // ID Q5FAC1_NEIG1 Unreviewed; 282 AA. AC Q5FAC1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Lauroyl acyltransferase {ECO:0000313|EMBL:AAW88866.2}; GN ORFNames=NGO_0105 {ECO:0000313|EMBL:AAW88866.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88866.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88866.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88866; AAW88866; NGO_0105. DR PATRIC; 20333109; VBINeiGon24812_0138. DR HOGENOM; HOG000265961; -. DR OMA; CCERLPD; -. DR OrthoDB; EOG6V4G92; -. DR BioCyc; NGON242231:GI2G-95-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR004960; LipA_acyltrans. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAW88866.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000313|EMBL:AAW88866.2}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 282 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364420. SQ SEQUENCE 282 AA; 31441 MW; 909C0E69E6844D40 CRC64; MHILLTALLK CLSLLSLSCL HTLGNRLGHL AFYLLKEDRA RIVANMRQAG LNPDTQTVKA VFAETAKCGL ELAPAFFKKP EDIETMFKAV HGWEHVQQAL DKGEGLLFIT PHIGSYDLGG RYISQQLPFH LTAMYKPPKI KAIDKIMQAG RVRGKGKTAP TGIQGVKQII KALRAGEATI ILPDHVPSPQ EGGGVWADFF GKPAYTMTLA AKLAHVKGVK TLFFCCERLP DGQGFVLHIR PVQGELNGNK AHDAAVFNRN TEYWIRRFPT QYLFMYNRYK TP // ID Q5F4Y4_NEIG1 Unreviewed; 280 AA. AC Q5F4Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Lacto-N-neotetraose biosynthesis glycosyl transferase {ECO:0000313|EMBL:AAW90753.1}; GN ORFNames=NGO_2159 {ECO:0000313|EMBL:AAW90753.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90753.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90753.1; -; Genomic_DNA. DR RefSeq; WP_010359715.1; NC_002946.2. DR RefSeq; YP_209165.1; NC_002946.2. DR CAZy; GT25; Glycosyltransferase Family 25. DR EnsemblBacteria; AAW90753; AAW90753; NGO_2159. DR GeneID; 3282765; -. DR KEGG; ngo:NGO2159; -. DR PATRIC; 20338172; VBINeiGon24812_2608. DR HOGENOM; HOG000218751; -. DR KO; K07270; -. DR OMA; KDREQGR; -. DR OrthoDB; EOG6R5C54; -. DR BioCyc; NGON242231:GI2G-2047-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90753.1}. SQ SEQUENCE 280 AA; 32433 MW; 14F096AB0F964BCF CRC64; MQNHVISLAS AAERRAHIAA TFGSRGIPFQ FFDALMPSER LEQAMAELVP GLSAHPYLSG VEKACFMSHA VLWKQALDEG LPYIAVFEDD VLLGKDAEKF LAEDTWLEER FDKDSAFIVR LETMFAKVIV RPDKVLNYEN RSFPLLESEH CGTAGYIISR EAMRFFLDRF AVLPPERIKA VDLMMFTYFF DKEGMPVYQV SPALCTQELH YAKFLSQNSM LGSDLEKDRE QGRRHRRSLK VMFDLKRALG KFGREKKKRM ERQRQAELEK VYGRRVILFK // ID Q5F687_NEIG1 Unreviewed; 324 AA. AC Q5F687; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 65. DE SubName: Full=Octaprenyl diphosphate synthase {ECO:0000313|EMBL:AAW90300.1}; GN ORFNames=NGO_1675 {ECO:0000313|EMBL:AAW90300.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90300.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90300.1; -; Genomic_DNA. DR RefSeq; WP_003689819.1; NC_002946.2. DR RefSeq; YP_208712.1; NC_002946.2. DR ProteinModelPortal; Q5F687; -. DR EnsemblBacteria; AAW90300; AAW90300; NGO_1675. DR GeneID; 3281251; -. DR KEGG; ngo:NGO1675; -. DR PATRIC; 20336904; VBINeiGon24812_1996. DR HOGENOM; HOG000009102; -. DR KO; K02523; -. DR OMA; NIYITIN; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; NGON242231:GI2G-1570-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU004466}. SQ SEQUENCE 324 AA; 35414 MW; 3907835CFF7DD761 CRC64; MLENLPYFQR HLPEDLAKVN EVINRAVQSD VALISQIGTY IISAGGKRLR PIMTILAGKA VGYDDEKLYS LAAMVEFIHT STLLHDDVVD ESDLRRGRAT ANNLFGNAAA VLVGDFLYTR AFQLMVASGS MRVLEVMADA TNIIAEGEVM QLMNIGNTDI TEEQYIRVIQ YKTAKLFEAA AQVGAILGKA SPGHEQALKD YGMYVGTAFQ IIDDVLDYSG ETEETGKNVG DDLAEGKPTL PLIYLMRQGS EQVANDVRTA LENADRGYFE KIRDYVVRSD ALAYSIGEAR KAVDCAVAAL DALSDSEVKD AMIQLAKESL VRVS // ID Q5F6N7_NEIG1 Unreviewed; 291 AA. AC Q5F6N7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90150.1}; GN ORFNames=NGO_1512 {ECO:0000313|EMBL:AAW90150.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90150.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90150.1; -; Genomic_DNA. DR RefSeq; WP_003693582.1; NC_002946.2. DR RefSeq; YP_208562.1; NC_002946.2. DR EnsemblBacteria; AAW90150; AAW90150; NGO_1512. DR GeneID; 3281508; -. DR KEGG; ngo:NGO1512; -. DR PATRIC; 20336500; VBINeiGon24812_1798. DR HOGENOM; HOG000219095; -. DR OMA; TMFYQIL; -. DR OrthoDB; EOG6M0T4B; -. DR BioCyc; NGON242231:GI2G-1416-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 143 275 EamA. {ECO:0000259|Pfam:PF00892}. SQ SEQUENCE 291 AA; 30885 MW; 0D16D5B07E2F8DC9 CRC64; MFYQILALII WGSSFIAAKY VYGGIDPALM VGVRLLIAAL PALPACRRHV GKIPREEWKP LLIVSFVNYV LTLLLQFVGL KYTSAASASV IVGLEPLLMV FVGHFFFNDK ARAYHWICGA AAFAGVALLM AGGAEEGGEV GWFGCLLVLL AGAGFCAAMR PTQRLIARIG APAFTSVSIA AASLMCLPFS LALAQSYTVD WSVGMVLSLL YLGLGCGWYA YWLWNKGMSR VPANASGLLI SLEPVVGVLL AVLILGEHLS PVSALGVFVV IAATFAAGRL SRRDAQNGNA V // ID Q5F7F5_NEIG1 Unreviewed; 223 AA. AC Q5F7F5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89882.1}; GN ORFNames=NGO_1223 {ECO:0000313|EMBL:AAW89882.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89882.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89882.1; -; Genomic_DNA. DR RefSeq; WP_003689669.1; NC_002946.2. DR RefSeq; YP_208294.1; NC_002946.2. DR EnsemblBacteria; AAW89882; AAW89882; NGO_1223. DR GeneID; 3281863; -. DR KEGG; ngo:NGO1223; -. DR PATRIC; 20335759; VBINeiGon24812_1438. DR HOGENOM; HOG000219031; -. DR OMA; YNIKYSS; -. DR OrthoDB; EOG62NX3T; -. DR BioCyc; NGON242231:GI2G-1134-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR021457; DUF3108. DR Pfam; PF11306; DUF3108; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256050. SQ SEQUENCE 223 AA; 24103 MW; 6BBDD24E2035F90A CRC64; MMKTFKNIFS AAILSAALPC AYAARLPQSA VLHYSGSYGI PATMTFERSG NAYKIVSTIK VPLYNIRFES GGTVVGNTLH PAYYKDIRRG KLYAEAKFAD GSVTYGKAGE SKTEQSPKAM DLFTLAWQLA ANDAKLPPGL KITNGKKLYS VGGLNKAGTG KYSIGGVETE VVKYRVRRGD DTVTYFFAPS LNNIPAQIGY TDDGKTYTLK LKSVQINGQA AKP // ID Q5F8E0_NEIG1 Unreviewed; 222 AA. AC Q5F8E0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Phosphoserine phosphatase {ECO:0000313|EMBL:AAW89547.1}; GN ORFNames=NGO_0842 {ECO:0000313|EMBL:AAW89547.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89547.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89547.1; -; Genomic_DNA. DR RefSeq; WP_003688561.1; NC_002946.2. DR RefSeq; YP_207959.1; NC_002946.2. DR ProteinModelPortal; Q5F8E0; -. DR DNASU; 3282880; -. DR EnsemblBacteria; AAW89547; AAW89547; NGO_0842. DR GeneID; 3282880; -. DR KEGG; ngo:NGO0842; -. DR PATRIC; 20334850; VBINeiGon24812_0995. DR HOGENOM; HOG000250087; -. DR OMA; ATNRFIT; -. DR OrthoDB; EOG61ZTM8; -. DR BioCyc; NGON242231:GI2G-789-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 222 AA; 25311 MW; DA706CDB38F5D057 CRC64; MKNLAIFDLD NTLINTDSDH AWPQYLIKKG LVDAAETEAQ NEKFYRDYQN GCLDIDAFLK LHLAPLARYS KEELAEFHRE FMAEYIIPHI SPMQRMLVQS HQMAGDETLV ISSTNEFIIT PVCRLFGIAN MIGTQLETGP DGRYTGNYIG TPSLKEGKIT RLNQWLAERG ETLESYGKTY FYSDSKNDLP LLRLVSEPVA VNPDAELEKE AKEKGWPVLN FK // ID Q5F951_NEIG1 Unreviewed; 291 AA. AC Q5F951; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89286.1}; GN ORFNames=NGO_0552 {ECO:0000313|EMBL:AAW89286.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89286.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89286.1; -; Genomic_DNA. DR RefSeq; WP_003689009.1; NC_002946.2. DR RefSeq; YP_207698.1; NC_002946.2. DR EnsemblBacteria; AAW89286; AAW89286; NGO_0552. DR GeneID; 3282119; -. DR KEGG; ngo:NGO0552; -. DR PATRIC; 20334156; VBINeiGon24812_0650. DR HOGENOM; HOG000218978; -. DR OMA; FNYITAI; -. DR OrthoDB; EOG6BW4ZJ; -. DR BioCyc; NGON242231:GI2G-526-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 116 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 145 169 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 264 282 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 291 AA; 30991 MW; 6C1BF1BBCFFA99F6 CRC64; MAYLLISIVF SVSVSILLKM ARKKKIDIAQ AVAVNYVVAV ILTLSVLKPD VGNIGAFLPT WPLFAALGVL LPSVFVIMGK SVESAGIVKS DAAQRLSLFL PIVAALTLFG EKLSEGKLIG LCLAFAALFC LLWKSDSGKK SGSAWRQALL LLGVWAGYGI IDILFKQIAK SGTAFAGNLL VAFALAGVLM FACLFAKSVR WRVESVVGGI LLGGLNFMNI VTYITAHQMM KDSPTLVFAG MNIGVIVLGT LSGALFFKEK INTINTAGIV LSLCSIACLF YWTEVKALFG I // ID Q5F6E1_NEIG1 Unreviewed; 163 AA. AC Q5F6E1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90246.1}; GN ORFNames=NGO_1618 {ECO:0000313|EMBL:AAW90246.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90246.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90246.1; -; Genomic_DNA. DR RefSeq; WP_004464807.1; NC_002946.2. DR RefSeq; YP_208658.1; NC_002946.2. DR EnsemblBacteria; AAW90246; AAW90246; NGO_1618. DR GeneID; 3281324; -. DR KEGG; ngo:NGO1618; -. DR PATRIC; 20336776; VBINeiGon24812_1933. DR HOGENOM; HOG000071216; -. DR OMA; EEHIGRM; -. DR OrthoDB; EOG6HQSQB; -. DR BioCyc; NGON242231:GI2G-1515-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008840; Sipho_Gp157. DR Pfam; PF05565; Sipho_Gp157; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 163 AA; 18232 MW; 36BE670456C7CEB6 CRC64; MTALTLYRCA ADVQAALDYY FDSETEREDT LEAVIGQFEV KAQSVIAYIK NQEITEKMLE GHIRQMTGKL KAAKARNQSL KDYLARNMQA AGITEIKADD GTFKASFRKS EAVVILDEAQ IPAEFMREAV KTEPDKTAIR KAIESGRQVA GAKIEGRKNL QIR // ID Q5FAA8_NEIG1 Unreviewed; 97 AA. AC Q5FAA8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Peptide ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW88879.1}; GN ORFNames=NGO_0119 {ECO:0000313|EMBL:AAW88879.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88879.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88879.1; -; Genomic_DNA. DR RefSeq; WP_003702280.1; NC_002946.2. DR RefSeq; YP_207291.1; NC_002946.2. DR EnsemblBacteria; AAW88879; AAW88879; NGO_0119. DR GeneID; 3282406; -. DR KEGG; ngo:NGO0119; -. DR PATRIC; 20333141; VBINeiGon24812_0154. DR HOGENOM; HOG000218783; -. DR OMA; VGFRAYG; -. DR OrthoDB; EOG63NMKT; -. DR BioCyc; NGON242231:GI2G-108-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 97 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256092. SQ SEQUENCE 97 AA; 10582 MW; 60C9B75B72EDF4E9 CRC64; MKTLVLLLLS FSTTTAFAAY GLGLGQAPKY PVGFRAYGYV YSGRQGWVLK TEADAIKLDT LFKRFVYRPS AANQNPVGQA VGQRSDGIPA NHTKEKP // ID Q5F5M2_NEIG1 Unreviewed; 672 AA. AC Q5F5M2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Peptide transporter {ECO:0000313|EMBL:AAW90515.1}; GN ORFNames=NGO_1900 {ECO:0000313|EMBL:AAW90515.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90515.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90515.1; -; Genomic_DNA. DR RefSeq; WP_010951366.1; NC_002946.2. DR RefSeq; YP_208927.1; NC_002946.2. DR EnsemblBacteria; AAW90515; AAW90515; NGO_1900. DR GeneID; 3282305; -. DR KEGG; ngo:NGO1900; -. DR PATRIC; 20337504; VBINeiGon24812_2283. DR HOGENOM; HOG000060682; -. DR OMA; FMTANLY; -. DR OrthoDB; EOG67DPKN; -. DR BioCyc; NGON242231:GI2G-1799-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 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; 70272 MW; F0C10FE9CDF734A0 CRC64; MNKSLSGSVE KYRELTLRGM ILGALITVIF TASNVYLGLK VGLTFASSIP AAVISMAVLK FFKGSNILEN NMVQTQASAA GTLSTIIFVL PGLLMAGYWS GFPFWQTTLL CIAGGILGVI FTIPLRYAMV VKSDLPYPEG VAAAEILKVG GHEEGDDRQG GSGIKELAAG GALAGLMSFC SGGLRVIADS ASYWFKSGTA IFQLPIGFSL ALLGAGYLVG LTGGIAILLG ISIAWGIAVP YFSSHIPQPS DMEMAAFAMK LWKEKVRFIG AGTIGIAAVW TLLMLLKPMV EGMKMSFKSF GGGAPATERA EQDLSPKAMI FWVLSMMFIL GVSFYHFIGD SHITGGMAWL LVAVCTLLAS VIGFLVAAAC GYMAGLVGSS SSPISGVGIV SIVVISLVLL LVGESGGLLA DEANRKFLLA LTLFCGSAVI CVASISNDNL QDLKTGYLLK ATPWRQQVAL IIGCIVGALV ISPVLELLYE AYGFTGAMPR EGMDAAQALA ALQATLMTTI ASGIFAHNLE WAYIFTGIAI GAVLIVVDLV LKKSSGGKLA LPVLAVGMGI YLPPSVNMPI VAGAVLAAVL KHIIGKKAEN REGRLKNADR IGTLFAAGLI VGESLIGVIM AFIIAFSVTN GGSDAPLALN LQNWDAAASW LGLAFFVTGM FFFAQRVLKA GR // ID Q5F7F8_NEIG1 Unreviewed; 300 AA. AC Q5F7F8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89879.1}; GN ORFNames=NGO_1220 {ECO:0000313|EMBL:AAW89879.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89879.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89879.1; -; Genomic_DNA. DR RefSeq; WP_003706734.1; NC_002946.2. DR RefSeq; YP_208291.1; NC_002946.2. DR DNASU; 3281998; -. DR EnsemblBacteria; AAW89879; AAW89879; NGO_1220. DR GeneID; 3281998; -. DR KEGG; ngo:NGO1220; -. DR PATRIC; 20335751; VBINeiGon24812_1434. DR HOGENOM; HOG000275902; -. DR OMA; MLFIFAP; -. DR OrthoDB; EOG6N3CR6; -. DR BioCyc; NGON242231:GI2G-1131-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 50 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 149 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 170 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 226 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 296 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 300 AA; 31612 MW; 5F6047077CD1C7BF CRC64; MSSLMTLFSV LVPMFAGFFI RVPKPYLPAS DKVLSVLVYA VLLLIGVSLS RVEDLGSRLG DMALTVLWLF VCTVGANLLA LAVLGKLSPW RIGGKGKGVS VGVSGSVRQL GCVLLGFVSG KLMCDIWMPS ENAGMYCLML LVFLIGVQLK SSGVSLRQVL LNRRGIRLSV WFILSSLSGG LLFAASADGV SWTKGLAMAS GFGWYSLSGL VMTEAYGAVW GSIMLLNDLA RELFALAFIP LLMKRFPDAA VGVGGATSMD FTLPVIQGAG GLEVVPVAVS FGVVVNIAAP FLMVVFSTLG // ID Q5FA87_NEIG1 Unreviewed; 407 AA. AC Q5FA87; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 76. DE SubName: Full=Major facilitator transporter {ECO:0000313|EMBL:AAW88900.2}; GN ORFNames=NGO_0142 {ECO:0000313|EMBL:AAW88900.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88900.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88900.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FA87; -. DR EnsemblBacteria; AAW88900; AAW88900; NGO_0142. DR PATRIC; 20333195; VBINeiGon24812_0180. DR HOGENOM; HOG000267862; -. DR OMA; FESCIFP; -. DR OrthoDB; EOG661H8H; -. DR BioCyc; NGON242231:GI2G-130-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 71 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 78 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 121 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 197 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 253 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 265 283 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 295 314 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 320 343 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 355 375 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 381 403 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 12 407 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 407 AA; 43177 MW; 77313E6F0196BA62 CRC64; MSAQSQNNHT SPLVVLTTLF FMMGFITCMN DILIPHLKEI FDLSYVQAML IQFCFFTAYA VMSIPMGAFV GKVGYKNGVI GGFLLTAVGC LLFYPAAGSH SYAVFLGALF ILASGVTLLQ VAGNPYVTLL AKPGKESATL TLVQAFNALG TTIAPQIGAF LILADATQTV SKAEQISSVQ IPYLGLAGLL IILAVFVKMI RLPDARKIAA EESAHNHDGK TGVWQYKHLV FGTAGIFCYV GAEVSIGSLM VNVLGYLKGL DHASAAHYLS FYWGGAMVGR FLGSAVMAKF APNRYLAFNA SAAVVLLAVA MATGSGNADV AMWSLLAIGF FNSIMFPTIF SLATKGLGKF TNAASGVLCT AIVGGAVVPV IQGWAADTYT LMSSFVVSVI CYLYIVFFAV YGYRADK // ID Q5F9L8_NEIG1 Unreviewed; 460 AA. AC Q5F9L8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 74. DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AAW89119.1}; GN ORFNames=NGO_0375 {ECO:0000313|EMBL:AAW89119.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89119.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00551227}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89119.1; -; Genomic_DNA. DR RefSeq; WP_003690828.1; NC_002946.2. DR RefSeq; YP_207531.1; NC_002946.2. DR ProteinModelPortal; Q5F9L8; -. DR SMR; Q5F9L8; 3-452. DR EnsemblBacteria; AAW89119; AAW89119; NGO_0375. DR GeneID; 3281907; -. DR KEGG; ngo:NGO0375; -. DR PATRIC; 20333753; VBINeiGon24812_0454. DR HOGENOM; HOG000268679; -. DR KO; K01835; -. DR OMA; AWFNLRA; -. DR OrthoDB; EOG6W9X55; -. DR BioCyc; NGON242231:GI2G-354-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016868; F:intramolecular transferase activity, phosphotransferases; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Magnesium {ECO:0000256|RuleBase:RU004326, KW ECO:0000256|SAAS:SAAS00436074}; KW Metal-binding {ECO:0000256|RuleBase:RU004326, KW ECO:0000256|SAAS:SAAS00436123}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 136 PGM_PMM_I. {ECO:0000259|Pfam:PF02878}. FT DOMAIN 155 252 PGM_PMM_II. {ECO:0000259|Pfam:PF02879}. FT DOMAIN 257 365 PGM_PMM_III. {ECO:0000259|Pfam:PF02880}. FT DOMAIN 372 450 PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}. SQ SEQUENCE 460 AA; 49436 MW; F41B2834F034972D CRC64; MASITRDIFK AYDIRGIVGK TLTDDAAYFI GRAIAAKAAE KGIARIAIGR DGRLSGPELM EHIQRGLTDS GIGVLNVGMV TTPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT LAGEAIQELL AIVEKDGFVA ADKQGSVTEK DISGAYHDHI VGHVKLKRPI NIAIDAGNGV GGAFAGKLYK GLGNEVTELF CEVDGNFPNH HPDPSKPENL QDLIAALKNG DAEIGLAFDG DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGEAIM EKTGHSFIKS AMKKTGALVA GEMSGHVFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL DNLPQSISTP ELNISLPEGS NGHQVIEELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA SNTTPILVLR FEADTQAAIE RIQNRFKAVI ESNPHLIWPL // ID A0A0H4IT54_NEIG1 Unreviewed; 98 AA. AC A0A0H4IT54; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 3. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63749.1}; GN ORFNames=NGO_08330 {ECO:0000313|EMBL:AKO63749.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63749.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63749.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63749; AKO63749; NGO_08330. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR020846; MFS_dom. DR SUPFAM; SSF103473; SSF103473; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 98 AA; 10608 MW; D0AB58116DBBF706 CRC64; MSEYTPQTAK QGLPAPAKST IWMLSFGYLG VQTAFTLQSS QMSRIFQTLG ADPHNLGWFF ILPPLAGMLV QPIVATTQTA LGSRAWAAAA CRICFTAR // ID Q5FA44_NEIG1 Unreviewed; 88 AA. AC Q5FA44; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 56. DE SubName: Full=Preprotein translocase subunit YajC {ECO:0000313|EMBL:AAW88943.1}; GN ORFNames=NGO_0188 {ECO:0000313|EMBL:AAW88943.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88943.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88943.1; -; Genomic_DNA. DR RefSeq; WP_003687494.1; NC_002946.2. DR RefSeq; YP_207355.1; NC_002946.2. DR ProteinModelPortal; Q5FA44; -. DR EnsemblBacteria; AAW88943; AAW88943; NGO_0188. DR GeneID; 3281554; -. DR KEGG; ngo:NGO0188; -. DR PATRIC; 20333305; VBINeiGon24812_0235. DR HOGENOM; HOG000018859; -. DR KO; K03210; -. DR OMA; ADGQAQN; -. DR OrthoDB; EOG6WQDDS; -. DR BioCyc; NGON242231:GI2G-173-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 9681 MW; 1193056C81A8FDE6 CRC64; MNQAVAQFAP LVLIMVVFYF LIMRPQQKKF KAHQAMLAAL KAGDKVVLAA GFKGKVTRVG EQFFTVDIGQ GTKIEVEVER NAIAAKVD // ID A0A0H4IWG8_NEIG1 Unreviewed; 47 AA. AC A0A0H4IWG8; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63778.1}; GN ORFNames=NGO_09900 {ECO:0000313|EMBL:AKO63778.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63778.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63778.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63778; AKO63778; NGO_09900. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 47 AA; 5553 MW; 25B5762F4F54C250 CRC64; MSKTVGIVRF NRNCPTQTVV LKHIARLLVR CLFRLPRWWD IVLVSCL // ID Q5F5Y2_NEIG1 Unreviewed; 330 AA. AC Q5F5Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00086154}; DE EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00086154}; DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536}; GN Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536}; GN ORFNames=NGO_1786 {ECO:0000313|EMBL:AAW90405.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90405.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00536, ECO:0000256|SAAS:SAAS00086189}. CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino- CC 2-oxopropyl phosphate + CO(2) + NADH. {ECO:0000256|HAMAP- CC Rule:MF_00536, ECO:0000256|SAAS:SAAS00086180}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00536}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00536}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00086172}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00086146}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536, CC ECO:0000256|SAAS:SAAS00086193}. CC -!- MISCELLANEOUS: The active site is located at the dimer interface. CC {ECO:0000256|HAMAP-Rule:MF_00536}. CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP- CC Rule:MF_00536, ECO:0000256|SAAS:SAAS00570486}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90405.1; -; Genomic_DNA. DR RefSeq; WP_010951346.1; NC_002946.2. DR RefSeq; YP_208817.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y2; -. DR SMR; Q5F5Y2; 1-328. DR EnsemblBacteria; AAW90405; AAW90405; NGO_1786. DR GeneID; 3282475; -. DR KEGG; ngo:NGO1786; -. DR PATRIC; 20337216; VBINeiGon24812_2144. DR HOGENOM; HOG000221592; -. DR KO; K00097; -. DR OMA; YVWDTPL; -. DR OrthoDB; EOG6GN6ZC; -. DR BioCyc; NGON242231:GI2G-1684-MONOMER; -. DR UniPathway; UPA00244; UER00312. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00536}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00459911}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00536}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00459879}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00459869}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00459894}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00459893}; KW Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536, KW ECO:0000256|SAAS:SAAS00459912}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00536}. FT METAL 167 167 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT METAL 212 212 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT METAL 267 267 Divalent metal cation; shared with FT dimeric partner. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT BINDING 137 137 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT BINDING 138 138 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT BINDING 275 275 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT BINDING 284 284 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00536}. FT BINDING 293 293 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_00536}. SQ SEQUENCE 330 AA; 34501 MW; BF938A26D670D334 CRC64; MKQPVFAVTS GEPAGIGPDI CLDLAFARLP CRCAVLGDKH LLRARAEALG KSVVLRDFDP ESGGAHGEGG LEVLHIPAAE AVEAGWLNPA NAAYVLQLLD AALAGISDGI FDGIVTAPLH KGIINAARAS TGFFSGHTEY LAEKSGTGQV VMMLAGKGLR VALVTTHLPL KDVAAAITQP LIESVARILH HDLKHKFGIK NPKILVAGLN PHAGEGGHLG HEETDTIIPA LENLRREGIN LAGPYPADTL FQPFMLEGAD AVLAMYHDQG LPVLKYHSFG QGVNITLGLP FIRTSVDHGT ALDLAATGRA DSGSLITAVE TAVEMARGSL // ID Q5F579_NEIG1 Unreviewed; 421 AA. AC Q5F579; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Peroxidase {ECO:0000313|EMBL:AAW90658.1}; GN ORFNames=NGO_2051 {ECO:0000313|EMBL:AAW90658.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90658.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90658.1; -; Genomic_DNA. DR RefSeq; WP_010951393.1; NC_002946.2. DR RefSeq; YP_209070.1; NC_002946.2. DR ProteinModelPortal; Q5F579; -. DR EnsemblBacteria; AAW90658; AAW90658; NGO_2051. DR GeneID; 3282852; -. DR KEGG; ngo:NGO2051; -. DR PATRIC; 20337901; VBINeiGon24812_2473. DR HOGENOM; HOG000236941; -. DR KO; K16301; -. DR OMA; VERWDRT; -. DR OrthoDB; EOG6F55G9; -. DR BioCyc; NGON242231:GI2G-1952-MONOMER; -. DR Proteomes; UP000000535; 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:UniProtKB-KW. 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 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. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW90658.1}; KW Peroxidase {ECO:0000313|EMBL:AAW90658.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 421 AA; 46065 MW; DB1D8FB6A3C9A313 CRC64; MSQNQPAQPT KRNLFKTALA VGAIGAIGGY FGGKKQGETA ERTAESQHSP QAYPCYGEHQ AGIVTPRQAF SIMCAFDVTA QSAKQLENLF RTLTARIEFL TQGGEYQDGD DKLPSAGSGI LGKAFNPDGL TVTVGVGSSL FDGRFGLKDK KTVHLQEMRD FPNDKLQKSW CDGDLSLQIC AFTPETCQTA LRDIIKHTAQ TAVIRWSIDG WQPKSEPGAM AARNLLGFRD GTGNPKVSDP KTADEVLWTG VAANSLDEPE WAKNGSYQAV RLIRRFVEFW DRTPLQEQTD IFGRRKYSGA PMDGKKEADQ PDFAKDPEGD ITPKDSHMRL ANPRDPEFLK KHCLFRRAYS YSRGPASSGQ LDVGLVFVCY QANLADGFIF VQNLLNGEPL EEYISPFGGG YFFVLPGVGK GGFLGQGLPG V // ID Q5F9A8_NEIG1 Unreviewed; 135 AA. AC Q5F9A8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89229.1}; GN ORFNames=NGO_0491 {ECO:0000313|EMBL:AAW89229.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89229.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89229.1; -; Genomic_DNA. DR RefSeq; WP_003689098.1; NC_002946.2. DR RefSeq; YP_207641.1; NC_002946.2. DR EnsemblBacteria; AAW89229; AAW89229; NGO_0491. DR GeneID; 3283074; -. DR KEGG; ngo:NGO0491; -. DR PATRIC; 20334022; VBINeiGon24812_0583. DR HOGENOM; HOG000071318; -. DR OMA; YGEDAMF; -. DR OrthoDB; EOG65QWSD; -. DR BioCyc; NGON242231:GI2G-469-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 135 AA; 15621 MW; D613536104242B18 CRC64; MNQQEFEFMN DLARAFERRY RDTRSLNRCF SIEGRYMGEE ACPHKPEIGL RYGEDAMFLT LQAWAKVDAP QQEAVRISFG IGAKSQAAYE ERLQAEIRRR GEGPLHLQTD LGLAAWYRAI RQAAGNDFDL LFEKV // ID Q5FA36_NEIG1 Unreviewed; 434 AA. AC Q5FA36; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 64. DE RecName: Full=Ammonium transporter {ECO:0000256|RuleBase:RU362002}; GN ORFNames=NGO_0198 {ECO:0000313|EMBL:AAW88951.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88951.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88951.2; -; Genomic_DNA. DR RefSeq; WP_003687507.1; NC_002946.2. DR RefSeq; YP_207363.2; NC_002946.2. DR ProteinModelPortal; Q5FA36; -. DR EnsemblBacteria; AAW88951; AAW88951; NGO_0198. DR GeneID; 3281685; -. DR KEGG; ngo:NGO0198; -. DR PATRIC; 20333325; VBINeiGon24812_0245. DR HOGENOM; HOG000017736; -. DR KO; K03320; -. DR OMA; NNSWIGN; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NGON242231:GI2G-181-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU362002}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 45365 MW; 6763299BCCCB3516 CRC64; MKKHIWAASL LPASLSAEPL NWWKPYSAVN SGDTAWVMTA AALVLLMTLP GLALFYGGMV RKKNLLSTMM HSFSIATLVG ILWVAVGYSL AFTPGNAFIG GLGRVFLSGM QIDAAARMLT 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 LWIQVKDGFI MAAYSGLMSW AILKAVGKIC GGLRVGKDVE REGLDLNIHG EHVE // ID Q5F7A2_NEIG1 Unreviewed; 185 AA. AC Q5F7A2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Nitroreductase {ECO:0000313|EMBL:AAW89935.1}; GN ORFNames=NGO_1279 {ECO:0000313|EMBL:AAW89935.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89935.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89935.1; -; Genomic_DNA. DR RefSeq; WP_003691591.1; NC_002946.2. DR RefSeq; YP_208347.1; NC_002946.2. DR ProteinModelPortal; Q5F7A2; -. DR EnsemblBacteria; AAW89935; AAW89935; NGO_1279. DR GeneID; 3282089; -. DR KEGG; ngo:NGO1279; -. DR PATRIC; 20335899; VBINeiGon24812_1504. DR HOGENOM; HOG000146733; -. DR OMA; QGIGAVW; -. DR OrthoDB; EOG69GZM0; -. DR BioCyc; NGON242231:GI2G-1193-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000232-1}; KW FMN {ECO:0000256|PIRSR:PIRSR000232-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 20592 MW; 2CED367369CBB65D CRC64; MDALKLLTNR RSSKKLKHPA PDAAELEQIL QAATQVSDHG NMRPFRFTVI QGEVGLQRFR DVLKQTVAEL NFGDDAMKKA EKVGNMAPMV IGVTFVPNRD VPKPKPEWEQ MLTAGCAAYA LQLAATAQGF DNVWITGMWV NSPLLREAFG CEDKDKIIGL MMVGTPTEEV HKPKNTDLEA FVSHW // ID Q5F7Y1_NEIG1 Unreviewed; 307 AA. AC Q5F7Y1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89706.1}; GN ORFNames=NGO_1030 {ECO:0000313|EMBL:AAW89706.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89706.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89706.1; -; Genomic_DNA. DR RefSeq; WP_010360332.1; NC_002946.2. DR RefSeq; YP_208118.1; NC_002946.2. DR EnsemblBacteria; AAW89706; AAW89706; NGO_1030. DR GeneID; 3281683; -. DR KEGG; ngo:NGO1030; -. DR PATRIC; 20335276; VBINeiGon24812_1204. DR HOGENOM; HOG000000467; -. DR OMA; GHRLWGR; -. DR OrthoDB; EOG6GTZFQ; -. DR BioCyc; NGON242231:GI2G-951-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 248 269 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 281 300 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; 33045 MW; 72F92B09D5FF2E15 CRC64; MENQRPLLGF ALALLAAMTW GTLPIAVRQV LKFVDAPTLV WVRFTVAAAV LFVLLALGGR LPKRRDFSWH SFRLLLLGVT GISANFVLIA QGLHYISPTT TQVLWQISPF TMIVVGVLVF KDRMTAAQKI GLVLLLVGLL MFFNDKFGEL SGLGAYAKGV LLCAAGSMAW VCYAVAQKLL SAQFGPQQIL LLIYAASAAV FLPFAEPAHI GSLDGTLAWV CFVYCCLNTL IGYGSFGEAL KHWEASKVSA VTTLLPVFTV IFSLLGHYVM PDTFAAPDMN GLGYVGALVV VGGAVTAAVG DRPFKRR // ID Q5F8Z4_NEIG1 Unreviewed; 96 AA. AC Q5F8Z4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 72. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAW89343.1}; GN ORFNames=NGO_6151 {ECO:0000313|EMBL:AAW89343.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89343.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89343.1; -; Genomic_DNA. DR RefSeq; WP_003688918.1; NC_002946.2. DR RefSeq; YP_207755.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z4; -. DR EnsemblBacteria; AAW89343; AAW89343; NGO_6151. DR GeneID; 3281078; -. DR KEGG; ngo:NGO6151; -. DR PATRIC; 20334314; VBINeiGon24812_0729. DR HOGENOM; HOG000217153; -. DR KO; K11107; -. DR OMA; YCGSCRC; -. DR OrthoDB; EOG6BPDNN; -. DR BioCyc; NGON242231:GI2G-583-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. FT DOMAIN 1 96 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. SQ SEQUENCE 96 AA; 10490 MW; CBB6506E3500E10D CRC64; MARIGTNKGL FELLEGETLL EGLERTGHMV EYQCRSGYCG SCRVKILEGS VTYREPPLAF LGRDEILPCC CCVEGDVRLD CGLAGEDEGL SDSLLK // ID Q5F520_NEIG1 Unreviewed; 196 AA. AC Q5F520; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 57. DE SubName: Full=Transporter {ECO:0000313|EMBL:AAW90717.1}; GN ORFNames=NGO_2119 {ECO:0000313|EMBL:AAW90717.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90717.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90717.1; -; Genomic_DNA. DR RefSeq; WP_003687105.1; NC_002946.2. DR RefSeq; YP_209129.1; NC_002946.2. DR ProteinModelPortal; Q5F520; -. DR DNASU; 3282801; -. DR EnsemblBacteria; AAW90717; AAW90717; NGO_2119. DR GeneID; 3282801; -. DR KEGG; ngo:NGO2119; -. DR PATRIC; 20338085; VBINeiGon24812_2565. DR HOGENOM; HOG000220777; -. DR KO; K07323; -. DR OMA; QTQFADQ; -. DR OrthoDB; EOG6X10ZT; -. DR BioCyc; NGON242231:GI2G-2011-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256025. SQ SEQUENCE 196 AA; 21053 MW; 826D2EED9B7C20E8 CRC64; MKKSSFISAL GIGILSIGMA FASPADAVGQ IRQNATQVLT ILKSGDAASA RPKAEAYAVP YFDFQRMTAL AVGNPWRTAS DAQKQALAKE FQTLLIRTYS GTMLKFKNAT VNVKDNPIVN KGGKEIVVRA EVGIPGQKPV NMDFTTYQSG GKYRTYNVAI EGTSLVTVYR NQFGEIIKAK GIDGLIAELK AKNGGK // ID Q5F5H2_NEIG1 Unreviewed; 485 AA. AC Q5F5H2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. DE SubName: Full=Major facilitator transporter {ECO:0000313|EMBL:AAW90565.1}; GN ORFNames=NGO_1954 {ECO:0000313|EMBL:AAW90565.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90565.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90565.1; -; Genomic_DNA. DR RefSeq; WP_003688130.1; NC_002946.2. DR RefSeq; YP_208977.1; NC_002946.2. DR ProteinModelPortal; Q5F5H2; -. DR EnsemblBacteria; AAW90565; AAW90565; NGO_1954. DR GeneID; 3282667; -. DR KEGG; ngo:NGO1954; -. DR PATRIC; 20337649; VBINeiGon24812_2351. DR HOGENOM; HOG000243451; -. DR KO; K03305; -. DR OMA; YLFAFAK; -. DR OrthoDB; EOG6V1M5C; -. DR BioCyc; NGON242231:GI2G-1855-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 52512 MW; 45F838AB445465BB CRC64; MSRHPARTGE KTFFGHPFQL STLFHIELWE RFSFYGMQGI LLIYLYYTAD KGGLGIDKTL AGGIVGAYSG SVYLSTILGA WFADRVWGAE KTLFLSGIVV MLGHIVLAAA PGLYGLLIGL IFIALGSGGV KSTASSMVGA LYEQDEMRPL RDAGFSIFYI AINIGGFLGP LLTGLLQENI GFHYGFGAAA VGMAFGLWRY SLGRKNLPHP TVPHPLSKGQ GKTAAAVGIT 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 Q5F886_NEIG1 Unreviewed; 468 AA. AC Q5F886; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE SubName: Full=Major facilitator transporter {ECO:0000313|EMBL:AAW89601.1}; GN ORFNames=NGO_0903 {ECO:0000313|EMBL:AAW89601.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89601.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89601.1; -; Genomic_DNA. DR RefSeq; WP_010951149.1; NC_002946.2. DR RefSeq; YP_208013.1; NC_002946.2. DR ProteinModelPortal; Q5F886; -. DR EnsemblBacteria; AAW89601; AAW89601; NGO_0903. DR GeneID; 3281338; -. DR KEGG; ngo:NGO0903; -. DR PATRIC; 20334987; VBINeiGon24812_1063. DR HOGENOM; HOG000193484; -. DR OMA; ILTPMML; -. DR OrthoDB; EOG651SWK; -. DR BioCyc; NGON242231:GI2G-843-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 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; 50392 MW; 4023C841F4350EE4 CRC64; MEKNTLSARA PSPWLPLLLA IAIFMQMLDA TILNTALPEI AADLNESPPD MQQAVVAYTL TVALLIPLSS YLADKFGTKK VFFGSIAVFM LGSALGAASG SLFELTLSRV VQGIGGSMLV PIPRLTILRV YEKSKLLNAI NYAVMPALIG PALGPLAGGY LVEYASWHWI FLLNLPIGLL GFVLGRNIMP DVKGNDTALD FKGYLTFSVA ACLLLLAAES LSHALPPYFA LLPLCGGLLF ARRYFRHMKT ASKPIYSADL FLIRTFRLGL AGNLFSRLGI SSIPFLMPLM FQVAFGFGAS LSGWLVAPVA LSSLLVKPLI APLMKRFGYR TVLLWNTKLL AAFIMLLALP DGNSPLWIWI FLSLAIGACN SLQFSAMNTL TLADLRPQQT GSGNSLMAVN QQLAISVGIV AGALILKNWT FLIPASSGLH FAFRMTLLSI GGITLASSLV FKRLHVSDGA NLTRGTRP // ID Q5F689_NEIG1 Unreviewed; 558 AA. AC Q5F689; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 84. DE SubName: Full=Pilus assembly protein PilF {ECO:0000313|EMBL:AAW90298.1}; GN ORFNames=NGO_1673 {ECO:0000313|EMBL:AAW90298.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90298.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90298.1; -; Genomic_DNA. DR RefSeq; WP_010951320.1; NC_002946.2. DR RefSeq; YP_208710.1; NC_002946.2. DR ProteinModelPortal; Q5F689; -. DR EnsemblBacteria; AAW90298; AAW90298; NGO_1673. DR GeneID; 3281222; -. DR KEGG; ngo:NGO1673; -. DR PATRIC; 20336898; VBINeiGon24812_1994. DR HOGENOM; HOG000008427; -. DR KO; K02652; -. DR OMA; NSAVECI; -. DR OrthoDB; EOG63Z76W; -. DR BioCyc; NGON242231:GI2G-1567-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 374 388 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 558 AA; 61891 MW; 495B1F9E7925A65A CRC64; MSVGLLRILV QNQVVTVERA EHYYNESQAG KEVLPMLFSD GVISPKSLAA LIARVFSYSI LDLRHYPRHR VLMGVLTEEQ MVEFHCVPVF RRGDKVFFAV SDPTQMPQIQ KTVSAAGIAV 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 GILDVAYKEG MVDLRRAGIL KIMQGITSLE EVTANTND // ID Q5F798_NEIG1 Unreviewed; 500 AA. AC Q5F798; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 85. 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:AAW89939.2}; GN ORFNames=NGO_1285 {ECO:0000313|EMBL:AAW89939.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89939.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89939.2; -; Genomic_DNA. DR RefSeq; WP_010358797.1; NC_002946.2. DR RefSeq; YP_208351.2; NC_002946.2. DR ProteinModelPortal; Q5F798; -. DR DNASU; 3282105; -. DR EnsemblBacteria; AAW89939; AAW89939; NGO_1285. DR GeneID; 3282105; -. DR KEGG; ngo:NGO1285; -. DR PATRIC; 20335913; VBINeiGon24812_1511. DR HOGENOM; HOG000006394; -. DR KO; K02600; -. DR OMA; QLFMDKL; -. DR OrthoDB; EOG6NSGHW; -. DR BioCyc; NGON242231:GI2G-1197-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 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; 2. 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:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}; KW Elongation factor {ECO:0000313|EMBL:AAW89939.2}; KW Protein biosynthesis {ECO:0000313|EMBL:AAW89939.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 55794 MW; F76F465705A909C2 CRC64; MSREMLQLAE ALASEKNVDA EVVFQALEFA LSTAAKKKAD REHMDVRVQI NRDTGEYQTF RRWLIVADED YTYPDVEKTI EEIQEEIPDT TIQIGEYYEE QLPNEGFGRQ AAQTAKQIIL QRIRDAEREQ NLNEFLAVKE DIVSGTVKRV ERHGIIVEVV AGKLDALIPR DQMIPRENFR SGDRIRALFL RVEEIGNTGR KQIILSRTSG DFLVKLYANE VPEIADGMLE IRAVARDPGQ RAKVAVKAND QRIDPQGTCI GVRGSRVNAV SNELSGERID VVLWSPEPAQ FVMSALSPAE VSRIVIDEDK HAVDVIVAED RLALAIGRGG QNVRLASDLT GWQLNIMTSA EADERNAAED AAIRRLFMNH LNVDEETADV LVQEGFATLE EVAYVPAAEL LAIEGFDEEI VDMLRNRARD AILTMAIAAE EKLGEVSDDM RNLEGVDADM LLSLAEAGIT TRDDLAELAV DELIEITGVN EETAKAVILT AREHWFTEDK // ID Q5FAK1_NEIG1 Unreviewed; 66 AA. AC Q5FAK1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88782.1}; GN ORFNames=NGO_0010 {ECO:0000313|EMBL:AAW88782.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88782.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88782.1; -; Genomic_DNA. DR RefSeq; WP_010950971.1; NC_002946.2. DR RefSeq; YP_009179203.1; NC_002946.2. DR EnsemblBacteria; AAW88782; AAW88782; NGO_0010. DR GeneID; 26142985; -. DR PATRIC; 20332852; VBINeiGon24812_0012. DR HOGENOM; HOG000071336; -. DR OMA; LQGVGFK; -. DR OrthoDB; EOG6GJBZC; -. DR BioCyc; NGON242231:GI2G-9-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 6869 MW; B90EF5A2FBD7B660 CRC64; MPDRIKPSRN GGGTDGIARQ QGTAQTGAKP ETSPTARHGD FLRPLQGGLD LSGTGLKAKR AGRRTV // ID Q5F5D7_NEIG1 Unreviewed; 350 AA. AC Q5F5D7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Restriction endonuclease HaeII {ECO:0000313|EMBL:AAW90600.1}; GN ORFNames=NGO_1992 {ECO:0000313|EMBL:AAW90600.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90600.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90600.1; -; Genomic_DNA. DR RefSeq; WP_003686885.1; NC_002946.2. DR RefSeq; YP_209012.1; NC_002946.2. DR REBASE; 2791; NgoAI. DR EnsemblBacteria; AAW90600; AAW90600; NGO_1992. DR GeneID; 3282632; -. DR KEGG; ngo:NGO1992; -. DR PATRIC; 20337753; VBINeiGon24812_2403. DR HOGENOM; HOG000263513; -. DR OMA; DMWANFG; -. DR OrthoDB; EOG628F2V; -. DR BioCyc; NGON242231:GI2G-1890-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR019058; Restrct_endonuc_II_HaeII. DR Pfam; PF09554; RE_HaeII; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW90600.1}; KW Hydrolase {ECO:0000313|EMBL:AAW90600.1}; KW Nuclease {ECO:0000313|EMBL:AAW90600.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 350 AA; 40552 MW; 2F7FC742266264CC CRC64; MTLEEQQAKE ALDGIIKKSR VHLYKPIQIA EILYHDRCIK QLDFLNLDTY RNQSKRWRDE ICRRFLGRIS TSSAKFQDNL FEKNAIPPEK LAVLGTLNRQ SDGGVESYIY KQFFNRFSQM SEALAYVGNT DRYSFQLSEF LNLFWLEPGL KRSIDKIYEI VVYALFDALV SELGITVSID FPKENLFLWE EYQDFAEKII TMPKNEHLKL PAKIHRVGVT NAADRGLDMW SNFGLAIQVK HLSLDEELAE DIVSSISADR IVIVCKKAEQ SVIVSLLTQI GWKSRIQNIV TEDDLISWYE KALRGQYPIA EALLENIKTE IMREFPAVNE ANEFLDFAQN RGYDITVTHF // ID Q5F640_NEIG1 Unreviewed; 241 AA. AC Q5F640; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90347.1}; GN ORFNames=NGO_1726 {ECO:0000313|EMBL:AAW90347.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90347.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90347.1; -; Genomic_DNA. DR RefSeq; WP_010951335.1; NC_002946.2. DR RefSeq; YP_208759.1; NC_002946.2. DR ProteinModelPortal; Q5F640; -. DR EnsemblBacteria; AAW90347; AAW90347; NGO_1726. DR GeneID; 3281250; -. DR KEGG; ngo:NGO1726; -. DR PATRIC; 20337048; VBINeiGon24812_2064. DR HOGENOM; HOG000075040; -. DR OMA; LARWLGC; -. DR OrthoDB; EOG6716R8; -. DR BioCyc; NGON242231:GI2G-1622-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 241 AA; 26929 MW; 0AA80186BC9E81B0 CRC64; MNFLSCWRRI ADAPTIRRCV LCHGSSGVSD GICAGCNTDL ASFRTDAANS CPLCFRHVQG GAVCGGCQKK PPAFDRMWAS LHYEPPVSNM IRALKHLADL GMAQPLADLT MQNPPDRLSD ECFNFVLPVP LSRERLLQRG FNQSESIVGL LAQRYGWQIL PRHTVFRHHR PPQSTLKGGE RRRNIKNAFE IRTPIPENCN ILLIDDVFTT GATLDELAKT LKKSGANRIC CWTLARTPMK K // ID Q5F820_NEIG1 Unreviewed; 160 AA. AC Q5F820; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:AAW89667.1}; GN ORFNames=NGO_0981 {ECO:0000313|EMBL:AAW89667.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89667.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89667.1; -; Genomic_DNA. DR RefSeq; WP_003688300.1; NC_002946.2. DR RefSeq; YP_208079.1; NC_002946.2. DR ProteinModelPortal; Q5F820; -. DR EnsemblBacteria; AAW89667; AAW89667; NGO_0981. DR GeneID; 3282866; -. DR KEGG; ngo:NGO0981; -. DR PATRIC; 20335164; VBINeiGon24812_1151. DR HOGENOM; HOG000154889; -. DR KO; K03775; -. DR OMA; PKDVFVG; -. DR OrthoDB; EOG6Q8J79; -. DR BioCyc; NGON242231:GI2G-909-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016853; F: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; 2. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Isomerase {ECO:0000313|EMBL:AAW89667.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 93 PPIase FKBP-type. FT {ECO:0000259|PROSITE:PS50059}. SQ SEQUENCE 160 AA; 17345 MW; B982D412C34DB37B CRC64; MAIAKNSVVS LHYEMYDANN QLLDKTEEPI AYLHGGYDGI FPLVEEALHG KDAGDTVDVA LSSDDAFGEQ DSELVRIEDA GAFPVEVEVG MMFEADDPET GDVVVYRVTD VADGKAVVDG NHPLAGMKIR FKATVESVRD ASDEEIAHGH VHGSHGHYHH // ID Q5F866_NEIG1 Unreviewed; 467 AA. AC Q5F866; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 80. DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:AAW89621.1}; DE EC=1.8.1.4 {ECO:0000313|EMBL:AAW89621.1}; GN ORFNames=NGO_0925 {ECO:0000313|EMBL:AAW89621.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89621.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89621.1; -; Genomic_DNA. DR RefSeq; WP_003688389.1; NC_002946.2. DR RefSeq; YP_208033.1; NC_002946.2. DR ProteinModelPortal; Q5F866; -. DR EnsemblBacteria; AAW89621; AAW89621; NGO_0925. DR GeneID; 3282876; -. DR KEGG; ngo:NGO0925; -. DR PATRIC; 20335033; VBINeiGon24812_1086. DR HOGENOM; HOG000276709; -. DR KO; K00382; -. DR OMA; IDDHTQI; -. DR OrthoDB; EOG6ZPSW0; -. DR BioCyc; NGON242231:GI2G-863-MONOMER; -. DR Proteomes; UP000000535; 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; -; 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89621.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 50832 MW; 710E5CF9A3AD7971 CRC64; MKKIQADIVV IGGGTAGMGA FRNARLHSDN VYLIENNVFG TTCARVGCMP SKLLIAAAEA RHHALHTDPF GVHLDKDSIV VNGEEVMRRV KSERDRFVGF VVTDVEEWPA DKRIMGSAKF IDEHTVQIDD HIQIAAKSFV IATGSRPVIL PQWQSLGDRL IINDDVFSWD TLPKRVAVFG PGVIGLELGQ ALHRLGVKVE IFGLGGIIGG ISDPVVSDEA KAVFGEELKL HLDAKTEVKL DADGNVEVHW EQDGEKGVFV AEYMLAAVGR RPNVDNIGLE NINIDKDARG VPVADPLTMQ TSIPHIFIAG DASNQLPLLH EAADQGKIAG DNAGRYPNIG SGLRRSTIGV VFTSPQIGFV GLKYAQVAAQ YQADEFVIGE VSFKNQGRSR VMLVNKGHMR LYAEKATGRF IGAEIVGPAA EHLAHLLAWA HQMKMTVPQM LDMPFYHPVI EEGLRTALRD ADAKLKA // ID Q5F6H2_NEIG1 Unreviewed; 93 AA. AC Q5F6H2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90215.1}; GN ORFNames=NGO_1586 {ECO:0000313|EMBL:AAW90215.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90215.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90215.1; -; Genomic_DNA. DR RefSeq; WP_003693718.1; NC_002946.2. DR RefSeq; YP_208627.1; NC_002946.2. DR EnsemblBacteria; AAW90215; AAW90215; NGO_1586. DR GeneID; 3281151; -. DR KEGG; ngo:NGO1586; -. DR PATRIC; 20336700; VBINeiGon24812_1896. DR HOGENOM; HOG000218652; -. DR OrthoDB; EOG6MH5G3; -. DR BioCyc; NGON242231:GI2G-1483-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 93 AA; 11048 MW; 7639CE17378FE0EF CRC64; MGNGHQNNQS SLEKRIFYLE HSGQYLMICA LSDYSQNKHT VVMANFLYPN EKMDWRNLDD LFNELVLEEL QSSFMDWYPT IEKAISHHLE DFS // ID Q5FA10_NEIG1 Unreviewed; 150 AA. AC Q5FA10; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 63. DE SubName: Full=Dihydroneopterin triphosphate pyrophosphatase {ECO:0000313|EMBL:AAW88977.2}; GN ORFNames=NGO_0224 {ECO:0000313|EMBL:AAW88977.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88977.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88977.2; -; Genomic_DNA. DR RefSeq; WP_010357032.1; NC_002946.2. DR RefSeq; YP_207389.2; NC_002946.2. DR ProteinModelPortal; Q5FA10; -. DR EnsemblBacteria; AAW88977; AAW88977; NGO_0224. DR GeneID; 3281460; -. DR KEGG; ngo:NGO0224; -. DR PATRIC; 20333387; VBINeiGon24812_0276. DR HOGENOM; HOG000264405; -. DR KO; K08310; -. DR OMA; VTRNTEH; -. DR OrthoDB; EOG69WFKW; -. DR BioCyc; NGON242231:GI2G-207-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 146 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 150 AA; 17296 MW; E11358907612D103 CRC64; MAKPLKYPVS ALVVLYSGDG GILLIERTHP KGFWQSVTGS LEPGETVAQT ARREVWEETG ILLEDGQLQD RHDSTVYEIY HHWRHRYPKG VFENREHVFR AEIPRDTPVV LQPEEHVSYG WFGLEEAAEK VFSPSNRRAI LELGRFLGKR // ID Q5F6Y7_NEIG1 Unreviewed; 179 AA. AC Q5F6Y7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90050.1}; GN ORFNames=NGO_1405 {ECO:0000313|EMBL:AAW90050.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90050.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90050.1; -; Genomic_DNA. DR RefSeq; WP_003689258.1; NC_002946.2. DR RefSeq; YP_208462.1; NC_002946.2. DR EnsemblBacteria; AAW90050; AAW90050; NGO_1405. DR GeneID; 3281184; -. DR KEGG; ngo:NGO1405; -. DR PATRIC; 20336213; VBINeiGon24812_1655. DR HOGENOM; HOG000071328; -. DR OMA; KINEAYL; -. DR OrthoDB; EOG6KHG75; -. DR BioCyc; NGON242231:GI2G-1315-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 179 AA; 19614 MW; E59A7678D7EEB2EF CRC64; MFFDTEGKSH TAIFMKIVGG NGKIAGEVVI DGEYALDIVR MNDDLSIAVQ DNKGRSRASD LEALSQAKSF TLIAFSRYAG TVEVDKVSAV TGICADYRSK GLKVAVADNM RPKQEIVVFR ASGVMASNKR KINEAYLDYS ASSKLPSAQK QELEQDKNNM IAVHYGRLEE LIARGICVR // ID Q5F5U7_NEIG1 Unreviewed; 436 AA. AC Q5F5U7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. 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:AAW90440.1}; GN ORFNames=NGO_1822 {ECO:0000313|EMBL:AAW90440.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90440.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90440.1; -; Genomic_DNA. DR RefSeq; WP_003705313.1; NC_002946.2. DR RefSeq; YP_208852.1; NC_002946.2. DR ProteinModelPortal; Q5F5U7; -. DR EnsemblBacteria; AAW90440; AAW90440; NGO_1822. DR GeneID; 3282367; -. DR KEGG; ngo:NGO1822; -. DR PATRIC; 20337308; VBINeiGon24812_2189. DR HOGENOM; HOG000080585; -. DR KO; K03076; -. DR OMA; QTYVISQ; -. DR OrthoDB; EOG651SWP; -. DR BioCyc; NGON242231:GI2G-1720-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 47526 MW; 7D905C26F0401AAC CRC64; MANQQTSSGS SKFGDLKKRL LFLFGALIVF RIGAHIPVPG VDAVALAKLY ESAGNGILGI LNMFSGGSLE RFSIFAIGIM PYISASIIVQ LASEILPSLK ALKKEGEAGR KVITKYTRYG TVLLAILQSL GVASFVFQQG IVVTSSFEFH VSTVVSLVTG TMFLMWLGEQ ITERGIGNGI SLIITAGIAS GIPSGIAKLV TLTNQGSMSM LTALLIVFGA LLLIYLVVYF ESAQRKIPIH YAKRQFNGRA GSQSTHMPFK LNMAGVIPPI FASSIILFPS TLLGWFGSAD TNSVLHKIAG LLQHGQLLYM ALFAATVIFF CYFYTALVFS PKEMAENLKK SGAFVPGIRP GEQTSRYLEK VVLRLTLFGA FYITTICLIP EFLTTILNVP FYLGGTSLLI LVVVTMDFST QINSYRLTQQ YDKLMTRSEM KSFSRK // ID Q5F501_NEIG1 Unreviewed; 288 AA. AC Q5F501; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE RecName: Full=Lipoprotein {ECO:0000256|PIRNR:PIRNR002854}; GN ORFNames=NGO_2139 {ECO:0000313|EMBL:AAW90736.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90736.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90736.1; -; Genomic_DNA. DR RefSeq; WP_003687141.1; NC_002946.2. DR RefSeq; YP_209148.1; NC_002946.2. DR ProteinModelPortal; Q5F501; -. DR EnsemblBacteria; AAW90736; AAW90736; NGO_2139. DR GeneID; 3282782; -. DR KEGG; ngo:NGO2139; -. DR PATRIC; 20338129; VBINeiGon24812_2587. DR HOGENOM; HOG000222927; -. DR KO; K02073; -. DR OMA; PHTIVFG; -. DR OrthoDB; EOG6P073X; -. DR BioCyc; NGON242231:GI2G-2030-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lipoprotein {ECO:0000256|PIRNR:PIRNR002854}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 288 Lipoprotein. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256016. SQ SEQUENCE 288 AA; 31338 MW; 3B34CA5BD4D244CC CRC64; MKTFFKTLSA AALALILAAC GGQKDSAPAA SAAAPSADNG AAKKEIVFGT TVGDFGDMVK EQIQAELEKK GYTVKLVEFT DYVRPNLALA EGELDINVFQ HKPYLDDFKK EHNLDITEAF QVPTAPLGLY PGKLKSLEEV KDGSTVSAPN DPSNFARALV MLNELGWIKL KDGINPLTAS KADIAENLKN IKIVELEAAQ LPRSRADVDF AVVNGNYAIS SGMKLTEALF QEPSFAYVNW SAVKTADKDS QWLKDVTEAY NSDAFKAYAH KRFEGYKYPA AWNEGAAK // ID Q5F7D3_NEIG1 Unreviewed; 288 AA. AC Q5F7D3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 51. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89904.1}; GN ORFNames=NGO_1245 {ECO:0000313|EMBL:AAW89904.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89904.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89904.1; -; Genomic_DNA. DR RefSeq; WP_003697963.1; NC_002946.2. DR RefSeq; YP_208316.1; NC_002946.2. DR ProteinModelPortal; Q5F7D3; -. DR EnsemblBacteria; AAW89904; AAW89904; NGO_1245. DR GeneID; 3282602; -. DR KEGG; ngo:NGO1245; -. DR PATRIC; 20335809; VBINeiGon24812_1464. DR HOGENOM; HOG000219034; -. DR OMA; LERDNHF; -. DR OrthoDB; EOG6GTZFW; -. DR BioCyc; NGON242231:GI2G-1157-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 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; 32730 MW; 3BE8455CE002D17B CRC64; MWKMLKHIAK THRKRLIGTF SPVGLENLLM LGYPVFGGWA INAVIAGRVW QALLYALVVF LMWLVGAARR IADTRTFTRI YTEIAVPVVL EQRQRQVPHS AVTARVALSR EFVSFFEEHL PIAATSVVSI FGACIMLLVL EFWVGVSAVG ILALFLWLLP RFAAISENLY FRLNNSLERD NHFIRKGDER QLYRHYGLVS RLRVLISNRE AFGYLCVGAA MGILFGFAFV MMTLKGYGSA GHIYSVGTYL WMFAMSLDDV PRLVEQYSNL KDIGQRIEWS ERNIKAGT // ID Q5F7A5_NEIG1 Unreviewed; 751 AA. AC Q5F7A5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 60. DE SubName: Full=Nitric oxide reductase large subunit {ECO:0000313|EMBL:AAW89932.2}; GN ORFNames=NGO_1275 {ECO:0000313|EMBL:AAW89932.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89932.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89932.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7A5; -. DR EnsemblBacteria; AAW89932; AAW89932; NGO_1275. DR PATRIC; 20335883; VBINeiGon24812_1496. DR HOGENOM; HOG000288072; -. DR OMA; QGYEYID; -. DR OrthoDB; EOG6PW211; -. DR BioCyc; NGON242231:GI2G-1190-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 84360 MW; 5D167759ADB4AA93 CRC64; MGQYKKLWYL LFAVLAVCFT ILGYMGSEVY KKAPPYPEQV VSASGKVLMT KDDILAGQSA WQSTGGMEVG SILGHGAYQA PDWTADWLHR ELSAWLDLTA QQTYGKKFDE VSPEEQAVLK TRLADEYRNQ SRIKEDGSVV ISDTRVKAIE SILPYYHGVY GDDPKLQTTR EHFAMKNNTL PSQEAREKLF DFFFWTSWSA STNRPGEVFT 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 ARFDDKLMTW GFWLLNGGLV GMIAISLLPV GVIQAYASIT HGLWYARSEE FLQMEILDTL RWVRTAPDLI FIGGAICVAI QATKIVFGRD K // ID Q5FAI4_NEIG1 Unreviewed; 354 AA. AC Q5FAI4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 71. DE SubName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000313|EMBL:AAW88803.1}; DE EC=4.1.2.13 {ECO:0000313|EMBL:AAW88803.1}; GN ORFNames=NGO_0034 {ECO:0000313|EMBL:AAW88803.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88803.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88803.1; -; Genomic_DNA. DR RefSeq; WP_003687252.1; NC_002946.2. DR RefSeq; YP_207215.1; NC_002946.2. DR ProteinModelPortal; Q5FAI4; -. DR EnsemblBacteria; AAW88803; AAW88803; NGO_0034. DR GeneID; 3282170; -. DR KEGG; ngo:NGO0034; -. DR PATRIC; 20332898; VBINeiGon24812_0034. DR HOGENOM; HOG000227792; -. DR KO; K01624; -. DR OMA; VNTREMF; -. DR OrthoDB; EOG6HXJ7B; -. DR BioCyc; NGON242231:GI2G-31-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|SAAS:SAAS00485079, ECO:0000313|EMBL:AAW88803.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00485111}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Zinc {ECO:0000256|SAAS:SAAS00485107}. FT REGION 233 235 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. FT REGION 275 278 Dihydroxyacetone phosphate binding. FT {ECO:0000256|PIRSR:PIRSR001359-2}. 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; 38313 MW; 8CD89AC86A35D2AA CRC64; MALVSMRQLL DHAAENSYGL PAFNVNNLEQ MRAIMEAADQ VNAPVIVQAS AGARKYAGAP FLRHLILAAV EEFPHIPVVM HQDHGASPDV CQRSIQLGFS SVMMDGSLLE DGKTPSSYEY NVNATRTVVN FSHACGVSVE GEIGVLGNLE TGEAGEEDGV GAAGKLSHDQ MLTSVEDAVR FVKDTGVDAL AIAVGTSHGA YKFTRPPTGD VLRIDRIKEI HQALPNTHIV MHGSSSVPQE WLKVINEYGG NIGETYGVPV EEIVEGIKHG VRKVNIDTDL RLASTGAVRR YLAENPSDFD PRKYLGKTIE AMKQICLDRY LAFGCEGQAG KIKPVSLEKM ASRYAKGELN QIVK // ID Q5F916_NEIG1 Unreviewed; 812 AA. AC Q5F916; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 11-MAY-2016, entry version 67. DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AAW89321.2}; GN ORFNames=NGO_0590 {ECO:0000313|EMBL:AAW89321.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89321.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA. CC {ECO:0000256|SAAS:SAAS00537806}. CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. CC {ECO:0000256|SAAS:SAAS00545451}. CC -!- SIMILARITY: Contains FtsK domain. {ECO:0000256|SAAS:SAAS00514329}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89321.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F916; -. DR EnsemblBacteria; AAW89321; AAW89321; NGO_0590. DR PATRIC; 20334254; VBINeiGon24812_0699. DR HOGENOM; HOG000010003; -. DR OMA; YELFANT; -. DR OrthoDB; EOG6S52GD; -. DR BioCyc; NGON242231:GI2G-561-MONOMER; -. DR Proteomes; UP000000535; 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; 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: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; IPR004042; Intein_endonuc. 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. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00514327}; KW Cell cycle {ECO:0000256|SAAS:SAAS00420121, KW ECO:0000313|EMBL:AAW89321.2}; KW Cell division {ECO:0000256|SAAS:SAAS00420121, KW ECO:0000313|EMBL:AAW89321.2}; KW Cell membrane {ECO:0000256|SAAS:SAAS00420089}; KW Chromosome partition {ECO:0000256|SAAS:SAAS00420072}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00429514}; KW Membrane {ECO:0000256|SAAS:SAAS00420084, KW ECO:0000256|SAAS:SAAS00420089, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00514327}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAAS:SAAS00420084, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00420084, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 62 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 158 178 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 211 230 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 461 670 FtsK. {ECO:0000259|PROSITE:PS50901}. FT DOMAIN 700 793 DOD-type homing endonuclease. FT {ECO:0000259|PROSITE:PS50819}. SQ SEQUENCE 812 AA; 88114 MW; BD6A7FD386F7D4C6 CRC64; MTEKSHKKTA KGRAGSPSPT SARNKKADNG ARGNKVSERL KAVKELQKTE AKKARPEHVV NLIADALWLM GLAATLYLAI SLISFDMGDP SWSHSSPVVE DAANWGGLFG AYVADVGYYL FGWSFWWWIA AACVVLYKNF RLHAKQTENE AYNHKIAAAA LFVLTVFSPV LEYFVLGGKY ADSLPVGAGG MVGIRVGAVF AWLLGKSGSL LIILVVLLLS LSLLVQISWL EFLNGAGRAV QNRLSALSGK VMALRKRRPN TKTDGVDTQN TRRMVKEAKN ITAKPVALPE GSSSNRKSVA VSVAPPPKIQ PSLFEDNEVQ QNGEYHKPTL NLLRIPDSEP VSINPAELER TAELIESKLA EFGIGVQVVS ATSGPVITRY EIEPAQGVKG SQIVALSKDL ARSMSLQSVR IVETIAGKNT MGIELPNDKR QDVMLSEILS SPVFAEAKSK LTVALGKDIA GTPVVGDLAK MPHLLVAGMT GSGKSVGVNG MIMSMLFKAT PEEVRFIMID PKMLELSIYD GIPHLLCPVV TDMREAGQAL NWCVAEMEKR YRLLSHAGVR NLEGFNQKVE QAKAAGKPLL NPFSLNLDEP EPLEKLPMIV VVIDELADLM MTERKAVEQQ IARLAQKARA AGIHMIVATQ RPSVDVVTGL IKANIPTRMA FTVQSKIDSR TILDQMGADE LLKYGDSLFL QPGSAEPTRL QGTFVSDGEV HQVVNYVKSQ APADYIEGLL SGEAALETAN IVNPNADSDE LFDQAVAYVL ESKKTSISSL QRQLRIGYNR AANLMEALEN AGIVSPSDLN GSRKILAHKD HL // ID A0A0H4IWH7_NEIG1 Unreviewed; 1006 AA. AC A0A0H4IWH7; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Pilus assembly protein {ECO:0000313|EMBL:AKO63788.1}; GN ORFNames=NGO_10270 {ECO:0000313|EMBL:AKO63788.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63788.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63788.1; -; Genomic_DNA. DR RefSeq; WP_039080664.1; NC_002946.2. DR RefSeq; YP_009115486.1; NC_002946.2. DR EnsemblBacteria; AKO63788; AKO63788; NGO_10270. DR GeneID; 22847894; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008707; PilC_beta_prop_dom. DR Pfam; PF05567; Neisseria_PilC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 481 817 Neisseria_PilC. FT {ECO:0000259|Pfam:PF05567}. SQ SEQUENCE 1006 AA; 110746 MW; E0F50C9BF1A4045F CRC64; MNAQNLPEVK WGQSYSSAPK KDRERQFTHT NNFKIRRNTT ISFDNTDNVV AQKGGIVVFG AATYLPPYGK VSGFDTDSLK GRGNAVDWIS TTRPGLVGYS YENVTCHNNY FAPSRGCPEV VYKTQFTFGQ QGLQRKAGNK LDIYEDKSRD NSPIYKLSDY PWLGVSFNLS SESLVKEKRH NKKIFYFNED VTQQNSGNPQ YKDQNLVYTT GDGNKYSSRY VGQNEHSAIA FYLNAKLHLL DKTQIKDITQ GKTVDLGTLK PRIELSKGWK NRLDRFFLGN WTLEDKGKVS VNLGLPQVKA GRCINKPNPN NNTKAPSPAL TAPALWFGPV QNGKVQMYSA SVSTYPDSSS SRIYLQNLKR KTESGKPGRY SLVTLNENDI KSKEPSFMGR ETIIRLDSGV QLIKLNRNKD EVVTFGNTGN NGTFGIVKEA NVNLKADEWK KVLLPWTVRA AADDGRFKSI NRESDKYSQR YRIRENGNRD LGDIVNSPIV AVGGYLATAA NDGMVHIFKK NGGSDERSYN LKLSYIPGTM PRKDIESNDS TLAKELRAFA EKGYVGDRYG VDGGFVLRRI TDDQDKQKHF FMFGAMGFGG RGAYALDLSK IDGNYPAAAP LFDVKNGDNN GKNRVKVELG YTVGTPQIGK TQNGKYAAFL ASGYAAKNIG SGDNKTALYV YDLENGSGSL IKKIEVQGGK GGLSSPTLVD KDLDGTVDIA YAGDRGGNMY RFDLSDSNPD KWSVRTIFEG DKPITSAPAV SRLADKRVVI FGTGSDLTED DVLNTGEQYI YGIFDDDKGT VKVTVQNGTG GGLLEQVLKE ENKTLFLNKG SDGSGSKGWV VKLKEGQRVT VKPTVVLRTA FVTIRSYTGN DKCGAQTAIL GINTADGGAL TPRSARPIVP DNQVAQYSGH QKMNGKSIPI GCMWKNGKTV CPNGYVYDKP VNVRYLDEKK TDDFPVTADG DAGGSGTFKE GKKPARNNRC FSGKGVRTLL MNDLDSLDIT GPMCGIKRLS WREVFF // ID Q5F5L8_NEIG1 Unreviewed; 263 AA. AC Q5F5L8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 70. 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 ORFNames=NGO_1905 {ECO:0000313|EMBL:AAW90519.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90519.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90519.1; -; Genomic_DNA. DR RefSeq; WP_003694504.1; NC_002946.2. DR RefSeq; YP_208931.1; NC_002946.2. DR ProteinModelPortal; Q5F5L8; -. DR SMR; Q5F5L8; 1-263. DR EnsemblBacteria; AAW90519; AAW90519; NGO_1905. DR GeneID; 3282276; -. DR KEGG; ngo:NGO1905; -. DR PATRIC; 20337530; VBINeiGon24812_2292. DR HOGENOM; HOG000230246; -. DR KO; K00286; -. DR OMA; RTFNEHQ; -. DR OrthoDB; EOG6JB16S; -. DR BioCyc; NGON242231:GI2G-1808-MONOMER; -. DR UniPathway; UPA00098; UER00361. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01925}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925}; KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 90 F420_oxidored. FT {ECO:0000259|Pfam:PF03807}. FT DOMAIN 154 258 P5CR_dimer. {ECO:0000259|Pfam:PF14748}. SQ SEQUENCE 263 AA; 28162 MW; 39204730CAC80021 CRC64; MNVYFLGGGN MAAAVAGGLV KQGGYRIHIA NRGAEKRERL GKELGVETSA TLPELHSDDV LILAVKPQDM EAACKNIRTN GALVLSVAAG LSVGTLSRYL GGSRRIVRVM PNTPGKIGLG VSGMYAEAEV SETDRRIADR IMKSVGLTVW LEDEAQMHSI TGISGSGPAY VFYLLDALQN AAIRQGFDMA EARALSLATF KGAVALAEQT GEDFEKLQKN VTSKGGTTHE AVEAFRRHRV AEAISEGVCA CVCRSQEMER QYQ // ID A0A0H4ISA9_NEIG1 Unreviewed; 226 AA. AC A0A0H4ISA9; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Large pilS cassette protein {ECO:0000313|EMBL:AKO63801.1}; GN ORFNames=NGO_10975 {ECO:0000313|EMBL:AKO63801.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63801.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63801.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63801; AKO63801; NGO_10975. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 226 AA; 24183 MW; 7451A0AFC155B96D CRC64; MASASTIKGK YVQKVEVTNG VVTAQMASTG VNKEIKGKKL SLWARRQDGS VKWFCGQPVK RDDAAAKDDT VTADATGNDG KIDTKHLPST CRDKSTAVCT KHHAPISNTS KKSAVAGYYL NHGEWPENNT SAGVASSDKI KGKYVQKVEV AKGVVTAQMA STGVNKEIQG KKLSLWAKRQ DGSVKWFCGQ PVTRNDAKAD DVKADAANAI ETKHLPSTCR DESSAT // ID A0A0H4IUZ4_NEIG1 Unreviewed; 94 AA. AC A0A0H4IUZ4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 4. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKO63600.1}; GN ORFNames=NGO_00790 {ECO:0000313|EMBL:AKO63600.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63600.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63600.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63600; AKO63600; NGO_00790. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR024445; Tnp_ISXO2-like. DR Pfam; PF12762; DDE_Tnp_IS1595; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 77 DDE_Tnp_IS1595. FT {ECO:0000259|Pfam:PF12762}. SQ SEQUENCE 94 AA; 10792 MW; 5519561F0F813444 CRC64; MPDGIVYADS PGSRGKLDAG GFTRCRINRS KEFADRRNHI NGIGNFWNQA KRALRKYNGI DRKPFPPLLR ECEFRLNSGT PSRQLKILRD WCGI // ID A0A0H4IS71_NEIG1 Unreviewed; 51 AA. AC A0A0H4IS71; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-MAY-2016, entry version 2. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AKO63761.1}; GN ORFNames=NGO_08990 {ECO:0000313|EMBL:AKO63761.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AKO63761.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AKO63761.1; -; Genomic_DNA. DR EnsemblBacteria; AKO63761; AKO63761; NGO_08990. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 51 AA; 6036 MW; FE6276A97DF80B3F CRC64; MLKTKRTNCL KKDLIGMRVF PTLSPFIYPH YKNMKKNPCL HSHLQPCPPL R // ID Q5F5Y8_NEIG1 Unreviewed; 125 AA. AC Q5F5Y8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 59. DE RecName: Full=Outer membrane protein assembly factor BamE {ECO:0000256|HAMAP-Rule:MF_00925}; DE Flags: Precursor; GN Name=bamE {ECO:0000256|HAMAP-Rule:MF_00925}; GN ORFNames=NGO_1780 {ECO:0000313|EMBL:AAW90399.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90399.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00925}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000256|HAMAP- CC Rule:MF_00925}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP- CC Rule:MF_00925}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00925}. CC -!- SIMILARITY: Belongs to the BamE family. {ECO:0000256|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; AE004969; AAW90399.1; -; Genomic_DNA. DR RefSeq; WP_003689992.1; NC_002946.2. DR RefSeq; YP_208811.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y8; -. DR EnsemblBacteria; AAW90399; AAW90399; NGO_1780. DR GeneID; 3282539; -. DR KEGG; ngo:NGO1780; -. DR PATRIC; 20337202; VBINeiGon24812_2137. DR HOGENOM; HOG000256181; -. DR OMA; RINIPQG; -. DR OrthoDB; EOG6J48RK; -. DR BioCyc; NGON242231:GI2G-1678-MONOMER; -. DR Proteomes; UP000000535; 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. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00925}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00925}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00925}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_00925}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00925}. FT SIGNAL 1 17 {ECO:0000256|HAMAP-Rule:MF_00925}. FT CHAIN 18 125 Outer membrane protein assembly factor FT BamE. {ECO:0000256|HAMAP-Rule:MF_00925}. FT /FTId=PRO_5005078752. FT DOMAIN 36 105 SmpA_OmlA. {ECO:0000259|Pfam:PF04355}. FT LIPID 18 18 N-palmitoyl cysteine. {ECO:0000256|HAMAP- FT Rule:MF_00925}. FT LIPID 18 18 S-diacylglycerol cysteine. FT {ECO:0000256|HAMAP-Rule:MF_00925}. SQ SEQUENCE 125 AA; 13953 MW; C9F6EF61DFDB5BFB CRC64; MNKTLILALS ALFSLTACSV ERVSLFPSYK LKIIQGNELE PRAVAALRPG MTKDQVLLLL GSPILRDAFH TDRWDYTFNT SRNGIIKERS NLTVYFENGV LVRTEGDALQ NAAEALRAKQ NADKQ // ID Q5F568_NEIG1 Unreviewed; 229 AA. AC Q5F568; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90669.1}; GN ORFNames=NGO_2068 {ECO:0000313|EMBL:AAW90669.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90669.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90669.1; -; Genomic_DNA. DR RefSeq; WP_003705080.1; NC_002946.2. DR RefSeq; YP_209081.1; NC_002946.2. DR DNASU; 3282734; -. DR EnsemblBacteria; AAW90669; AAW90669; NGO_2068. DR GeneID; 3282734; -. DR KEGG; ngo:NGO2068; -. DR PATRIC; 20337967; VBINeiGon24812_2506. DR HOGENOM; HOG000218649; -. DR OMA; PPHNTAN; -. DR OrthoDB; EOG6WHNTR; -. DR BioCyc; NGON242231:GI2G-1963-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR002725; DUF45. DR Pfam; PF01863; DUF45; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 229 AA; 26220 MW; 658A779419BDC671 CRC64; MTSLIHTLSD GIELTVEINR RAKKNLIIRP IGTHTVRISV PPCFSVSALN RWLYENEAVL RRTLAKTPPH NTANRLPEHI WFHGRQLALT AHQDTQILLM PSEIRVPEGA PEKQLALLRD FLERQAHSYL IPRLERHARA TQLFPASSSL TSAKTFWGVC RKTTGIRLNR RLVGAPEYVA DYVCIHELCH LAHPDHSPAF WELTRRFAPY TPEAKQRIKI HGRELFALG // ID Q5F6X0_NEIG1 Unreviewed; 272 AA. AC Q5F6X0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Serine acetyltransferase {ECO:0000313|EMBL:AAW90067.1}; GN ORFNames=NGO_1423 {ECO:0000313|EMBL:AAW90067.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90067.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90067.1; -; Genomic_DNA. DR RefSeq; WP_003689278.1; NC_002946.2. DR RefSeq; YP_208479.1; NC_002946.2. DR ProteinModelPortal; Q5F6X0; -. DR SMR; Q5F6X0; 12-264. DR EnsemblBacteria; AAW90067; AAW90067; NGO_1423. DR GeneID; 3281764; -. DR KEGG; ngo:NGO1423; -. DR PATRIC; 20336259; VBINeiGon24812_1678. DR HOGENOM; HOG000049437; -. DR KO; K00640; -. DR OMA; FHALQSY; -. DR OrthoDB; EOG6HMXK6; -. DR BioCyc; NGON242231:GI2G-1332-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:InterPro. 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90067.1}. FT DOMAIN 13 117 SATase_N. {ECO:0000259|SMART:SM00971}. SQ SEQUENCE 272 AA; 29321 MW; 56EFC57B497CF960 CRC64; MKKNHLNTTG FDLWHTIREE TAAAAAAEPM LASFLHQTVL RHESLGSVLA YHLSSKLGSP IMDVRALFEI YQQALGSDTQ ISKCVEADLK AIYERDPACD EYSLPLLYFK GFHAIQAHRI NHRLYLDGRK TLAYFLQNRM SEVFGVDIHP AARLGYGLML DHATGFVAGE TAVLGNNISI LHGVTLGGSG KEGGDRHPKI GDGVMIGANA SILGNIRIGS NAKIGAGSVV VSDVPPSITV VGVPAKPVAR SLKTPSADMD QNIQFAEIDF MI // ID Q5FAD5_NEIG1 Unreviewed; 280 AA. AC Q5FAD5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:AAW88852.1}; GN ORFNames=NGO_0091 {ECO:0000313|EMBL:AAW88852.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88852.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88852.1; -; Genomic_DNA. DR RefSeq; WP_003687345.1; NC_002946.2. DR RefSeq; YP_207264.1; NC_002946.2. DR ProteinModelPortal; Q5FAD5; -. DR SMR; Q5FAD5; 2-254. DR EnsemblBacteria; AAW88852; AAW88852; NGO_0091. DR GeneID; 3282132; -. DR KEGG; ngo:NGO0091; -. DR PATRIC; 20333069; VBINeiGon24812_0118. DR HOGENOM; HOG000256248; -. DR KO; K07008; -. DR OMA; YWVFAHN; -. DR OrthoDB; EOG62K1T4; -. DR BioCyc; NGON242231:GI2G-81-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.60.20.10; -; 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:UP000000535}; KW Glutamine amidotransferase {ECO:0000313|EMBL:AAW88852.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88852.1}. FT DOMAIN 2 280 Glutamine amidotransferase type-2. FT {ECO:0000259|PROSITE:PS51278}. SQ SEQUENCE 280 AA; 31478 MW; 802C384E442A9E04 CRC64; MCQLLGMNCN TPTDIMFSFE GFRRRGGITD HHADGFGIGF FEGKGVRLFH DDKPSANSPV ADLVRAYQIK SENVVAHIRK ASQGQTSLAN THPFMREMWG GYWLFAHNGH LVDFFPEQGE FFHPVGTTDS ERAFCHILNR LRTRFAARPD DDTLFDAIAG LTHEIRKFGL FNFMLSDGIS LFAHASTLLH YIVRQAPFGK ARLLDDDVMV DFAEVTTPDD RVAVISTLPL TRDESWSQLA VNELVMFREG NIVRHDRPEN PVYMSAEEGL EIARAAGVSV // ID Q5F531_NEIG1 Unreviewed; 1468 AA. AC Q5F531; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=Adhesin {ECO:0000313|EMBL:AAW90706.1}; GN ORFNames=NGO_2105 {ECO:0000313|EMBL:AAW90706.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90706.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90706.1; -; Genomic_DNA. DR RefSeq; WP_010951407.1; NC_002946.2. DR RefSeq; YP_209118.1; NC_002946.2. DR ProteinModelPortal; Q5F531; -. DR MEROPS; S06.006; -. DR EnsemblBacteria; AAW90706; AAW90706; NGO_2105. DR GeneID; 3282812; -. DR KEGG; ngo:NGO2105; -. DR PATRIC; 20338049; VBINeiGon24812_2547. DR HOGENOM; HOG000218734; -. DR KO; K01347; -. DR OMA; YFIEREN; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NGON242231:GI2G-2000-MONOMER; -. DR Proteomes; UP000000535; 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 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; 2. 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; 2. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 43 310 Peptidase S6. FT {ECO:0000259|PROSITE:PS51691}. FT DOMAIN 1215 1468 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. SQ SEQUENCE 1468 AA; 160508 MW; 87F50E4F71FA6E35 CRC64; MKTTDKRTTE THRKAPKTGR IRFSPAYLAI CLSFGILPQA RAGHTYFGIN YQYYRDFAEN KGKFAVGAKD IEVYNKKGEL VGKSMTKAPM IDFSVVSRNG VAALAGDQYI VSVAHNGGYN NVDFGAEGSN PDQHRFSYQI VKRNNYKAGT NGHPYGGDYH MPRLHKFVTD AEPVEMTSYM DGWKYADLNK YPDRVRIGAG RQYWRSDEDE PNNRESSYHI ASAYSWLVGG NTFAQNGSGG GTVNLGSEKI KHSPYGFLPT GGSFGDSGSP MFIYDAQKQK WLINGVLQTG NPYIGKSNGF QLVRKDWFYD EIFAGDTHSV FYEPHQNGKY FFNDNNNGAG KIDAKHKHYS LPYRLKTRTV QLFNVSLSET AREPVYHAAG GVNSYRPRLN NGENISFIDK GKGELILTSN INQGAGGLYF EGNFTVSPKN NETWQGAGVH ISDGSTVTWK VNGVANDRLS KIGKGTLLVQ AKGENQGSVS VGDGKVILDQ QADDQGKKQA FSEIGLVSGR GTVQLNADNQ FNPDKLYFGF RGGRLDLNGH SLSFHRIQNT DEGAMIVNHN QDKESTVTIT GNKDITTTGN NNNLDSKKEI AYNGWFGEKD ATKTNGRLNL NYQPEEADRT LLLSGGTNLN GNITQTNGKL FFSGRPTPHA YNHLGSGWSK MEGIPQGEIV WDNDWIDRTF KAENFHIQGG QAVVSRNVAK VEGDWHLSNH AQAVFGVAPH QSHTICTRSD WTGLTSCTEK TITDDKVIAS LSKTDIRGNV SLADHAHLNL TGLATLNGNL SAGGDTHYTV TRNATQNGNL SLVGNAQATF NQATLNGNTS ASDNASFNLS NNAVQNGSLT LSDNAKANVS HSALNGNVSL ADKAVFHFEN SRFTGKISGG KDTALHLKDS EWTLPSGTEL GNLNLDNATI TLNSAYRHDA AGAQTGSAAD APRRRSRRSL LSVTPPTSAE SRFNTLTVNG KLNGQGTFRF MSELFGYRSG KLKLAESSEG TYTLAVNNTG NEPVSLEQLT VVEGKDNTPL SENLNFTLQN EHVDAGAWRY QLIRKDGEFR LHNPVKEQEL SDKLGKAGET EAALTAKQAQ LAAKQQAEKD NAQSLDALIA AGRNATEKAE SVAEPARQAG GENAGIMQAE EEKKRVQADK DTALAKQREA ETRPATTAFP RARRARRDLP QPQPQPQPQP QRDLISRYAN SGLSEFSATL NSVFAVQDEL DRVFAEDRRN AVWTSGIRDT KHYRSQDFRA YRQQTDLRQI GMQKNLGSGR VGILFSHNRT GNTFDDGIGN SARLAHGAVF GQYGIGRFDI GISAGAGFSS GSLSDGIRGK IRRRVLHYGI QARYRAGFGG FGIEPHIGAT RYFVQKADYR YENVNIATPG LAFNRYRAGI KADYSFKPAQ HISITPYLSL SYTDAASGKV RTRVNTAVLA QDFGKTRSAE WGVNAEIKGF TLSLHAAAAK GPQLEAQHSA GIKLGYRW // ID Q5F6H8_NEIG1 Unreviewed; 473 AA. AC Q5F6H8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. DE RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167}; DE EC=1.3.99.22 {ECO:0000256|PIRNR:PIRNR000167}; GN ORFNames=NGO_1580 {ECO:0000313|EMBL:AAW90209.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90209.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90209.1; -; Genomic_DNA. DR RefSeq; WP_003689506.1; NC_002946.2. DR RefSeq; YP_208621.1; NC_002946.2. DR ProteinModelPortal; Q5F6H8; -. DR EnsemblBacteria; AAW90209; AAW90209; NGO_1580. DR GeneID; 3281420; -. DR KEGG; ngo:NGO1580; -. DR PATRIC; 20336686; VBINeiGon24812_1889. DR HOGENOM; HOG000257214; -. DR KO; K02495; -. DR OMA; CEIDPRH; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; NGON242231:GI2G-1477-MONOMER; -. DR UniPathway; UPA00251; UER00323. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 54284 MW; 278EF30E98D750BE CRC64; MKIIQIQNNH NVNDDRPEFD RALIASLPAS GPRYTSYPTA DRFHDGFREG EYIKVLHLRG MGALNKPLSL YIHIPFCNTI CYYCGCNKII TKDKSRADTY IEYLEKEMEL LAPHLNGRHQ LAQLHFGGGT PTFLSDEQIE RVFRMIRKHF ELIPSGEYSI EIDPRKVSRD TVLMLGRLGF NRMSVGIQDF 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 Q5F7I6_NEIG1 Unreviewed; 72 AA. AC Q5F7I6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89851.1}; GN ORFNames=NGO_1191 {ECO:0000313|EMBL:AAW89851.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89851.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89851.1; -; Genomic_DNA. DR RefSeq; WP_003689624.1; NC_002946.2. DR RefSeq; YP_208263.1; NC_002946.2. DR EnsemblBacteria; AAW89851; AAW89851; NGO_1191. DR GeneID; 3282036; -. DR KEGG; ngo:NGO1191; -. DR PATRIC; 20335679; VBINeiGon24812_1398. DR HOGENOM; HOG000218730; -. DR OMA; LMGCDEQ; -. DR OrthoDB; EOG6MM1RZ; -. DR BioCyc; NGON242231:GI2G-1103-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 72 AA; 8207 MW; 7D2AB3461ACB9770 CRC64; MSMPEMPKWY GDDGQIVSCT EKVKVMSENM AELYQTAQDA FEDALLMGCG ERQLRAYLLA LIEGLENPYR KV // ID Q5F8M3_NEIG1 Unreviewed; 237 AA. AC Q5F8M3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Tetratricopeptide repeat family protein {ECO:0000313|EMBL:AAW89464.1}; GN ORFNames=NGO_0747 {ECO:0000313|EMBL:AAW89464.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89464.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89464.1; -; Genomic_DNA. DR RefSeq; WP_003697104.1; NC_002946.2. DR RefSeq; YP_207876.1; NC_002946.2. DR ProteinModelPortal; Q5F8M3; -. DR EnsemblBacteria; AAW89464; AAW89464; NGO_0747. DR GeneID; 3281461; -. DR KEGG; ngo:NGO0747; -. DR PATRIC; 20334634; VBINeiGon24812_0889. DR HOGENOM; HOG000219013; -. DR OMA; PTQENAS; -. DR OrthoDB; EOG6PCPVX; -. DR BioCyc; NGON242231:GI2G-704-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004255543. FT COILED 53 80 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 237 AA; 26163 MW; 72A48077208CF3B1 CRC64; MKTKLPLFII WLSVSASCAS VLPVPEGSRT EMPTQENASD GIPYPVPTLQ DRLDYLEGKI VRLSNEVEML NGKVKALEHT KIHPSGRTYV QKLDDRKLKE HYLNTEGGSA SAHTVETAQN LYNQALKHYQ NGRFSAAAAL LKGADGGDGG SIAQRSMYLL LQSRARMGNC ESVIEIGGRY ANRFKDSPTA PEVIFKIGEC QYRLQQKDIA RATWRSLIQT YPGSPAAKRA AAAVRKR // ID Q5FAA5_NEIG1 Unreviewed; 117 AA. AC Q5FAA5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88882.2}; GN ORFNames=NGO_0122 {ECO:0000313|EMBL:AAW88882.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88882.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88882.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88882; AAW88882; NGO_0122. DR PATRIC; 20333147; VBINeiGon24812_0157. DR HOGENOM; HOG000218785; -. DR OMA; SIKMIEL; -. DR OrthoDB; EOG65TRTR; -. DR BioCyc; NGON242231:GI2G-111-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 117 AA; 12189 MW; CA0A35AAA9D1F67E CRC64; MIELQLHELK LVSGGGPVTD NIAGNVANAA TTKGGPTWGD FVAIPAAAAT VHFLPKNFFG AIGANGVYNL TRDWVNDAVN APPYNGRPIF EIEHGLTAPA TKADKSGNGY TDGTDYC // ID Q5F5C0_NEIG1 Unreviewed; 408 AA. AC Q5F5C0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 58. DE SubName: Full=Hydrogenase expression protein {ECO:0000313|EMBL:AAW90617.1}; GN ORFNames=NGO_2009 {ECO:0000313|EMBL:AAW90617.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90617.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90617.1; -; Genomic_DNA. DR RefSeq; WP_003705129.1; NC_002946.2. DR RefSeq; YP_209029.1; NC_002946.2. DR EnsemblBacteria; AAW90617; AAW90617; NGO_2009. DR GeneID; 3282131; -. DR KEGG; ngo:NGO2009; -. DR PATRIC; 20337799; VBINeiGon24812_2423. DR HOGENOM; HOG000218719; -. DR OMA; FGLKGSW; -. DR OrthoDB; EOG6SFPCB; -. DR BioCyc; NGON242231:GI2G-1910-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 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 154 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 202 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 241 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 269 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 290 312 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 318 339 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 351 368 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 374 397 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 408 AA; 42587 MW; 06DCD0C490107957 CRC64; MSGNASSPSS SAAIGLVWFG AAVSIAEIST GTLLAPLGWQ RGLAALLLGH AVGGALFFAA AYIGALTGRS SMESVRLSFG KCGSVLFSVA NMLQLAGWTA VMIYVGATVS SALGKVLWDG ESFVWWALAN GALIVLWLVF GARRTGGLKT VSMLLMLLAV LWLSVEVFAS SGTNAAPAVS DGMTFGTAVE LSAVMPLSWL PLAADYTRQA RRPFAATLTA TLAYTLTGCW MYALGLAAAL FTGETDVAKI LLGAGLGITG ILAVVLSTVT TTFLDTYSAG ASANNISARF AEIPVAVGVT LIGTVLAVML PVTEYKNFLL LIGSVFAPMA AVLIADFFVL KRREEIEGFD FAGLVLWLAG FILYRFLLSS GWESSIGLTA PVMSAVAIAT VSVRLFFKKT QSLQRNPS // ID Q5F6M4_NEIG1 Unreviewed; 436 AA. AC Q5F6M4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Guanine permease {ECO:0000313|EMBL:AAW90163.1}; GN ORFNames=NGO_1527 {ECO:0000313|EMBL:AAW90163.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90163.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90163.1; -; Genomic_DNA. DR RefSeq; WP_003689428.1; NC_002946.2. DR RefSeq; YP_208575.1; NC_002946.2. DR EnsemblBacteria; AAW90163; AAW90163; NGO_1527. DR GeneID; 3281533; -. DR KEGG; ngo:NGO1527; -. DR PATRIC; 20336550; VBINeiGon24812_1823. DR HOGENOM; HOG000244362; -. DR KO; K06901; -. DR OMA; MVDFFDT; -. DR OrthoDB; EOG6DNT97; -. DR BioCyc; NGON242231:GI2G-1429-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 174 195 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 221 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; 46088 MW; 934C513C68B12ADF CRC64; MDISKQTLLD RVFNLKANGT TVRTELMAGL TTFLTMCYIV IVNPLILGET GMDMGAVFVA TCIASAIGCF VMGFIGNYPI ALAPGMGLNA YFTFAVVKGM GVPWQVALGA VFISGLIFIL FSFFKVREML VNALPMGLKM SIAAGIGLFL ALISLKGAGI IVANPATLVG LGDIHQPSAL LALFGFVMVV VLGYFRVQGA IIITILTITV IASLMGLNEF HGVVGEVPGI APTFMQMDFK GLFTVSMVSV IFVFFLVDLF DSTGTLVGVS HRAGLLVDGK LPRLKRALLA DSTAIVAGAA LGTSSTTPYV ESAAGVSAGG RTGLTAVTVG VLMLACLMFS PLAKSVPVFA TAPALLYVGT QMLRSARDID WDDMTEAAPA FLTIVFMPFT YSIADGIAFG FISYAVVKLL CRRTGDVPPM VWVVAVLWAL KFWYLG // ID Q5F9G2_NEIG1 Unreviewed; 307 AA. AC Q5F9G2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE SubName: Full=Pseudouridine synthase {ECO:0000313|EMBL:AAW89175.1}; GN ORFNames=NGO_0433 {ECO:0000313|EMBL:AAW89175.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89175.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89175.1; -; Genomic_DNA. DR RefSeq; WP_003696870.1; NC_002946.2. DR RefSeq; YP_207587.1; NC_002946.2. DR ProteinModelPortal; Q5F9G2; -. DR EnsemblBacteria; AAW89175; AAW89175; NGO_0433. DR GeneID; 3282061; -. DR KEGG; ngo:NGO0433; -. DR PATRIC; 20333881; VBINeiGon24812_0518. DR HOGENOM; HOG000275916; -. DR KO; K06177; -. DR OMA; GEYVEQT; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NGON242231:GI2G-410-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 103 253 PseudoU_synth_2. FT {ECO:0000259|Pfam:PF00849}. SQ SEQUENCE 307 AA; 35078 MW; E367C3B03B7F228A CRC64; MKKRNNPLPL LNGVKPSYLV LPHEKQFYGL PLLHFLCIRF PFLGADDWRR RLNSGFVVGS DGAALDEHSL FEPGKTMFYY RETGCESEPR IPFEEKILFV DEHLIVVDKP HFLPVIPGGR FLRETLLTRL RLRPELQHLN VEDITPIHRL DKDTAGVMLL SHNPATRGAY QTMFQNKTVW KTYEALAPTK TDLPYPLDVV SRLVRGEKFF TTQEAEGVPN AHTTVELIEN RGEFSLYRLT PHTGKKHQLR VHMMGLGMPL LNDALYPVPS EAGSEDYRKP LKLLAKKIAF ADPLSGRERV FCSGFCL // ID Q5F6L3_NEIG1 Unreviewed; 58 AA. AC Q5F6L3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90174.2}; GN ORFNames=NGO_1538 {ECO:0000313|EMBL:AAW90174.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90174.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90174.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90174; AAW90174; NGO_1538. DR PATRIC; 20336572; VBINeiGon24812_1834. DR HOGENOM; HOG000219097; -. DR OrthoDB; EOG6PW24H; -. DR BioCyc; NGON242231:GI2G-1440-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 58 AA; 6326 MW; 27B295981AF9E879 CRC64; MKSRRFFKAL LLIAALVGAF YAGMRTQAYL YEDLCLDLGG GKNPGSYPIC VIGKVPAR // ID Q5F7A3_NEIG1 Unreviewed; 251 AA. AC Q5F7A3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89934.1}; GN ORFNames=NGO_1277 {ECO:0000313|EMBL:AAW89934.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89934.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89934.1; -; Genomic_DNA. DR RefSeq; WP_003689183.1; NC_002946.2. DR RefSeq; YP_208346.1; NC_002946.2. DR ProteinModelPortal; Q5F7A3; -. DR EnsemblBacteria; AAW89934; AAW89934; NGO_1277. DR GeneID; 3282088; -. DR KEGG; ngo:NGO1277; -. DR PATRIC; 20335887; VBINeiGon24812_1498. DR HOGENOM; HOG000135466; -. DR OMA; YAAFMRY; -. DR OrthoDB; EOG6ZKXPR; -. DR BioCyc; NGON242231:GI2G-1192-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256217. FT DOMAIN 20 249 FGE-sulfatase. FT {ECO:0000259|Pfam:PF03781}. SQ SEQUENCE 251 AA; 27937 MW; 313210885685A9AF CRC64; MKYVRLFFLG TALAGTQAAA AEMVQIEGGS YRPLYLKKDT GLIKVKPFKL DKYPVTNAEF AEFVNSHPQW QKGRIGSKQA EPAYLKHWMK NGSRSYAPKA GELKQPVTNI SWFAANAYCA AQGKRLPTID EWEFAGLASA TQKNGSNEPG YNRTILDWYA DGGRKGLHDV GKDRPNYWGV YDMHGLIWEW TEDFNSSLLS SGNANAQMFC SGASVGASDS SNYAAFLRYG IRTSLQSKYV LHNLGFRCAS R // ID Q5FAI9_NEIG1 Unreviewed; 147 AA. AC Q5FAI9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88777.1}; GN ORFNames=NGO_0004 {ECO:0000313|EMBL:AAW88777.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88777.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88777.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88777; AAW88777; NGO_0004. DR KEGG; ngo:NGO0004; -. DR PATRIC; 20332836; VBINeiGon24812_0004. DR HOGENOM; HOG000218754; -. DR OMA; PIFAPAH; -. DR OrthoDB; EOG6J74V5; -. DR BioCyc; NGON242231:GI2G-4-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256098. SQ SEQUENCE 147 AA; 16214 MW; A39EB607173B92BA CRC64; MPPRLLSGIL CCLLTTAPVF AQGQPDAVSA YIQKKKVIVD TSKAELCFAD DRQCHPVLIG TATPKGTFGL TLNSTDKPGY GGEVIGFKQE GDFLFALHRV WNQIPSERRN ERIASPSVSD RIMTNGCINV SDAVYEKLRH YFVLEVI // ID Q5F5L1_NEIG1 Unreviewed; 130 AA. AC Q5F5L1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90526.1}; GN ORFNames=NGO_1913 {ECO:0000313|EMBL:AAW90526.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90526.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90526.1; -; Genomic_DNA. DR RefSeq; WP_003692089.1; NC_002946.2. DR RefSeq; YP_208938.1; NC_002946.2. DR EnsemblBacteria; AAW90526; AAW90526; NGO_1913. DR GeneID; 3282255; -. DR KEGG; ngo:NGO1913; -. DR PATRIC; 20337560; VBINeiGon24812_2308. DR OrthoDB; EOG6FNHWX; -. DR BioCyc; NGON242231:GI2G-1815-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 115 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 130 AA; 14696 MW; 675F848BE65F884F CRC64; MQKKRHSRRH LFIPTSSKHI SGLNIHSIPV LKGTGSHSVK KSGMSSAQQA NYPQNLFPTK NNPQVCTKGN PPYRHPFKTA IQMILKIKKS YPQKIPHINI IIVLLFKPYI LFITLQGNGT AKRKGIFSKN // ID Q5F6U1_NEIG1 Unreviewed; 417 AA. AC Q5F6U1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90096.1}; GN ORFNames=NGO_1455 {ECO:0000313|EMBL:AAW90096.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90096.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90096.1; -; Genomic_DNA. DR RefSeq; WP_003697398.1; NC_002946.2. DR RefSeq; YP_208508.1; NC_002946.2. DR EnsemblBacteria; AAW90096; AAW90096; NGO_1455. DR GeneID; 3281701; -. DR KEGG; ngo:NGO1455; -. DR PATRIC; 20336333; VBINeiGon24812_1715. DR HOGENOM; HOG000287672; -. DR OMA; MCMFGTT; -. DR OrthoDB; EOG6MWNC9; -. DR BioCyc; NGON242231:GI2G-1361-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 330 349 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 355 375 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 387 410 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 417 AA; 44843 MW; 8F728B5A001BA02C CRC64; MSEQHISTWK SKINALGPGI MMASAAVGGS HLIASTQAGA LYGWQLALII ILTNLFKYPF FRFSAHYTLD TGKSLIEGYA EKSCVYLWVF LILCIASATI NAGAVAIVTA AIVKMAIPSL MFDAGTVAAL IMASCLIILV SGRYRALDRV SKIIIVTLSI ATLAAAGIAM SRGMQMQPDF IEPTPWTLAG LGFLIALMGW MPAPIEISAI NSLWVTEKQR INPSEYRDGI FDFNVGYIAS AVLALVFLAL GAFVQYGNGE AVQMAGGKYI GQLINMYAVT IGGWSRPLVA FIAFACMYGT TITVVDGYAR AIAEPVRLLR GRDKTGNAEL FAWNIWVAGS GLAVIFWFDG AMAELLKFAM IAAFVSAPVF AWLNYRLVKG DKRHRLTAGM NALAIVGLLY LAGFAVLFLL NLTGLLA // ID Q5F8F4_NEIG1 Unreviewed; 133 AA. AC Q5F8F4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=tRNA synthetase RNA-binding protein {ECO:0000313|EMBL:AAW89533.1}; GN ORFNames=NGO_0822 {ECO:0000313|EMBL:AAW89533.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89533.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89533.1; -; Genomic_DNA. DR RefSeq; WP_003688587.1; NC_002946.2. DR RefSeq; YP_207945.1; NC_002946.2. DR ProteinModelPortal; Q5F8F4; -. DR EnsemblBacteria; AAW89533; AAW89533; NGO_0822. DR GeneID; 3282222; -. DR KEGG; ngo:NGO0822; -. DR PATRIC; 20334798; VBINeiGon24812_0969. DR HOGENOM; HOG000216822; -. DR KO; K04762; -. DR OMA; RFYKTRT; -. DR OrthoDB; EOG64NB4B; -. DR BioCyc; NGON242231:GI2G-775-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW. 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 Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:AAW89533.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW89533.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 10 72 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 133 AA; 15466 MW; 9F5229D2BD6974E4 CRC64; MKDKHDSSAM RLDKWLWAAR FFKTRSLAQK HIELGRVQVN GSKVKNSKTI DIGDIIDLTL NSLPHKIKVK GLNHQRRPAP EARLLYEEDA KTAALREECK QLDQFSRITS AHPDGRPTKR DRRQLDRLKK GDW // ID Q5F9M1_NEIG1 Unreviewed; 274 AA. AC Q5F9M1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 71. DE SubName: Full=Amino acid ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW89116.2}; GN ORFNames=NGO_0372 {ECO:0000313|EMBL:AAW89116.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89116.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:2YLN, ECO:0000213|PDB:3ZSF} RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 20-275. RX PubMed=22138345; DOI=10.1016/j.jmb.2011.11.030; RA Bulut H., Moniot S., Licht A., Scheffel F., Gathmann S., Saenger W., RA Schneider E.; RT "Crystal structures of two solute receptors for L-cystine and L- RT cysteine, respectively, of the human pathogen Neisseria gonorrhoeae."; RL J. Mol. Biol. 415:560-572(2012). 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; AE004969; AAW89116.2; -; Genomic_DNA. DR PDB; 2YLN; X-ray; 1.12 A; A=19-274. DR PDB; 3ZSF; X-ray; 2.32 A; A/B/C/D/E/F/G/H=16-274. DR PDBsum; 2YLN; -. DR PDBsum; 3ZSF; -. DR ProteinModelPortal; Q5F9M1; -. DR EnsemblBacteria; AAW89116; AAW89116; NGO_0372. DR PATRIC; 20333747; VBINeiGon24812_0451. DR HOGENOM; HOG000031895; -. DR OMA; ANEIDCA; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; NGON242231:GI2G-351-MONOMER; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2YLN, ECO:0000213|PDB:3ZSF}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 274 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364489. FT DOMAIN 49 270 PBPb. {ECO:0000259|SMART:SM00062}. SQ SEQUENCE 274 AA; 28712 MW; C609251E961219A1 CRC64; MLKKFVLGGI AALVLAACGG SEGGSGASSA PAQSAISGSL IERINNKGTV TVGTEGTYAP FTYHDKDGKL TGYDVEVTRA VAEKLGVKVE FKETQWDSMM AGLKAGRFDV VANQVGLTSP ERQATFDKSE PYSWSGAVLV AHNDSNIKSI ADIKGVKTAQ SLTSNYGEKA KAAGAQLVPV DGLAQSLTLI EQKRADATLN DELAVLDYLK KNPNAGVKIV WSAPADEKVG SGLIVNKGND EAVAKFSTAI NELKADGTLK KLGEQFFGKD ISVQ // ID Q5F9C3_NEIG1 Unreviewed; 137 AA. AC Q5F9C3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89214.1}; GN ORFNames=NGO_0476 {ECO:0000313|EMBL:AAW89214.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89214.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89214.1; -; Genomic_DNA. DR RefSeq; WP_003687963.1; NC_002946.2. DR RefSeq; YP_207626.1; NC_002946.2. DR EnsemblBacteria; AAW89214; AAW89214; NGO_0476. DR GeneID; 3282968; -. DR KEGG; ngo:NGO0476; -. DR OrthoDB; EOG68DD7H; -. DR BioCyc; NGON242231:GI2G-454-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 137 AA; 15576 MW; C639100295A5D883 CRC64; MIHLNVHYCD EIIRHAENDK YSLIGIFPDI CHIPTPQAIL GRLCLSVSFS AEGMDIQTMK TGQIFLEIVR NDDVISALEI PSYDGSDTEE NVSFMLHQTI SGLPVSDNDR IYVRMTTHNH ILSESRPLSF SWLPYHS // ID Q5F898_NEIG1 Unreviewed; 563 AA. AC Q5F898; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=D-lactate dehydrogenase {ECO:0000256|PIRNR:PIRNR000101}; DE EC=1.1.1.28 {ECO:0000256|PIRNR:PIRNR000101}; GN ORFNames=NGO_0890 {ECO:0000313|EMBL:AAW89589.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89589.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89589.1; -; Genomic_DNA. DR RefSeq; WP_003691095.1; NC_002946.2. DR RefSeq; YP_208001.1; NC_002946.2. DR ProteinModelPortal; Q5F898; -. DR SMR; Q5F898; 5-561. DR EnsemblBacteria; AAW89589; AAW89589; NGO_0890. DR GeneID; 3281117; -. DR KEGG; ngo:NGO0890; -. DR PATRIC; 20334953; VBINeiGon24812_1046. DR HOGENOM; HOG000122232; -. DR KO; K03777; -. DR OMA; RDRYEHH; -. DR OrthoDB; EOG6Z3KJX; -. DR BioCyc; NGON242231:GI2G-831-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW89589.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 36 266 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. SQ SEQUENCE 563 AA; 63390 MW; DC0C9B135682E23A CRC64; MNASQLISSL TQTVGEKYII TDPAKTEQYR QGYRFGEGKA LAVVRPGSIL EMWKILQACV EADVIVITQA ANTGLTGGST PDGNDYDRDI VIVNTMRMNI IQTINNNEQV VCLPGSTLNQ LELLLKPLGR EPHSVIGSSC IGASVLGGVC NNSGGALVQR GPAYTEMALF AQINEEGRLE LVNHLGIDLG DTPEEILTNL QGHHYQKKDI KQDAGKGHDH AYCEHVRQVD EPTAARFNAD PARHYEASGC AGKLMVFAVR LDTFPQEKQT AVFYIGTNDI NELTDIRRAA LGEFESLPVS GEYIHRHAFD IADVYGKDTF YVIKKFGTHQ LPKLFDLKAR VDRFGKKVSF LPKHFSDKAM QFVSKFLPDH LPKSMRDYRD KYEHHLILKM GGKGVDEARA FLKEYFSHHG GAFFECNAEE TQAAMLHRFA VASAAIRYRS VHDDEVEDLV ALDIALRRDD RDWFEKLPPE IDNKIIHKLY YGHFMCHVFH QDYIIKKGNG CMALEHEMLH LLDQRGAQYP AEHNVGHLYE AKPALKQFYR KLDPTNSFNP GIGKTSKKKN WAE // ID Q5F7Y4_NEIG1 Unreviewed; 66 AA. AC Q5F7Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89703.1}; GN ORFNames=NGO_1027 {ECO:0000313|EMBL:AAW89703.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89703.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89703.1; -; Genomic_DNA. DR RefSeq; WP_003688228.1; NC_002946.2. DR RefSeq; YP_208115.1; NC_002946.2. DR EnsemblBacteria; AAW89703; AAW89703; NGO_1027. DR GeneID; 3281637; -. DR KEGG; ngo:NGO1027; -. DR HOGENOM; HOG000027845; -. DR OMA; FVYELAP; -. DR OrthoDB; EOG6TJ84R; -. DR BioCyc; NGON242231:GI2G-948-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41 60 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 66 AA; 7351 MW; 03461377877F6A98 CRC64; MLSRKGRTRG KAAAGGGRWG RIFDLRAKPA IIPFEIKRYR LCAGLLIAFV YELAPAVLPI RGCLFF // ID Q5F847_NEIG1 Unreviewed; 310 AA. AC Q5F847; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Proline iminopeptidase {ECO:0000256|RuleBase:RU003421}; DE EC=3.4.11.5 {ECO:0000256|RuleBase:RU003421}; GN ORFNames=NGO_0949 {ECO:0000313|EMBL:AAW89640.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89640.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Release of N-terminal proline from a peptide. CC {ECO:0000256|RuleBase:RU003421}. CC -!- SIMILARITY: Belongs to the peptidase S33 family. CC {ECO:0000256|RuleBase:RU003421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89640.1; -; Genomic_DNA. DR RefSeq; WP_003688351.1; NC_002946.2. DR RefSeq; YP_208052.1; NC_002946.2. DR ProteinModelPortal; Q5F847; -. DR ESTHER; neigo-pip; Proline_iminopeptidase. DR EnsemblBacteria; AAW89640; AAW89640; NGO_0949. DR GeneID; 3282130; -. DR KEGG; ngo:NGO0949; -. DR PATRIC; 20335081; VBINeiGon24812_1110. DR HOGENOM; HOG000171480; -. DR KO; K01259; -. DR OMA; VSEMFPD; -. DR OrthoDB; EOG6BPDDC; -. DR BioCyc; NGON242231:GI2G-882-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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 {ECO:0000256|RuleBase:RU003421}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU003421}; KW Protease {ECO:0000256|RuleBase:RU003421}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 33 290 AB_hydrolase_1. FT {ECO:0000259|Pfam:PF00561}. FT ACT_SITE 107 107 Nucleophile. FT {ECO:0000256|PIRSR:PIRSR006431-1}. FT ACT_SITE 260 260 {ECO:0000256|PIRSR:PIRSR006431-1}. FT ACT_SITE 287 287 Proton donor. FT {ECO:0000256|PIRSR:PIRSR006431-1}. SQ SEQUENCE 310 AA; 34792 MW; D0E7AEBA908A1AE0 CRC64; MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI VIIDQRGCGR SHPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH PERVKGLVLR GIFLCRPSET AWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL FHQDEEVCLS AAKAWADWES YLIRFEPEGV DEDAYASLAI ARLENHYFVN GGWLQGDKAI LNNIGKIRHI PTVIVQGRYD LCTPMQSAWE LSKAFPEAEL RVVQAGHCAF DPPLADALVQ AVEDILPRLL // ID Q5F5J2_NEIG1 Unreviewed; 226 AA. AC Q5F5J2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 56. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AAW90545.1}; GN ORFNames=NGO_1932 {ECO:0000313|EMBL:AAW90545.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90545.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90545.1; -; Genomic_DNA. DR RefSeq; WP_003688090.1; NC_002946.2. DR RefSeq; YP_208957.1; NC_002946.2. DR ProteinModelPortal; Q5F5J2; -. DR EnsemblBacteria; AAW90545; AAW90545; NGO_1932. DR GeneID; 3282687; -. DR KEGG; ngo:NGO1932; -. DR PATRIC; 20337604; VBINeiGon24812_2329. DR HOGENOM; HOG000225518; -. DR OMA; YVPYADI; -. DR OrthoDB; EOG60SCKQ; -. DR BioCyc; NGON242231:GI2G-1835-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW90545.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90545.1}. FT DOMAIN 5 144 TsaA-like. {ECO:0000259|PROSITE:PS51668}. SQ SEQUENCE 226 AA; 25160 MW; 35B6884EC51FC68E CRC64; MTYTITPIGT ARSPYKQKFG IARQPGLVSA AEACIELNPE FTADSVRGLE DFDYVWISFI FHGVLDEGWA QMVRPPRLGG KQKMGVFATR SPHRPNHLGL SLLKLERIET GKPVRLYCSG SDLLDGTPIV DIKPYIPFIE SKPDAASGFV SGKPVELEVV WQENIGAENL SANTKNLISQ SIAQDPRPAY QNIPERIYVM NIADYEVRFQ IEENRATVIN LSPTPL // ID Q5F785_NEIG1 Unreviewed; 90 AA. AC Q5F785; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=UPF0237 protein NGO_1298 {ECO:0000256|HAMAP-Rule:MF_01054}; GN ORFNames=NGO_1298 {ECO:0000313|EMBL:AAW89952.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89952.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the UPF0237 family. {ECO:0000256|HAMAP- CC Rule:MF_01054}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000256|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; AE004969; AAW89952.1; -; Genomic_DNA. DR RefSeq; WP_003691603.1; NC_002946.2. DR RefSeq; YP_208364.1; NC_002946.2. DR ProteinModelPortal; Q5F785; -. DR EnsemblBacteria; AAW89952; AAW89952; NGO_1298. DR GeneID; 3282120; -. DR KEGG; ngo:NGO1298; -. DR PATRIC; 20335943; VBINeiGon24812_1526. DR HOGENOM; HOG000241054; -. DR KO; K07166; -. DR OMA; IFKYMHR; -. DR OrthoDB; EOG6ZPT4H; -. DR BioCyc; NGON242231:GI2G-1210-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 79 ACT. {ECO:0000256|HAMAP-Rule:MF_01054, FT ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 90 AA; 10414 MW; 5342EB32ED0621C4 CRC64; MNNSVITVIG KDRVGIVYDV SKILAENRIN ILNISQQLMD DFFTMIILVD TSKCPKSRQE ILDLFAEESK KLALDIRMQN EEIFQAMHRI // ID Q5F9D4_NEIG1 Unreviewed; 178 AA. AC Q5F9D4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89203.1}; GN ORFNames=NGO_0465 {ECO:0000313|EMBL:AAW89203.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89203.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89203.1; -; Genomic_DNA. DR RefSeq; WP_010951051.1; NC_002946.2. DR RefSeq; YP_207615.1; NC_002946.2. DR EnsemblBacteria; AAW89203; AAW89203; NGO_0465. DR GeneID; 3282981; -. DR KEGG; ngo:NGO0465; -. DR PATRIC; 20333968; VBINeiGon24812_0556. DR HOGENOM; HOG000071248; -. DR OMA; EFHAVEI; -. DR OrthoDB; EOG6JMN2V; -. DR BioCyc; NGON242231:GI2G-443-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 178 AA; 19973 MW; AE9B9DDC34F5CFBE CRC64; MQTVATKPTA KQMLAAKRAA KESTRQERAV KRAGTVRNVD RNRLSARSKA QKENIARMLS GAKVSEDEAL TCGIMMRLVA AKVRRYCGEH PGVFDGAAGS RQLERYIKPS EFHAVEIQPE ACKALLQNYP AAAGNLGRRK QKKPRVRKRI SPSRMARPNR KQSERRMGKG AKLKYRTN // ID Q5F574_NEIG1 Unreviewed; 333 AA. AC Q5F574; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW90663.1}; GN ORFNames=NGO_2056 {ECO:0000313|EMBL:AAW90663.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90663.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90663.1; -; Genomic_DNA. DR RefSeq; WP_003686999.1; NC_002946.2. DR RefSeq; YP_209075.1; NC_002946.2. DR ProteinModelPortal; Q5F574; -. DR EnsemblBacteria; AAW90663; AAW90663; NGO_2056. DR GeneID; 3282740; -. DR KEGG; ngo:NGO2056; -. DR PATRIC; 20337913; VBINeiGon24812_2479. DR HOGENOM; HOG000272498; -. DR KO; K02064; -. DR OMA; DICVNYD; -. DR OrthoDB; EOG6D8BCG; -. DR BioCyc; NGON242231:GI2G-1957-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256020. SQ SEQUENCE 333 AA; 36324 MW; A89EFAE439B8A0CB CRC64; MKRKIWLLPL LAVSAYLQAQ TEVRLAVHKS FSLPKGLIAR FERANDAKVS IIQAGGANEM LNKLILSRAN PIADAVYGLD NANIGKAREM GILAAAQPES APVAVGLPSA LAVDYGYVSV NYDKKWFEGK KLPLPQTLQD LTRPEYKNLL VVPSPATSSP GLGFLMANIG GLGEEGAFKW WAQMRQNGVK VAKGWSEAYY TDFSHNGGAY PLVVGYAASP AAEVYFSKGK YSEPPTGNLF LKGGVFRQVE GAAVLKGAKQ PKLAAKLVQW LQSLEVQQAV PSEMWVYPAV KNTRLPDVFR FAQAPAHTTA PAQRDIDANQ RGWVSRWIRT VLK // ID Q5F6K3_NEIG1 Unreviewed; 214 AA. AC Q5F6K3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488}; GN ORFNames=NGO_1548 {ECO:0000313|EMBL:AAW90184.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90184.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90184.1; -; Genomic_DNA. DR RefSeq; WP_003689466.1; NC_002946.2. DR RefSeq; YP_208596.1; NC_002946.2. DR ProteinModelPortal; Q5F6K3; -. DR DNASU; 3281487; -. DR EnsemblBacteria; AAW90184; AAW90184; NGO_1548. DR GeneID; 3281487; -. DR KEGG; ngo:NGO1548; -. DR PATRIC; 20336598; VBINeiGon24812_1845. DR HOGENOM; HOG000265318; -. DR KO; K03673; -. DR OMA; PHCYKFE; -. DR OrthoDB; EOG68Q0Q6; -. DR BioCyc; NGON242231:GI2G-1452-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488}; KW Periplasm {ECO:0000256|PIRNR:PIRNR001488}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256593. 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; 24003 MW; 31A85BBA5EB3CE18 CRC64; MKFKHLLPLL LSAVLSAQAY ALTEGEDYLV LDKPIPQEQP GKIEVLEFFG YFCVHCHHFD PLLLKLGKAL PSDTYLRTEH VVWRPEMLGL ARMAAAVKLS GLKYQANSAV FKAVYEQKIR LENRAVAGKW ALSQKGFDGK KLMRAYDSPE AAAVALKMQK LTEQYGIDST PTVIVGGKYR VIFNNGFDGG VHTIKELVAK VREERKRQTP AVQK // ID Q5F6G6_NEIG1 Unreviewed; 139 AA. AC Q5F6G6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90221.2}; GN ORFNames=NGO_1593 {ECO:0000313|EMBL:AAW90221.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90221.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90221.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90221; AAW90221; NGO_1593. DR HOGENOM; HOG000027892; -. DR OrthoDB; EOG68DD3F; -. DR BioCyc; NGON242231:GI2G-1489-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025361; DUF4265. DR Pfam; PF14085; DUF4265; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 139 AA; 15735 MW; 28A0DAA4E5850D9F CRC64; MKSKLTVVYY DLESNIAEEI LSGNIMPDGN FLIQEIPLFA PNLALNDIVA IEREDKMLFF DHLIKASGNT TINIVVLDHF PKDLLAAIEE HSGKIRKNGE NYLSVNFPPK KYNSDLKGIL NRYEEANILS YREACLGFS // ID Q5F5C6_NEIG1 Unreviewed; 40 AA. AC Q5F5C6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90611.1}; GN ORFNames=NGO_2003 {ECO:0000313|EMBL:AAW90611.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90611.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90611.1; -; Genomic_DNA. DR RefSeq; WP_010355812.1; NC_002946.2. DR RefSeq; YP_209023.1; NC_002946.2. DR EnsemblBacteria; AAW90611; AAW90611; NGO_2003. DR GeneID; 3282621; -. DR KEGG; ngo:NGO2003; -. DR PATRIC; 20337783; VBINeiGon24812_2415. DR OrthoDB; EOG6P073Q; -. DR BioCyc; NGON242231:GI2G-1904-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 40 AA; 4545 MW; C85FF0AE5E8C5B03 CRC64; MPADPDLSGA MKVCRPKSQT SADRLICLFF IALQKIRIYF // ID Q5F6X3_NEIG1 Unreviewed; 351 AA. AC Q5F6X3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 11-MAY-2016, entry version 60. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|RuleBase:RU363002}; DE EC=2.7.1.180 {ECO:0000256|RuleBase:RU363002}; GN ORFNames=NGO_1420 {ECO:0000313|EMBL:AAW90064.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90064.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90064.1; -; Genomic_DNA. DR RefSeq; WP_003693694.1; NC_002946.2. DR RefSeq; YP_208476.1; NC_002946.2. DR ProteinModelPortal; Q5F6X3; -. DR EnsemblBacteria; AAW90064; AAW90064; NGO_1420. DR GeneID; 3281796; -. DR KEGG; ngo:NGO1420; -. DR PATRIC; 20336249; VBINeiGon24812_1673. DR HOGENOM; HOG000080808; -. DR KO; K03734; -. DR OMA; MGTFWRV; -. DR OrthoDB; EOG6CGCF7; -. DR BioCyc; NGON242231:GI2G-1329-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW FAD {ECO:0000256|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|RuleBase:RU363002}; KW Lipoprotein {ECO:0000256|RuleBase:RU363002}; 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:UP000000535}; 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; 38614 MW; 6386657B673B24F2 CRC64; MPSETRLPNL IRALIFALGF IFLNACSEQT AQTVTLQGET MGTTYTVKYL SNNRDKLPSP AKIQKRIDDA LKEVNRQMST YQTDSEISRF NQHTAGKPLR ISSDFAHVTA EAVRLNRLTH GALDVTVGPL VNLWGFGPDK SVTREPSPEQ IKQAASYTGI DKIILQQGKD YASLSKTHPK AYLDLSSIAK GFGVDKVAGE LEKYGIQNYL VEIGGELHGK GKNAHGEPWR IGIEQPNIIQ GGNTQIIVPL NNRSLATSGD YRIFHVDKNG KRLSHIINPN NKRPISHNLA SISVVSDSAM TADGLSTGLF VLGETEALRL AEQEKLAVFL IVRDKDGYRT AMSSEFAKLL R // ID Q5F7G8_NEIG1 Unreviewed; 128 AA. AC Q5F7G8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89869.1}; GN ORFNames=NGO_1210 {ECO:0000313|EMBL:AAW89869.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89869.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89869.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89869; AAW89869; NGO_1210. DR PATRIC; 20335725; VBINeiGon24812_1421. DR OrthoDB; EOG65XN2G; -. DR BioCyc; NGON242231:GI2G-1121-MONOMER; -. DR Proteomes; UP000000535; 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 SUPFAM; SSF143422; SSF143422; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 128 AA; 14266 MW; 1CB722F19B5D2DA9 CRC64; METSGPTKLN LKQQTIPSPT PQPQTKILWR VIAETSLPAA HSFSPSNPPP RNRVCLSDIS ASRAAYMDVQ KQYPFETVAV CVLPNHIHAI WTLPPDDADY SLLRRLIKTK FSAYSPHTKN LGAVLDYP // ID Q5F7I2_NEIG1 Unreviewed; 469 AA. AC Q5F7I2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. DE SubName: Full=Chloride channel protein EriC {ECO:0000313|EMBL:AAW89855.1}; GN ORFNames=NGO_1195 {ECO:0000313|EMBL:AAW89855.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89855.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89855.1; -; Genomic_DNA. DR RefSeq; WP_003697502.1; NC_002946.2. DR RefSeq; YP_208267.1; NC_002946.2. DR ProteinModelPortal; Q5F7I2; -. DR EnsemblBacteria; AAW89855; AAW89855; NGO_1195. DR GeneID; 3282040; -. DR KEGG; ngo:NGO1195; -. DR PATRIC; 20335689; VBINeiGon24812_1403. DR HOGENOM; HOG000257545; -. DR OMA; EMTDNHA; -. DR OrthoDB; EOG6C0143; -. DR BioCyc; NGON242231:GI2G-1107-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00438323, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 49985 MW; B4084FB5F481AC9C CRC64; MTSTFPRRLA RKIRQTRRLS RKSIAFLFLL AGSALVALTA LFFAHLADFA LELNAKLVQQ YPWFAWIALP PGLPVIVWLT RKFAPFTAGS GIPQVIASLS LPYGAQKTRL IRLGQTLLKI PLTFLGMLFG ASIGREGPSV QVGAAVMGAW GAWCKKHGLA FKGMQENDLM AAGAAGGLAA AFNAPLAGVI FAIEELGRGI MLRWERQILL GVLAAGFIQV AIQGNNPYFS GFNGGVLENI LMWIVAAGLV CGAAGGIFAR MLYRGAAAFA PRKIRGFIRN RPLLLAALMG LLLALLGTFY QGKTYGTGYH EAAQALHGIY EAPVGLAAAK WLATVFSYWA GIPGGIFTPS LTIGAVLGEH IAAIADISQG ANIIVLICMA AFLAGATQSP ITSAVVVMEM TGGQSLLFWM LIACIFASQV SRQFSPRPFY HASGMRFRRR VLQETAAQTG NAPARPQAAN SKTGMPSEN // ID Q5F7R4_NEIG1 Unreviewed; 49 AA. AC Q5F7R4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89773.1}; GN ORFNames=NGO_1106 {ECO:0000313|EMBL:AAW89773.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89773.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89773.1; -; Genomic_DNA. DR RefSeq; WP_010360014.1; NC_002946.2. DR RefSeq; YP_208185.1; NC_002946.2. DR EnsemblBacteria; AAW89773; AAW89773; NGO_1106. DR GeneID; 3281933; -. DR KEGG; ngo:NGO1106; -. DR PATRIC; 20335462; VBINeiGon24812_1297. DR HOGENOM; HOG000071251; -. DR BioCyc; NGON242231:GI2G-1018-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5247 MW; 926DCB9CE05F56CC CRC64; MDTLLSIITA LSFGGAATLA VWLLVEAADA VLRRKRDGKG EDDFDGFGY // ID Q5F8Q4_NEIG1 Unreviewed; 212 AA. AC Q5F8Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=2-dehydro-3-deoxyphosphogluconate aldolase {ECO:0000313|EMBL:AAW89433.1}; GN ORFNames=NGO_0713 {ECO:0000313|EMBL:AAW89433.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89433.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89433.1; -; Genomic_DNA. DR RefSeq; WP_003695341.1; NC_002946.2. DR RefSeq; YP_207845.1; NC_002946.2. DR ProteinModelPortal; Q5F8Q4; -. DR EnsemblBacteria; AAW89433; AAW89433; NGO_0713. DR GeneID; 3282885; -. DR KEGG; ngo:NGO0713; -. DR PATRIC; 20334552; VBINeiGon24812_0848. DR HOGENOM; HOG000233114; -. DR KO; K01625; -. DR OMA; KFFPAEY; -. DR OrthoDB; EOG67DPKT; -. DR BioCyc; NGON242231:GI2G-673-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 212 AA; 22005 MW; 013D19E4A10C0A05 CRC64; MSKLTPREIL TAGAVVPVMA IDDLSTAVDL SRALVEGGIP TLEITLRTPV GLEAIRLIAK EMPNAIIGAG TVTNPEQLKA VEDAGAVFAI SPGLHESLAR AGRNSGIPLI PGVATPGEVQ LALEHGIDTL KLFPAEVVGG KAMLKALYGP YADVRFCPTG GISLATAPDY LALPNVLCVG GSWLTPKEAV KNKDWDTITR LAKEAAALKP KA // ID Q5F731_NEIG1 Unreviewed; 444 AA. AC Q5F731; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185}; GN ORFNames=NGO_1358 {ECO:0000313|EMBL:AAW90006.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90006.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90006.1; -; Genomic_DNA. DR RefSeq; WP_003691714.1; NC_002946.2. DR RefSeq; YP_208418.1; NC_002946.2. DR ProteinModelPortal; Q5F731; -. DR SMR; Q5F731; 3-444. DR EnsemblBacteria; AAW90006; AAW90006; NGO_1358. DR GeneID; 3282370; -. DR KEGG; ngo:NGO1358; -. DR PATRIC; 20336101; VBINeiGon24812_1599. DR HOGENOM; HOG000243799; -. DR KO; K00262; -. DR OMA; VPWVDDA; -. DR OrthoDB; EOG65XN4D; -. DR BioCyc; NGON242231:GI2G-1271-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 201 443 ELFV_dehydrog. FT {ECO:0000259|SMART:SM00839}. SQ SEQUENCE 444 AA; 48473 MW; 934D50EE07FCFE3A CRC64; MTDLNTLFAN LKQRNPNQEP FHQAVEEVFM SLDPFLAKNP KYTQQSLLER IVEPERVVMF RVTWQDDKGQ VQVNRGYRVQ MSSAIGPYKG GLRFHPTVDL GVLKFLAFEQ VFKNALTTLP MGGGKGGSDF DPKGKSDAEV MRFCQAFMTE LYRHIGADTD VPAGDIGVGG REIGYLFGQY KKIRNEFTSV LTGKGLEWGG SLIRPEATGY GCVYFAQAML QTRNDSFEGK RVLISGSGNV AQYAAEKAIQ LGAKVLTVSD SDGFVLFPDI GMTEAQLAAL IELKEVRRER VATYAKEQGL QYFENQKPWG VAAEIALPCA TQNELDEEAA KTLLANGCYV VAEGANMPST LGAVEQFIKA GILYAPGKAS NAGGVATSGL EMSQNAIRLS WAREEVDSRL FGIMQSIHES CLKYGKVGDK VNYVNGANIA GFVKVADAML AQGF // ID Q5FAK9_NEIG1 Unreviewed; 318 AA. AC Q5FAK9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 73. DE SubName: Full=AraC family transcriptional regulator {ECO:0000313|EMBL:AAW88794.1}; GN ORFNames=NGO_0025 {ECO:0000313|EMBL:AAW88794.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88794.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88794.1; -; Genomic_DNA. DR RefSeq; WP_003694694.1; NC_002946.2. DR RefSeq; YP_207206.1; NC_002946.2. DR ProteinModelPortal; Q5FAK9; -. DR EnsemblBacteria; AAW88794; AAW88794; NGO_0025. DR GeneID; 3283069; -. DR KEGG; ngo:NGO0025; -. DR PATRIC; 20332880; VBINeiGon24812_0025. DR HOGENOM; HOG000218757; -. DR OMA; PSAGEIX; -. DR OrthoDB; EOG63Z765; -. DR BioCyc; NGON242231:GI2G-22-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 221 318 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 318 AA; 35763 MW; B10D2ABBB27F6ECF CRC64; MNTAAIYRQY QTYVRSDKSG WALDGCSDSA LIAQAKQPGL HLKMCINRFD SGITLSRMRG GGTGAFPTEI HNFSHNCALF VMVSGQNRLQ MGGREYRPSA GEIWLVRGEL ADVSETLLPD SGGMCALHLD FSLEKLRRWH DEGLLDERLF SPQTIGRFAL QRLAQNAGTL TAAACPLLQR PFESDGFGLL ADEADALELS ARLLRFTFRR HDNGYRRRRI DEAADILNSE FARPLTIAEI ARRVGLNECY LKRYFKAQTG ETVAGRLRRL RLEHALALIE SGSTIQAAMH FCGYRHAGRF NEAFRRHYGF LPSDVKKC // ID Q5F740_NEIG1 Unreviewed; 105 AA. AC Q5F740; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 49. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89997.2}; GN ORFNames=NGO_1347 {ECO:0000313|EMBL:AAW89997.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89997.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89997.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89997; AAW89997; NGO_1347. DR PATRIC; 20336067; VBINeiGon24812_1583. DR HOGENOM; HOG000282159; -. DR OMA; WALYSGG; -. DR OrthoDB; EOG680X0R; -. DR BioCyc; NGON242231:GI2G-1261-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 70 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 76 98 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 105 AA; 12142 MW; BB5E3C4A08C42F4B CRC64; MYWYPVLVNL MMLAVFGSSL FAGQTVIEKL ARLQQPDLPE KAVRYTRRVT QVWCVFFIAN GTLAALLARL GRYDWWAVYT GVIAYVLMGM LFAGEWLYRK LVLKV // ID Q5F8M1_NEIG1 Unreviewed; 302 AA. AC Q5F8M1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89466.1}; GN ORFNames=NGO_0751 {ECO:0000313|EMBL:AAW89466.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89466.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89466.1; -; Genomic_DNA. DR RefSeq; WP_003688683.1; NC_002946.2. DR RefSeq; YP_207878.1; NC_002946.2. DR ProteinModelPortal; Q5F8M1; -. DR EnsemblBacteria; AAW89466; AAW89466; NGO_0751. DR GeneID; 3282603; -. DR KEGG; ngo:NGO0751; -. DR PATRIC; 20334646; VBINeiGon24812_0895. DR HOGENOM; HOG000071292; -. DR OMA; MEFKSED; -. DR OrthoDB; EOG6J74T6; -. DR BioCyc; NGON242231:GI2G-706-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR InterPro; IPR006315; OM_autotransptr_brl. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 302 AA; 32404 MW; 301D63B74A156600 CRC64; MRFPLPITNA VLKITNGAME FKSEDIGTIK LTKATFHLKK DTSLTTPEGT TLLSGGTLTL SNTGISLSGT TSVFEKGTFT NGGIITLANQ SYADKLTIEG NYVGKDGVLK VNTEWNSPGD DQGGNSQSDL LEITGDASGK TTVISVGKDG KENIIDGSIG ELSDRYKRSA AVVKVLGQDK GAETGKLNIE DAKHTYTMRD TFSGTAKTTG AGELQLVSHK DEAGATEYFW TLTTPNQDKT IITPSAPAYA LVPRQNLESG YAMLDTLHQR RGENQTLSRD RQGNYRQDAE ATDIKATKAP WV // ID Q5F566_NEIG1 Unreviewed; 187 AA. AC Q5F566; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|PIRNR:PIRNR004682}; DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682}; GN ORFNames=NGO_2070 {ECO:0000313|EMBL:AAW90671.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90671.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004682, CC ECO:0000256|SAAS:SAAS00078038}. CC -!- SIMILARITY: Belongs to the gmhB family. CC {ECO:0000256|PIRNR:PIRNR004682}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90671.1; -; Genomic_DNA. DR RefSeq; WP_003705078.1; NC_002946.2. DR RefSeq; YP_209083.1; NC_002946.2. DR ProteinModelPortal; Q5F566; -. DR EnsemblBacteria; AAW90671; AAW90671; NGO_2070. DR GeneID; 3282847; -. DR KEGG; ngo:NGO2070; -. DR PATRIC; 20337971; VBINeiGon24812_2508. DR HOGENOM; HOG000016503; -. DR KO; K03273; -. DR OMA; DEWVALP; -. DR OrthoDB; EOG68SVXZ; -. DR BioCyc; NGON242231:GI2G-1965-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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 {ECO:0000256|PIRNR:PIRNR004682}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR004682, KW ECO:0000256|SAAS:SAAS00455224}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR004682, KW ECO:0000256|SAAS:SAAS00455242}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 187 AA; 20524 MW; 774689FB16D9F8D8 CRC64; MKLIILDRDG VINRDRDDFV KSADEWIPVE GSMDAVAFLT QAGCTVAVAT NQSGIGRKYF TVQDLTEMHA KMHRLIRQAG GEIDGIWFCP HTGADGCNCR KPKPGMIEDI LERFNAQASE TWLVGDSLRD LQAIDAVGGK PALVLTGKGK KTLSQHGHEL PGHTQVFDTL LDFSQYIMQE NAAPQAD // ID Q5F735_NEIG1 Unreviewed; 252 AA. AC Q5F735; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 59. DE SubName: Full=Beta-1,4-glucosyltransferase {ECO:0000313|EMBL:AAW90002.2}; GN ORFNames=NGO_1353 {ECO:0000313|EMBL:AAW90002.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90002.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90002.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F735; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAW90002; AAW90002; NGO_1353. DR PATRIC; 20336087; VBINeiGon24812_1592. DR HOGENOM; HOG000262849; -. DR OMA; DWPGFGK; -. DR OrthoDB; EOG6W19MV; -. DR BioCyc; NGON242231:GI2G-1267-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90002.2}. FT DOMAIN 5 117 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 252 AA; 29328 MW; B8EB51A9D035EA0A CRC64; MKKVSVLIVA KNEANHIREC IESCRFDKEV IVIDDHSADN TAEIAEGLGA KVFRRHLNGD FGAQKTFAIE QAGGEWVFLI DADERCTPEL SDEISKIVRT GDYAAYFVER RNLFPNHPAT HGAMRPDSVC RLMPKKGGSV QGKVHETVQT PYPERRLKHF MYHYTYDNWE QYFNKFNKYT SISAEKYREQ GKPVSFVRDI ILRPIWGFFK IYILNKGFLD GKMGWIMSVN HSYYTMIKYV KLYYLYKSGG KF // ID Q5F606_NEIG1 Unreviewed; 157 AA. AC Q5F606; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90381.1}; GN ORFNames=NGO_1760 {ECO:0000313|EMBL:AAW90381.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90381.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90381.1; -; Genomic_DNA. DR RefSeq; WP_003694272.1; NC_002946.2. DR RefSeq; YP_208793.1; NC_002946.2. DR EnsemblBacteria; AAW90381; AAW90381; NGO_1760. DR GeneID; 3282555; -. DR KEGG; ngo:NGO1760; -. DR PATRIC; 20337134; VBINeiGon24812_2107. DR HOGENOM; HOG000218651; -. DR OMA; YENKYLG; -. DR OrthoDB; EOG6SBT2N; -. DR BioCyc; NGON242231:GI2G-1656-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR016630; UCP015278. DR Pfam; PF10004; DUF2247; 1. DR PIRSF; PIRSF015278; UCP015278; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 157 AA; 18462 MW; C5F7E015241ED30E CRC64; MNLDLTAQKV RLSWKDILWG YENKYLGWAD VAAYARKMTL SDHDERVFKL SLTNKSNILE LKPVLEDLAS ETRGYSPKNW LYILLNDVFH RKEEFYGPLG EVEKIYADFD YPEEIESFVR YMPPKDGYIP SAHTYEENIA RLYSHWEHYL NNGGGQG // ID Q5F790_NEIG1 Unreviewed; 94 AA. AC Q5F790; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89947.1}; GN ORFNames=NGO_1293 {ECO:0000313|EMBL:AAW89947.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89947.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89947.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89947; AAW89947; NGO_1293. DR BioCyc; NGON242231:GI2G-1205-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10953 MW; 1B2D8202F34FDE5F CRC64; MPSLQRRSRG EKSSCIKQLN GGNYPPFLIC CQLFFENLPD RFKFCKKLAR WLSGNKFPQK PVNPIIQKII CFHRVSFSVE TLPFRAVESD FIVD // ID Q5F8E3_NEIG1 Unreviewed; 215 AA. AC Q5F8E3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAW89544.1}; GN ORFNames=NGO_0835 {ECO:0000313|EMBL:AAW89544.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89544.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89544.1; -; Genomic_DNA. DR RefSeq; WP_003688570.1; NC_002946.2. DR RefSeq; YP_207956.1; NC_002946.2. DR EnsemblBacteria; AAW89544; AAW89544; NGO_0835. DR GeneID; 3282212; -. DR KEGG; ngo:NGO0835; -. DR PATRIC; 20334830; VBINeiGon24812_0985. DR HOGENOM; HOG000265543; -. DR OMA; ILYGPRS; -. DR OrthoDB; EOG6X3W4X; -. DR BioCyc; NGON242231:GI2G-786-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008517; DUF799. DR Pfam; PF05643; DUF799; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000313|EMBL:AAW89544.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 215 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256067. SQ SEQUENCE 215 AA; 22947 MW; 46B2203B4CC1E253 CRC64; MKPLILGLAA VLALSACQVR KAPDLDYTSF KESKPASILV VPPLNESPDV NGTWGMLAST AAPISEAGYY VFPAAVVEET FKENGLTNAA DIHAVRPEKL HQIFGNDAVL YITVTEYGTS YQILDSVTTV SAKARLVDSR NGKELWSGSA SIREGSNNSN SGLLGALVGA VVNQIANSLT DRGYQVSKTA AYNLLSPYSR NGILKGPRFV EEQPK // ID Q5F8V1_NEIG1 Unreviewed; 336 AA. AC Q5F8V1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 82. DE SubName: Full=CDP-6-deoxy-delta-3,4-glucoseen reductase {ECO:0000313|EMBL:AAW89386.1}; GN ORFNames=NGO_0659 {ECO:0000313|EMBL:AAW89386.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89386.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89386.1; -; Genomic_DNA. DR RefSeq; WP_003706173.1; NC_002946.2. DR RefSeq; YP_207798.1; NC_002946.2. DR ProteinModelPortal; Q5F8V1; -. DR EnsemblBacteria; AAW89386; AAW89386; NGO_0659. DR GeneID; 3282454; -. DR KEGG; ngo:NGO0659; -. DR PATRIC; 20334414; VBINeiGon24812_0779. DR HOGENOM; HOG000263662; -. DR KO; K00523; -. DR OMA; RTGFVHE; -. DR OrthoDB; EOG6Q5NS6; -. DR BioCyc; NGON242231:GI2G-626-MONOMER; -. DR Proteomes; UP000000535; 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; 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; 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:UP000000535}; 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:UP000000535}. 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; 36563 MW; 2518D2487192B5DD CRC64; MNHTVTLPDQ TTFAAGDGET VLSAAARQNL NLPHSCKNGV CGQCKAELAS GDIQMGGHSE QALSEAEKAQ GKILMCRTTA QSDININIPG CKADALPVRT LPARIESMVF KHDVAFLKLA LPKAPPFAFY AGQYIDLLLP GNVSRSYSIA NSPDQEGILE LHIRRRENGV CSEMIFGSEP KVKEKGIVRV KGPLGSFTLQ EDSGKPVILP ATDTGYAPIR SILLDLIRQN SSRAAHFYWG ARHQDDLYAL EEAQGLACRL KNTCFTPVLS RPGEGWQGRK GHVQDIAAQD HPDLSEYEVF ACGSPAMTEQ AKNLFVQQHK LPENLFFSDA FTPSAS // ID Q5F580_NEIG1 Unreviewed; 388 AA. AC Q5F580; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 73. DE SubName: Full=Ferrous iron transporter {ECO:0000313|EMBL:AAW90657.1}; GN ORFNames=NGO_2050 {ECO:0000313|EMBL:AAW90657.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90657.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90657.1; -; Genomic_DNA. DR RefSeq; WP_003705102.1; NC_002946.2. DR RefSeq; YP_209069.1; NC_002946.2. DR PRIDE; Q5F580; -. DR EnsemblBacteria; AAW90657; AAW90657; NGO_2050. DR GeneID; 3282857; -. DR KEGG; ngo:NGO2050; -. DR PATRIC; 20337899; VBINeiGon24812_2472. DR HOGENOM; HOG000236929; -. DR KO; K07224; -. DR OMA; PQLQKEN; -. DR OrthoDB; EOG696C0D; -. DR BioCyc; NGON242231:GI2G-1951-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028096; EfeO_Cupredoxin. DR Pfam; PF13473; Cupredoxin_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 388 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256567. FT DOMAIN 33 128 Cupredoxin_1. {ECO:0000259|Pfam:PF13473}. SQ SEQUENCE 388 AA; 42023 MW; 12EFA2946CED6A6E CRC64; MRKFNLTALS VMLALGLTAC QPPEAEKAAP AASGETQSAN EGGSVGIAVN DNACEPMNLT VPSGQVVFNI KNNSGRKLEW EILKGVMVVD ERENIAPGLS DKMTVTLLPG EYEMTCGLLT NPRGKLVVAD SGFKDTANEA DLEKLPQPLA DYKAYVQGEV KELAAKTKTF TEAVKAGDIE KAKSLFAATR VHYERIEPIA ELFSELDPVI DACEDDFKDG AKDAGFTGFH RIEHALWVEK DVSGVKETAA KLMTDVEALQ KEIDALAFPP GKVVGGASEL IEEAAGSKIS GEEDRYSHTD LSDFQANADG SKKIVDLFRP LIEAKNKALL EKTDTNFKQV NEILAKYRTK DGFETYDKLS EADRKALQAP INALAEDLAQ LRGILGLK // ID Q5F6Z2_NEIG1 Unreviewed; 164 AA. AC Q5F6Z2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Copper-binding protein {ECO:0000313|EMBL:AAW90045.1}; GN ORFNames=NGO_1397 {ECO:0000313|EMBL:AAW90045.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90045.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90045.1; -; Genomic_DNA. DR RefSeq; WP_003689238.1; NC_002946.2. DR RefSeq; YP_208457.1; NC_002946.2. DR ProteinModelPortal; Q5F6Z2; -. DR EnsemblBacteria; AAW90045; AAW90045; NGO_1397. DR GeneID; 3281172; -. DR KEGG; ngo:NGO1397; -. DR PATRIC; 20336189; VBINeiGon24812_1643. DR HOGENOM; HOG000146264; -. DR KO; K19342; -. DR OMA; TLMPDQP; -. DR OrthoDB; EOG6GJBT9; -. DR BioCyc; NGON242231:GI2G-1310-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008719; N2O_reductase_NosL. DR Pfam; PF05573; NosL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256048. SQ SEQUENCE 164 AA; 18166 MW; 1708F10594F767A2 CRC64; MKKTLLAIVA VFALSACRQA EEAPPPLPRQ ISDRSVGHYC SMNLTEHNGP KAQIFLNGKP DQPVWFSTVK QMFGYTKLPE EPKGIRVIYV TDMGNVTDWT NPNADTEWID AKKAFYVIDS GFIGGMGAED ALPFGNKEQA EKFAKDKGGK VVGFDDMPDA YIFK // ID Q5F6Q8_NEIG1 Unreviewed; 233 AA. AC Q5F6Q8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 51. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90129.2}; GN ORFNames=NGO_1491 {ECO:0000313|EMBL:AAW90129.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90129.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90129.2; -; Genomic_DNA. DR DNASU; 3281559; -. DR EnsemblBacteria; AAW90129; AAW90129; NGO_1491. DR PATRIC; 20336434; VBINeiGon24812_1764. DR HOGENOM; HOG000264416; -. DR OMA; GTMDQSL; -. DR OrthoDB; EOG61308T; -. DR BioCyc; NGON242231:GI2G-1395-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 25113 MW; 8DEA53EDA1DB9667 CRC64; MTEPAAEGGK AAKALKKYLI TGILVWLPIA VTVWVVSYIV SASDQLVNLL PKQWRPQYVL GFNIPGLGVI VAIAVLFVTG LFAANVLGRQ ILAAWDSLLG RIPVVKSIYS SVKKVSESLL SDSSRSFKTP VLVPFPQSGI WTIAFVSGQV SNAVKAALPQ DGDYLSVYVP TTPNPTGGYY IMVKKSDVRE LDMSVDEALK YVISLGMVIP DDLPVKTLAG PMPPEKAELP EQQ // ID Q5F9N4_NEIG1 Unreviewed; 254 AA. AC Q5F9N4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Uroporphyrinogen-III synthase {ECO:0000313|EMBL:AAW89103.1}; GN ORFNames=NGO_0359 {ECO:0000313|EMBL:AAW89103.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89103.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89103.1; -; Genomic_DNA. DR RefSeq; WP_003687770.1; NC_002946.2. DR RefSeq; YP_207515.1; NC_002946.2. DR ProteinModelPortal; Q5F9N4; -. DR EnsemblBacteria; AAW89103; AAW89103; NGO_0359. DR GeneID; 3283032; -. DR KEGG; ngo:NGO0359; -. DR PATRIC; 20333713; VBINeiGon24812_0434. DR HOGENOM; HOG000247992; -. DR KO; K01719; -. DR OMA; AKPFSEH; -. DR OrthoDB; EOG6RZB2F; -. DR BioCyc; NGON242231:GI2G-338-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 22 233 HEM4. {ECO:0000259|Pfam:PF02602}. SQ SEQUENCE 254 AA; 28001 MW; BE46FFAA7A54DFCC CRC64; METAKPVMLI VRPSGRAKDD VEVCRRAGWQ AEVLSPIEIE TDEASLKRLP EMYARADAVF WVSPAAVETA VPYLNLSDGI KAHIAVGQGS RRALARYAGA GVFAPEDGND SEAVLRLPVW NSLPEGARVL SVRGHGGRDF LMNALQEKGF RTEVAEVYFR RHKPLNFQNF QTENIAAAYI TSTELVQSLF AQLPPQFSRF FKSLLYFTHH PRIAEALKRE GVCSVETVPT LEAALSYSSI SVSDGMVFPG TSNQ // ID Q5F7Q9_NEIG1 Unreviewed; 376 AA. AC Q5F7Q9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89778.1}; GN ORFNames=NGO_1111 {ECO:0000313|EMBL:AAW89778.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89778.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89778.1; -; Genomic_DNA. DR RefSeq; WP_010951191.1; NC_002946.2. DR RefSeq; YP_208190.1; NC_002946.2. DR EnsemblBacteria; AAW89778; AAW89778; NGO_1111. DR GeneID; 3281852; -. DR KEGG; ngo:NGO1111; -. DR PATRIC; 20335474; VBINeiGon24812_1303. DR HOGENOM; HOG000071250; -. DR OrthoDB; EOG6RNQ9M; -. DR BioCyc; NGON242231:GI2G-1023-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 376 AA; 41211 MW; 1344501AF8FAD353 CRC64; MMKPSESLRA AGRPIAYYPK LAKPLGGVNA AILFGHFFYW NDKTQYESGI YRTAEEIEIE TGLSVQEQRT ARAKLRERGV LIETEKRIEH RIYYKLNLDA FDDLMLQHSG GGEPTAPKCN INSPELQNQH SGGGEPTAPK CNINSPELQN QHSGSGESTA PKCNINSPEL QNQHSGSEES TAVIRTEDLT EDLAVYTPLP PNAENGKGGL NADAFVSADA ETCGRETGEP TSPKAESDSN GNGGLSGKPK NANVPRRRKT HGVPLQEIAD LYNEVLGGRL PSVQVLNDTR KRAIANRWCE MLGTAAPNGK VRFGDKETGL AWFAGFFRKV AMNPFWMGEN QTGFAVGFDW IFKAGNFVKI LEWHPPKTNQ AARGRA // ID Q5F8F2_NEIG1 Unreviewed; 113 AA. AC Q5F8F2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE SubName: Full=2Fe-2S ferredoxin {ECO:0000313|EMBL:AAW89535.1}; GN ORFNames=NGO_0825 {ECO:0000313|EMBL:AAW89535.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89535.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89535.1; -; Genomic_DNA. DR RefSeq; WP_003688580.1; NC_002946.2. DR RefSeq; YP_207947.1; NC_002946.2. DR ProteinModelPortal; Q5F8F2; -. DR SMR; Q5F8F2; 2-111. DR EnsemblBacteria; AAW89535; AAW89535; NGO_0825. DR GeneID; 3282203; -. DR KEGG; ngo:NGO0825; -. DR PATRIC; 20334808; VBINeiGon24812_0974. DR HOGENOM; HOG000244519; -. DR KO; K04755; -. DR OMA; SACGGVC; -. DR OrthoDB; EOG6KMB9X; -. DR BioCyc; NGON242231:GI2G-777-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. FT DOMAIN 2 105 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. SQ SEQUENCE 113 AA; 12400 MW; 28228A1FDB3C0E6A CRC64; MPKITVLPHA TLCPEGAVID NAPEGKTVLD VLLDHDIEVD HACEKSCACT TCHVIIRKGF DSLEEPAELE EDLLDQAWGL EADSRLSCQA VVAGEDLIVE IPKYTINHAR EEH // ID Q5F9T3_NEIG1 Unreviewed; 161 AA. AC Q5F9T3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Exclusion suppressor FxsA {ECO:0000313|EMBL:AAW89054.1}; GN ORFNames=NGO_0307 {ECO:0000313|EMBL:AAW89054.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89054.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89054.1; -; Genomic_DNA. DR RefSeq; WP_003687689.1; NC_002946.2. DR RefSeq; YP_207466.1; NC_002946.2. DR EnsemblBacteria; AAW89054; AAW89054; NGO_0307. DR GeneID; 3281690; -. DR KEGG; ngo:NGO0307; -. DR PATRIC; 20333595; VBINeiGon24812_0377. DR HOGENOM; HOG000218854; -. DR KO; K07113; -. DR OMA; TIDGEYH; -. DR OrthoDB; EOG6742Z1; -. DR BioCyc; NGON242231:GI2G-287-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 17541 MW; 1F80221C955A7ED8 CRC64; MRFFGIGFLV LLFLEIMSIV WVADWLGGGW TLFLMAATFA AGVLMLRHTG LSGLLLAGAA VKSSGKVSVY QMLWPIRYTV AAVCLMSPGF VSSVLAVLLL LPFKGGAVLQ AGGAENFFNM NQSGRKEGFF HDDDIIEGEY TVEEPYGGNR SRNAIEHKKD E // ID Q5FA04_NEIG1 Unreviewed; 485 AA. AC Q5FA04; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247}; GN ORFNames=NGO_0230 {ECO:0000313|EMBL:AAW88983.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88983.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Low-affinity potassium transport system. Interacts with CC Trk system potassium uptake protein TrkA. CC {ECO:0000256|PIRNR:PIRNR006247}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|PIRNR:PIRNR006247}; Multi-pass membrane protein CC {ECO:0000256|PIRNR:PIRNR006247}. CC -!- SIMILARITY: Belongs to the TrkH potassium transport family. CC {ECO:0000256|PIRNR:PIRNR006247}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88983.1; -; Genomic_DNA. DR RefSeq; WP_003706675.1; NC_002946.2. DR RefSeq; YP_207395.1; NC_002946.2. DR EnsemblBacteria; AAW88983; AAW88983; NGO_0230. DR GeneID; 3281492; -. DR KEGG; ngo:NGO0230; -. DR PATRIC; 20333405; VBINeiGon24812_0284. DR HOGENOM; HOG000225541; -. DR KO; K03498; -. DR OMA; ILFWRSI; -. DR OrthoDB; EOG63589N; -. DR BioCyc; NGON242231:GI2G-214-MONOMER; -. DR Proteomes; UP000000535; 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:0022820; F:potassium ion symporter activity; IEA:InterPro. DR InterPro; IPR003445; Cat_transpt. DR InterPro; IPR004772; TrkH. DR Pfam; PF02386; TrkH; 1. DR PIRSF; PIRSF006247; TrkH; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|PIRNR:PIRNR006247}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR006247}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ion transport {ECO:0000256|PIRNR:PIRNR006247}; KW Membrane {ECO:0000256|PIRNR:PIRNR006247, ECO:0000256|SAM:Phobius}; KW Potassium {ECO:0000256|PIRNR:PIRNR006247}; KW Potassium transport {ECO:0000256|PIRNR:PIRNR006247}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|PIRNR:PIRNR006247}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 255 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 276 294 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 326 345 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 415 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 422 441 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 461 483 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 485 AA; 53016 MW; 27AFF6E0384F8529 CRC64; MHKILPIAHV LSRLGMLFSF ILLIPAALSY AFSDGAYTAF ATTATVTLSG SCIVRLATLR FRRELRPRDG FTLVLMLWLA FAAMAAMPMY LYFPNMGFTD AFFESMSGLT TTGATVIPHV DGLAPSVNFW RHMLNWLGGM GIIVLAVAIL PMLGVGGTQL FKAEIPGIDK ESKMSPRISQ VAKKLWFGYT LITILAAACL HFAGMGWFDA VCHALATLSL GGFSTHDASI GYYNSPLIEA VIIVFTIFGG INFASHFAAL NSRSLKTYWK DEECRTMLLL LSGSILASAL YLWHTGHYAG FGESLRYTAF NFVSIGLANG LSNTDFAQWP LLISLWMFFL ANILASSGST GGGIKTIRAL VLFKFSLREM MVLLHPKAVR TVKISGKAIP DRLALTVMSF IFIYFMTVVL FSFLLMASGM EFTTAFTAVI ACITNAGPGL GEVGPAGNYA GLDVMQKWIC VTAMLLGRLE IFTVFILFTP AYWKK // ID Q5F8P5_NEIG1 Unreviewed; 46 AA. AC Q5F8P5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89442.1}; GN ORFNames=NGO_0722 {ECO:0000313|EMBL:AAW89442.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89442.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89442.1; -; Genomic_DNA. DR RefSeq; WP_003688719.1; NC_002946.2. DR RefSeq; YP_207854.1; NC_002946.2. DR EnsemblBacteria; AAW89442; AAW89442; NGO_0722. DR GeneID; 3282095; -. DR KEGG; ngo:NGO0722; -. DR PATRIC; 20334574; VBINeiGon24812_0859. DR HOGENOM; HOG000027837; -. DR OrthoDB; EOG6P33CW; -. DR BioCyc; NGON242231:GI2G-682-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 46 AA; 5208 MW; B26921F74843ABF0 CRC64; MPQYRNWQNG LGAKCADGDE YGVAQSDCRT REINAKTKEI QGYLID // ID Q5F9W7_NEIG1 Unreviewed; 242 AA. AC Q5F9W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 86. DE SubName: Full=Amino acid ABC transporter ATPase {ECO:0000313|EMBL:AAW89020.1}; GN ORFNames=NGO_0269 {ECO:0000313|EMBL:AAW89020.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89020.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89020.1; -; Genomic_DNA. DR RefSeq; WP_010357138.1; NC_002946.2. DR RefSeq; YP_207432.1; NC_002946.2. DR ProteinModelPortal; Q5F9W7; -. DR SMR; Q5F9W7; 1-239. DR EnsemblBacteria; AAW89020; AAW89020; NGO_0269. DR GeneID; 3281579; -. DR KEGG; ngo:NGO0269; -. DR PATRIC; 20333507; VBINeiGon24812_0334. DR KO; K02028; -. DR OMA; VFFEGGK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-252-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 242 AA; 27027 MW; D82443400E8F8725 CRC64; MIKFKNVHKH FKDLHVINGV NLEIKKGEVV VVCGPSGSGK STLIRTVNQL ESIESGEIWV DGVNVADPKT DLNKIREEVG FVFQSFNLYP HLTVLDNITL APMKVKGQNA EQAEKKAMEL LERVGLAHKK DAFPSQLSGG QQQRVAIARG LAMEPRVMLF DEPTSALDPE MVGEVLKVMK DLAESGMTMM CVTHEMGFAR EVADRVIFVD KGQILEDETP EAFFTNPKHE RAKQFLQQVM TH // ID Q5F708_NEIG1 Unreviewed; 219 AA. AC Q5F708; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 69. DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:AAW90029.2}; GN ORFNames=NGO_1381 {ECO:0000313|EMBL:AAW90029.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90029.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90029.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F708; -. DR EnsemblBacteria; AAW90029; AAW90029; NGO_1381. DR PATRIC; 20336151; VBINeiGon24812_1624. DR HOGENOM; HOG000064700; -. DR OMA; LRNLTCV; -. DR OrthoDB; EOG64BQ52; -. DR BioCyc; NGON242231:GI2G-1294-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 83 GST N-terminal. FT {ECO:0000259|PROSITE:PS50404}. FT COILED 140 167 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 219 AA; 24496 MW; FCA29EBD2FBDC849 CRC64; MTRNILMKLY IYDHCPFCVR ARMAAGLFGA DVEEVVLAND DEATPIGMIG AKQVPVLQKE DGSFMGESLD IVCHFDREGR LKDEVRPEIQ AWLDKVGGYN NKLVQPRLIK IGLPEFVTPE AVKYFTDKKE KSIGSFSANL NKTAQYLERI NADLQELENL MDGTSDGING GIGMEDILVF PVLRNLTVVR GIAFPRKTMD YLIGMSEKSG VPLYFDRAL // ID Q5F6J1_NEIG1 Unreviewed; 61 AA. AC Q5F6J1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90196.1}; GN ORFNames=NGO_1563 {ECO:0000313|EMBL:AAW90196.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90196.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90196.1; -; Genomic_DNA. DR RefSeq; WP_010951296.1; NC_002946.2. DR RefSeq; YP_208608.1; NC_002946.2. DR EnsemblBacteria; AAW90196; AAW90196; NGO_1563. DR GeneID; 3281444; -. DR KEGG; ngo:NGO1563; -. DR BioCyc; NGON242231:GI2G-1464-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 61 AA; 6985 MW; E51136620632DA11 CRC64; MILIIFINFI INQLFISHCT GLYVPFPTIF ANKRKDRLSD GIKLPPLPCL TLLPNGIIRI F // ID Q5F7G9_NEIG1 Unreviewed; 377 AA. AC Q5F7G9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 77. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_1209 {ECO:0000313|EMBL:AAW89868.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89868.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89868.1; -; Genomic_DNA. DR RefSeq; WP_003689650.1; NC_002946.2. DR RefSeq; YP_208280.1; NC_002946.2. DR ProteinModelPortal; Q5F7G9; -. DR REBASE; 3461; M.NgoAIII. DR DNASU; 3281877; -. DR EnsemblBacteria; AAW89868; AAW89868; NGO_1209. DR GeneID; 3281877; -. DR KEGG; ngo:NGO1209; -. DR PATRIC; 20335719; VBINeiGon24812_1418. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; RSYPGHT; -. DR OrthoDB; EOG62NX2W; -. DR BioCyc; NGON242231:GI2G-1120-MONOMER; -. DR Proteomes; UP000000535; 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; 3. 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417}. FT DOMAIN 1 365 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 377 AA; 42983 MW; 6939CDDBEE4CD871 CRC64; MKSLEIFSGA GGLAKGLELA GFQHASFIEL NKDACNSLRS NFNPKLVYQG DVADFDLSSQ EGIEVIAGGP PCQPFSLGGK HLAHEDRRDM FPHAVRYVEY YRPKAFIFEN VKGLLRKSFA DYFEYILLRL TYPNLGILQN EDWKGHLTRL KEIEFNLYKG IKYKVSYQLL NAADYGVPQK RERVVIVGIR ADLDIDWKFP KRTHSEDRLN WEKYVTGEYW EKHNEPKRFN KDIAEKLQKK YGIFEPEKKP WQTVRDTLSD IPHPLGNHKI TGHEYRDGAR IYPGHTGSGI DEPSKTIKAG GHGVPGGENM IRYDDGTVRY FTSYEAKLLQ TFPEEFVISG AWGEAMRQIG NAVPVKLSEI LGKHLMGVLS EKSSLHN // ID Q5F5K2_NEIG1 Unreviewed; 216 AA. AC Q5F5K2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 88. DE SubName: Full=GMP synthase {ECO:0000313|EMBL:AAW90535.1}; GN ORFNames=NGO_1922 {ECO:0000313|EMBL:AAW90535.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90535.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90535.1; -; Genomic_DNA. DR RefSeq; WP_010355614.1; NC_002946.2. DR RefSeq; YP_208947.1; NC_002946.2. DR ProteinModelPortal; Q5F5K2; -. DR PRIDE; Q5F5K2; -. DR EnsemblBacteria; AAW90535; AAW90535; NGO_1922. DR GeneID; 3282858; -. DR KEGG; ngo:NGO1922; -. DR PATRIC; 20337580; VBINeiGon24812_2317. DR KO; K09812; -. DR OMA; AQDICKE; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1825-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 216 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 216 AA; 23843 MW; 20CEE5D714268484 CRC64; MIRFEQVSKT YPGGFEALKN VSFQINKGEM IFIAGHSGSG KSTVLKLISG ITKPSMGKVL FNGQDLGTLS DNQIGFMRQH IGIVFQDHKI LNDRNVLQNV ILPLRIIGYP PRKAEERARI AIEKVGLKGR ELDDPVTLSG GEQQRLCIAR AVVHQPGLLI ADEPSANLDR AYALDIMELF KTFHEAGTTV IVAAHDETLM ADYGHRILRL SKGRLA // ID Q5F6A3_NEIG1 Unreviewed; 92 AA. AC Q5F6A3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=BolA family transcriptional regulator {ECO:0000313|EMBL:AAW90284.1}; GN ORFNames=NGO_1657 {ECO:0000313|EMBL:AAW90284.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90284.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90284.1; -; Genomic_DNA. DR RefSeq; WP_003689791.1; NC_002946.2. DR RefSeq; YP_208696.1; NC_002946.2. DR ProteinModelPortal; Q5F6A3; -. DR EnsemblBacteria; AAW90284; AAW90284; NGO_1657. DR GeneID; 3281281; -. DR KEGG; ngo:NGO1657; -. DR PATRIC; 20336860; VBINeiGon24812_1975. DR HOGENOM; HOG000255169; -. DR KO; K05527; -. DR OMA; RHAGHKG; -. DR OrthoDB; EOG6VMTQ7; -. DR BioCyc; NGON242231:GI2G-1553-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 92 AA; 10017 MW; E3E795F0396D0600 CRC64; MPAVDLIRER LQTLDPLVLE IGDESHLHKG HAGNTGGGHY AVLVVSGRFE GLSRLNRQKT VKSLLKDLFS GGMIHALGIR AATPDEYFHT AD // ID Q5F7C1_NEIG1 Unreviewed; 47 AA. AC Q5F7C1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89916.1}; GN ORFNames=NGO_1257 {ECO:0000313|EMBL:AAW89916.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89916.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89916.1; -; Genomic_DNA. DR RefSeq; WP_010951226.1; NC_002946.2. DR RefSeq; YP_208328.1; NC_002946.2. DR EnsemblBacteria; AAW89916; AAW89916; NGO_1257. DR GeneID; 3281839; -. DR KEGG; ngo:NGO1257; -. DR OrthoDB; EOG64BQH5; -. DR BioCyc; NGON242231:GI2G-1174-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 47 AA; 5375 MW; EFFDD0389215E137 CRC64; MPSEGLSISD GIFDGKRREG FSLPINNRKR RNSNRRVGFS PLIDKQK // ID Q5F995_NEIG1 Unreviewed; 109 AA. AC Q5F995; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89242.1}; GN ORFNames=NGO_0504 {ECO:0000313|EMBL:AAW89242.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89242.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89242.1; -; Genomic_DNA. DR RefSeq; WP_003689072.1; NC_002946.2. DR RefSeq; YP_207654.1; NC_002946.2. DR EnsemblBacteria; AAW89242; AAW89242; NGO_0504. DR GeneID; 3282945; -. DR KEGG; ngo:NGO0504; -. DR PATRIC; 20334050; VBINeiGon24812_0597. DR HOGENOM; HOG000071314; -. DR OMA; LIDIGNM; -. DR OrthoDB; EOG65QWN9; -. DR BioCyc; NGON242231:GI2G-482-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 109 AA; 11556 MW; 5F7115DF61EC16A0 CRC64; MTVRIKGVTV ELNGADYVIP PIALGALEQL QERIGSFDGN AADAGQISTV IDCAHAALKR NYPDLTREEA ADLIDIGNMN EVFAAVMDVS GLKRKEQEAA QAGEARAAD // ID Q5F6G5_NEIG1 Unreviewed; 90 AA. AC Q5F6G5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90222.1}; GN ORFNames=NGO_1594 {ECO:0000313|EMBL:AAW90222.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90222.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90222.1; -; Genomic_DNA. DR RefSeq; WP_002221302.1; NC_002946.2. DR RefSeq; YP_208634.1; NC_002946.2. DR EnsemblBacteria; AAW90222; AAW90222; NGO_1594. DR GeneID; 3281653; -. DR KEGG; ngo:NGO1594; -. DR PATRIC; 20336714; VBINeiGon24812_1903. DR HOGENOM; HOG000220704; -. DR OMA; DTYHETL; -. DR OrthoDB; EOG6B62D4; -. DR BioCyc; NGON242231:GI2G-1490-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 90 AA; 10539 MW; DEB3520A0E821313 CRC64; MMSVKELFKV ILDENKDFPI RTIHRTPMGI LPKPVALSIV QYENDPGFYL FYLDETGQEQ TDTYHDTLDS AFEQAEFEFG ISKEEWMQSP // ID Q5F917_NEIG1 Unreviewed; 403 AA. AC Q5F917; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Uracil transporter {ECO:0000313|EMBL:AAW89320.1}; GN ORFNames=NGO_0589 {ECO:0000313|EMBL:AAW89320.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89320.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89320.1; -; Genomic_DNA. DR RefSeq; WP_003688961.1; NC_002946.2. DR RefSeq; YP_207732.1; NC_002946.2. DR EnsemblBacteria; AAW89320; AAW89320; NGO_0589. DR GeneID; 3282460; -. DR KEGG; ngo:NGO0589; -. DR PATRIC; 20334250; VBINeiGon24812_0697. DR HOGENOM; HOG000038200; -. DR KO; K02824; -. DR OMA; DTTSIAH; -. DR OrthoDB; EOG6Z3KKZ; -. DR BioCyc; NGON242231:GI2G-560-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 41856 MW; 6166C6D818F1E7BD CRC64; MNQLKLAVSG AQILFVAFGA MVLVPLLTGL NPALALLGAG LGTLLFQITT KRKVPIFLGS SFAFIAPIIY SVGEWGLPST MFGLFAAGFM YFVFAALIRW RGLAAVHKLL PPVVTGPVIM VIGLSVAVAA SSMAMGQADG KQVIDYTDSL ILSGFTFAVT AIVSVFGSRM MKLIPILIGV ASGYVLALLM GLVDTTSIAH APWFAVPHFE TPQVNWQAAL FMLPVAVAPA IEHIGGIMAI GNVTGKDYTK DPGLDKTLAG DGLGVCVAGL IGGPPVTTYG EVTGAVMITK NSNPVIMTWA AVFAVCMAFF GKFNAFLASI PMPVMGGIML LLFGTIASLG IKTLIDAKVD LMLPKNLVIV SSVLTTGIGG MTLKLGSFSF VGVGLCAVLA IVLNSLLPDP KES // ID Q5F5K9_NEIG1 Unreviewed; 423 AA. AC Q5F5K9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000313|EMBL:AAW90528.1}; GN ORFNames=NGO_1915 {ECO:0000313|EMBL:AAW90528.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90528.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90528.1; -; Genomic_DNA. DR RefSeq; WP_010355587.1; NC_002946.2. DR RefSeq; YP_208940.1; NC_002946.2. DR ProteinModelPortal; Q5F5K9; -. DR CAZy; GT30; Glycosyltransferase Family 30. DR DNASU; 3282860; -. DR EnsemblBacteria; AAW90528; AAW90528; NGO_1915. DR GeneID; 3282860; -. DR KEGG; ngo:NGO1915; -. DR PATRIC; 20337564; VBINeiGon24812_2310. DR HOGENOM; HOG000257156; -. DR KO; K02527; -. DR OMA; KHGGHNP; -. DR OrthoDB; EOG6H7FNN; -. DR BioCyc; NGON242231:GI2G-1817-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR007507; Glycos_transf_N. DR Pfam; PF04413; Glycos_transf_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90528.1}. FT DOMAIN 36 207 Glycos_transf_N. FT {ECO:0000259|Pfam:PF04413}. SQ SEQUENCE 423 AA; 47083 MW; A75896024F2BCE2D CRC64; MFQWLYDVLW LLAPIWIRRY LDKRSGSAPA YRAHRDERFG KPHPNPVTGA VWIHAVSVGE TRAAQPLIRE LRRRFPDAPL LMTQMTPTGR ETAQVLFPDA QCRYLPYDKK TWVRQFLREH RPMFGILMET EIWPNLMKEC RRAGVPLFLA NARLSEKSLN GYLKVRRLIR PAAASLTGCL AQTEADAARL AKLGAASVQV CGNTKYDLMP SEDMKTLAGQ FEKRIGGRPV AVCGSTRVYR GEDEAEKLLA AWQQYRGDAL LAVVPRHPEH FQTTFETAKR FGFKVQRRSD GLPVEPDTQV WVGDSMGELY AYYLCADVAF VGGSLVGSGC QNIIEPLSCG VTTIFGFSTY NFSEACRHAL ASGAAVQVES ADAWREAVEK TLSGEGGGMQ MQARVDGFIA QHRGAGARIA EAVREAVCGH RGR // ID Q5F747_NEIG1 Unreviewed; 227 AA. AC Q5F747; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 53. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89990.1}; GN ORFNames=NGO_1340 {ECO:0000313|EMBL:AAW89990.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89990.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89990.1; -; Genomic_DNA. DR RefSeq; WP_002216652.1; NC_002946.2. DR RefSeq; YP_208402.1; NC_002946.2. DR EnsemblBacteria; AAW89990; AAW89990; NGO_1340. DR GeneID; 3282064; -. DR KEGG; ngo:NGO1340; -. DR PATRIC; 20336049; VBINeiGon24812_1574. DR HOGENOM; HOG000219073; -. DR OMA; WVYLGDF; -. DR OrthoDB; EOG613091; -. DR BioCyc; NGON242231:GI2G-1254-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 137 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 193 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 206 227 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 227 AA; 25535 MW; 6593BE4B5667FA74 CRC64; MFALLEAFFV EYGYAAVFFV LVICGFGVPI PEDLTLVTGG VISGMGYTNP HIMFAVGMLG VLAGDGVMFA AGRIWGQKIL KFKPIARIMT PKRYAQVQEK FDKYGNWVLF VARFLPGLRT AVFVTAGISR KVSYLRFLIM DGLAALISVP VWIYLGEYGA HNIDWLMAKM HSLQSGIFIA LGVLAAALAW FWWRKRRHYQ LYRAQLSEKR AKRKAEKAAK KAAQKQQ // ID Q5FA77_NEIG1 Unreviewed; 109 AA. AC Q5FA77; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88910.1}; GN ORFNames=NGO_0152 {ECO:0000313|EMBL:AAW88910.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88910.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88910.1; -; Genomic_DNA. DR ProteinModelPortal; Q5FA77; -. DR EnsemblBacteria; AAW88910; AAW88910; NGO_0152. DR PATRIC; 20333227; VBINeiGon24812_0196. DR HOGENOM; HOG000256331; -. DR OMA; MSDNANL; -. DR OrthoDB; EOG67HJXZ; -. DR BioCyc; NGON242231:GI2G-140-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR002197; HTH_Fis. DR Pfam; PF02954; HTH_8; 1. DR PRINTS; PR01590; HTHFIS. DR SUPFAM; SSF46689; SSF46689; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 66 103 HTH_8. {ECO:0000259|Pfam:PF02954}. SQ SEQUENCE 109 AA; 12371 MW; 7766915FACA14824 CRC64; MPSENEWNGF RQKAFRRHSV LKTFQSKGYA MNPATADIAQ CIEQNLNQYF KDLNGTEPCG VYDMVLHQVE KPLLVCVMEQ CGGNQSKASV MLGLNRNTLR KKLIQHGLL // ID Q5F5I0_NEIG1 Unreviewed; 248 AA. AC Q5F5I0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90557.1}; GN ORFNames=NGO_1945 {ECO:0000313|EMBL:AAW90557.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90557.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3DEE} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS). RX PubMed=20944208; DOI=10.1107/S1744309109022672; RA Das D., Grishin N.V., Kumar A., Carlton D., Bakolitsa C., Miller M.D., RA Abdubek P., Astakhova T., Axelrod H.L., Burra P., Chen C., Chiu H.J., RA Chiu M., Clayton T., Deller M.C., Duan L., Ellrott K., Ernst D., RA Farr C.L., Feuerhelm J., Grzechnik A., Grzechnik S.K., Grant J.C., RA Han G.W., Jaroszewski L., Jin K.K., Johnson H.A., Klock H.E., RA Knuth M.W., Kozbial P., Krishna S.S., Marciano D., McMullan D., RA Morse A.T., Nigoghossian E., Nopakun A., Okach L., Oommachen S., RA Paulsen J., Puckett C., Reyes R., Rife C.L., Sefcovic N., Tien H.J., RA Trame C.B., van den Bedem H., Weekes D., Wooten T., Xu Q., RA Hodgson K.O., Wooley J., Elsliger M.A., Deacon A.M., Godzik A., RA Lesley S.A., Wilson I.A.; RT "The structure of the first representative of Pfam family PF09836 RT reveals a two-domain organization and suggests involvement in RT transcriptional regulation."; RL Acta Crystallogr. F 66:1174-1181(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; AE004969; AAW90557.1; -; Genomic_DNA. DR RefSeq; WP_003705168.1; NC_002946.2. DR RefSeq; YP_208969.1; NC_002946.2. DR PDB; 3DEE; X-ray; 2.10 A; A=1-248. DR PDBsum; 3DEE; -. DR DNASU; 3282675; -. DR EnsemblBacteria; AAW90557; AAW90557; NGO_1945. DR GeneID; 3282675; -. DR KEGG; ngo:NGO1945; -. DR PATRIC; 20337635; VBINeiGon24812_2344. DR HOGENOM; HOG000218684; -. DR KO; K09929; -. DR OMA; PLNGYAE; -. DR OrthoDB; EOG6716MP; -. DR BioCyc; NGON242231:GI2G-1847-MONOMER; -. DR EvolutionaryTrace; Q5F5I0; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018640; DUF2063. DR Pfam; PF09836; DUF2063; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3DEE}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 90 DUF2063. {ECO:0000259|Pfam:PF09836}. SQ SEQUENCE 248 AA; 28579 MW; C9F78BB489F99ADB CRC64; MQPETSAQYQ HRFSQAIRGG EAADGLPQDR LNVYIRLIRN NIHSFIDRCY TETRQYFDSK EWSRLKEGFV RDARAQTPYF QEIPGEFLQY CQSPPLSDGI LALMDFEYTQ LLAEVAQIPD IPDIHYSNDS KYTPSPAAFI RQYRYDVTHD LQEAETALLI WRNAEDDVMY QTLDGFDMML LEIMGSSALS FDTLAQTLVE FMPKADNWKN ILLGKWSGWI EQRIIIPSLS AISENMEGNS PSQNHLSA // ID Q5F808_NEIG1 Unreviewed; 140 AA. AC Q5F808; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89679.1}; GN ORFNames=NGO_0995 {ECO:0000313|EMBL:AAW89679.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89679.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89679.1; -; Genomic_DNA. DR RefSeq; WP_003688269.1; NC_002946.2. DR RefSeq; YP_208091.1; NC_002946.2. DR EnsemblBacteria; AAW89679; AAW89679; NGO_0995. DR GeneID; 3281728; -. DR KEGG; ngo:NGO0995; -. DR PATRIC; 20335194; VBINeiGon24812_1165. DR HOGENOM; HOG000027858; -. DR OMA; ACRAVRI; -. DR OrthoDB; EOG6WMJ0T; -. DR BioCyc; NGON242231:GI2G-922-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007922; DUF721/UPF0232. DR Pfam; PF05258; DUF721; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 15287 MW; 34EECF48B7C59F54 CRC64; MNLEQLGRRD ALLSGLLKQA GQWRRLDAAV KKLLPANLHP HFQTACIEDG RLVLLAANNM AASRLKMIAP SVLPQLAGLD ASIRSVSVRL VPKPEKPPKT NTLHLSKAAL ESFDSAAAKL EERHPELAEA LEELVRKYGA // ID Q5F8L7_NEIG1 Unreviewed; 205 AA. AC Q5F8L7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 20-JAN-2016, entry version 61. DE SubName: Full=Riboflavin synthase subunit alpha {ECO:0000313|EMBL:AAW89470.2}; GN ORFNames=NGO_0755 {ECO:0000313|EMBL:AAW89470.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89470.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89470.2; -; Genomic_DNA. DR RefSeq; WP_010358100.1; NC_002946.2. DR RefSeq; YP_207882.2; NC_002946.2. DR ProteinModelPortal; Q5F8L7; -. DR EnsemblBacteria; AAW89470; AAW89470; NGO_0755. DR GeneID; 3282502; -. DR KEGG; ngo:NGO0755; -. DR PATRIC; 20334658; VBINeiGon24812_0901. DR HOGENOM; HOG000151758; -. DR KO; K00793; -. DR OMA; HILSGHV; -. DR OrthoDB; EOG6VMTQH; -. DR BioCyc; NGON242231:GI2G-710-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 98 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT DOMAIN 99 195 Lumazine-binding. FT {ECO:0000259|PROSITE:PS51177}. FT REGION 4 6 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 49 51 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. FT REGION 63 68 Substrate binding. FT {ECO:0000256|PIRSR:PIRSR000498-1}. SQ SEQUENCE 205 AA; 22554 MW; C1540040EF9F5254 CRC64; MFTGIVQGLG KLTAIHRPSE AFQTYVVELP QEAAENLQHG ASVANNGCCL TITEIEGNRV SFDLMAETLA KTNLGLLKEG DCVNIERAAR FGDEIGGHVM SGHIMATVPI VEIERDGFNR TVWFALPHEL KPYILTKGFV GLDGCSLTIG KVEDSRFNVH LIPETLERTL FGSRKAGDRI NIEIDPNTQA IVDTVERLMA QRYAK // ID Q5F9P2_NEIG1 Unreviewed; 103 AA. AC Q5F9P2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894}; GN ORFNames=NGO_0351 {ECO:0000313|EMBL:AAW89095.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89095.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89095.1; -; Genomic_DNA. DR RefSeq; WP_003687762.1; NC_002946.2. DR RefSeq; YP_207507.1; NC_002946.2. DR ProteinModelPortal; Q5F9P2; -. DR EnsemblBacteria; AAW89095; AAW89095; NGO_0351. DR GeneID; 3281239; -. DR KEGG; ngo:NGO0351; -. DR PATRIC; 20333699; VBINeiGon24812_0427. DR HOGENOM; HOG000095211; -. DR KO; K07390; -. DR OMA; EMHARNE; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NGON242231:GI2G-330-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. 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; 11494 MW; 4C8E954E95E366DF CRC64; MASIHDQIKE VVTTHRVVLF MKGTKQFPQC GFSSRAVQIL NAAGCTDYVA VNVLENPEVR QGIKEYSDWP TIPQLYVNGE FVGGSDILME MYEAGELQEL LKA // ID Q5F6S2_NEIG1 Unreviewed; 119 AA. AC Q5F6S2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90115.1}; GN ORFNames=NGO_1475 {ECO:0000313|EMBL:AAW90115.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90115.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90115.1; -; Genomic_DNA. DR RefSeq; WP_002212575.1; NC_002946.2. DR RefSeq; YP_208527.1; NC_002946.2. DR ProteinModelPortal; Q5F6S2; -. DR EnsemblBacteria; AAW90115; AAW90115; NGO_1475. DR GeneID; 3281636; -. DR KEGG; ngo:NGO1475; -. DR PATRIC; 20336389; VBINeiGon24812_1742. DR HOGENOM; HOG000219083; -. DR OMA; MIRIEMK; -. DR OrthoDB; EOG6S52PG; -. DR BioCyc; NGON242231:GI2G-1381-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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 Q5F8Q5_NEIG1 Unreviewed; 61 AA. AC Q5F8Q5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89432.1}; GN ORFNames=NGO_0712 {ECO:0000313|EMBL:AAW89432.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89432.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89432.1; -; Genomic_DNA. DR RefSeq; WP_003688739.1; NC_002946.2. DR RefSeq; YP_207844.1; NC_002946.2. DR EnsemblBacteria; AAW89432; AAW89432; NGO_0712. DR GeneID; 3282886; -. DR KEGG; ngo:NGO0712; -. DR OrthoDB; EOG674359; -. DR BioCyc; NGON242231:GI2G-672-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 61 AA; 6895 MW; E83F70260B3953A4 CRC64; MGYFGGNGGY LKRKQPKNLW LDVGCLKKRN FAKVSERYFL TTVNLLVSAA HHGILPIGRF L // ID Q5F8P4_NEIG1 Unreviewed; 82 AA. AC Q5F8P4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89443.1}; GN ORFNames=NGO_0723 {ECO:0000313|EMBL:AAW89443.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89443.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89443.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89443; AAW89443; NGO_0723. DR PATRIC; 20334576; VBINeiGon24812_0860. DR OrthoDB; EOG61KBN7; -. DR BioCyc; NGON242231:GI2G-683-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR031807; HicB-like. DR Pfam; PF15919; HicB_lk_antitox; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 9384 MW; 79F2D7C63E2AC901 CRC64; MFHLEGLLQE NLPIPEAQSI EVNRDNPDYA DAVLWTMVEA DDAALTGQVR FNVSWPQHIL NRVDACTAAR HETRAVFWRK PP // ID Q5F7U1_NEIG1 Unreviewed; 273 AA. AC Q5F7U1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 68. DE SubName: Full=Malonic semialdehyde reductase {ECO:0000313|EMBL:AAW89746.1}; GN ORFNames=NGO_1079 {ECO:0000313|EMBL:AAW89746.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89746.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89746.1; -; Genomic_DNA. DR RefSeq; WP_003696927.1; NC_002946.2. DR RefSeq; YP_208158.1; NC_002946.2. DR ProteinModelPortal; Q5F7U1; -. DR EnsemblBacteria; AAW89746; AAW89746; NGO_1079. DR GeneID; 3281795; -. DR KEGG; ngo:NGO1079; -. DR PATRIC; 20335402; VBINeiGon24812_1267. DR OMA; AGHGTYE; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NGON242231:GI2G-991-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 273 AA; 30124 MW; D91FCB3C444C53FC CRC64; MAVLITGASA GFGEAMCRTF VGAGYRVIGA ARRADRLQAL ADELGALFYP LEMDVSCRES VENALNGIPD EFSDIDCLIN NAGLALGLDT ADKADFEDWE TMIQTNVLGL TFLTRKILPQ MVERGGGYVM NLGSIAGNYA YAGSNVYGAT KAFVRQFSLN LRAELADKNI RVTNIEPGLC GNTEFSNVRF KGDNERVAGV YEGVEFIRPE DIAETALWLY RRPAHMNVNT IEIMPVAQTF AGMKVIKTAV PEVREDFEKQ SMSLFSRIRS WFK // ID Q5FA61_NEIG1 Unreviewed; 251 AA. AC Q5FA61; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 80. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW88926.1}; GN ORFNames=NGO_0170 {ECO:0000313|EMBL:AAW88926.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88926.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88926.1; -; Genomic_DNA. DR RefSeq; WP_003692614.1; NC_002946.2. DR RefSeq; YP_207338.1; NC_002946.2. DR ProteinModelPortal; Q5FA61; -. DR PRIDE; Q5FA61; -. DR EnsemblBacteria; AAW88926; AAW88926; NGO_0170. DR GeneID; 3281376; -. DR KEGG; ngo:NGO0170; -. DR PATRIC; 20333261; VBINeiGon24812_0213. DR KO; K02074; -. DR OMA; RGWHREG; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NGON242231:GI2G-156-MONOMER; -. DR Proteomes; UP000000535; 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:AAW88926.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW88926.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 13 241 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 251 AA; 28128 MW; 7A49334616614C0B CRC64; MGCLPLGGIG MSIIVENLTV SYRRRPAVHH VDITFEEHSM WAVFGPNGAG KSTFLKSLMG LQPIDTGSIR LDGLTRQNIA YLPQQSDIDR SQPMTVFDLA AMGLWYEIGF FKGINTAQKQ RVHEALERVG MRQFARRQIA HLSNGQFQRV LFARMLVQNA KFLLLDEPFN AVDARTTYEL LDVLQKCHCG GHAIIAVLHD YEQVRAYFPN TLLLAREKIA AGATETILTE SYLAQASAKM QQQESPDWCA S // ID Q5F7T9_NEIG1 Unreviewed; 378 AA. AC Q5F7T9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2, 3-sialyltransferase {ECO:0000313|EMBL:AAW89748.1}; GN ORFNames=NGO_1081 {ECO:0000313|EMBL:AAW89748.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89748.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89748.1; -; Genomic_DNA. DR RefSeq; WP_003690950.1; NC_002946.2. DR RefSeq; YP_208160.1; NC_002946.2. DR CAZy; GT52; Glycosyltransferase Family 52. DR EnsemblBacteria; AAW89748; AAW89748; NGO_1081. DR GeneID; 3281757; -. DR KEGG; ngo:NGO1081; -. DR PATRIC; 20335406; VBINeiGon24812_1269. DR HOGENOM; HOG000220741; -. DR KO; K00785; -. DR OMA; CCTPLQV; -. DR OrthoDB; EOG6MD922; -. DR BioCyc; NGON242231:GI2G-993-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR012477; Glyco_transf_52. DR Pfam; PF07922; Glyco_transf_52; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Glycosyltransferase {ECO:0000313|EMBL:AAW89748.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89748.1}. SQ SEQUENCE 378 AA; 43405 MW; A4D168C69D7B3DC1 CRC64; MGLKKVCLTV LCLIVFCFGI FYTFDRVNQG ERNAVSLLKD KLFNEEGKPV NLIFCYTILQ MKVAERIMAQ HPGERFYVVL MSENRNEKYD YYFNQIKDKA ERAYFFYLPY GLNKSFNFIP TMAELKVKSM LLPKVKRIYL ASLEKVSIAA FLSTYPDAEI KTFDDGTNNL IRESSYLGGE FAVNGAIKRN FARMMVGDWS IAKTRNASDE HYTIFKGLKN IMDDGRRKMT YLPLFDASEL KAGDETGGTV RILLGSPDKE MKEISEKAAK NFNIQYVAPH PRQTYGLSGV TALNSPYVIE DYILREIKKN PHTRYEIYTF FSGAALTMKD FPNVHVYALK PASLPEDYWL KPVYALFRQA DIPILAFDDK NQSHGKSK // ID Q5FAH0_NEIG1 Unreviewed; 129 AA. AC Q5FAH0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=DNA (Cytosine-5-)-methyltransferase {ECO:0000313|EMBL:AAW88817.1}; GN ORFNames=NGO_0050 {ECO:0000313|EMBL:AAW88817.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88817.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3HRL} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-126. RA Filippova E.V., Minasov G., Shuvalova L., Kiryukhina O., Cobb G., RA Joachimiak A., Anderson W.F.; RT "Crystal Structure of a Putative Endonuclease-Like Protein (Ngo0050) RT from Neisseria Gonorrhoeae."; RL Submitted (JUN-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; AE004969; AAW88817.1; -; Genomic_DNA. DR RefSeq; WP_003687278.1; NC_002946.2. DR RefSeq; YP_207229.1; NC_002946.2. DR PDB; 3HRL; X-ray; 1.95 A; A=27-126. DR PDBsum; 3HRL; -. DR ProteinModelPortal; Q5FAH0; -. DR DNASU; 3282350; -. DR EnsemblBacteria; AAW88817; AAW88817; NGO_0050. DR GeneID; 3282350; -. DR KEGG; ngo:NGO0050; -. DR PATRIC; 20332940; VBINeiGon24812_0055. DR HOGENOM; HOG000218764; -. DR OMA; DFACHAK; -. DR OrthoDB; EOG6PKFM9; -. DR BioCyc; NGON242231:GI2G-45-MONOMER; -. DR EvolutionaryTrace; Q5FAH0; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF04480; DUF559; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3HRL}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW88817.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88817.1}. FT DOMAIN 15 121 DUF559. {ECO:0000259|Pfam:PF04480}. FT COILED 12 39 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 129 AA; 14987 MW; D785150EB75E7D12 CRC64; MNPPEKLLTA ENPALRQRAK AMRQEMSEAE AKLWQHLRAG RLNGYKFRRQ QPMGNYIVDF MCVTPKLIVE ADGGQHAEQA VYDHARTVYL NSLGFTVLRF WNHEILQQTN DVLAEILRVL QELEKQPAR // ID Q5F677_NEIG1 Unreviewed; 228 AA. AC Q5F677; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90310.1}; GN ORFNames=NGO_1685 {ECO:0000313|EMBL:AAW90310.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90310.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90310.1; -; Genomic_DNA. DR RefSeq; WP_003689839.1; NC_002946.2. DR RefSeq; YP_208722.1; NC_002946.2. DR EnsemblBacteria; AAW90310; AAW90310; NGO_1685. DR GeneID; 3281207; -. DR KEGG; ngo:NGO1685; -. DR PATRIC; 20336928; VBINeiGon24812_2008. DR HOGENOM; HOG000284591; -. DR KO; K09125; -. DR OMA; GEFNLFV; -. DR OrthoDB; EOG65J51G; -. DR BioCyc; NGON242231:GI2G-1580-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 111 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 205 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 228 AA; 25658 MW; 36E818D6859CAB37 CRC64; MYALTAAQQQ KALFRLVLFH ILIIAASNYL VQFPFRIFGI HTTWGAFSFP FIFLATDLTV RIFGSHLARR IIFWVMFPAL LLSYVFSVLF HNGSWTGLGA LSQFNTFVGR IALASFAAYA LGQILDIFVF DKLRRLKAWW IAPAASTVIG NALDTLVFFA VAFYASSDEF MAANWQGIAF VDYLFKLTVC TLFFLPAYGV ILNLLTKKLT ALQTKQAQDR PVPSLQNP // ID Q5F6J7_NEIG1 Unreviewed; 112 AA. AC Q5F6J7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90190.1}; GN ORFNames=NGO_1557 {ECO:0000313|EMBL:AAW90190.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90190.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90190.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90190; AAW90190; NGO_1557. DR BioCyc; NGON242231:GI2G-1458-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 112 AA; 12617 MW; 442F855F48434353 CRC64; MRRAEARPAT LSMHPLASPT LRNILRTHPV KNTRTVPIHR NPKTRHSRAA MGHRRQRGGF PFARTVSALF HHRYAQHGDD ASAGRCNPFD AHGPARQPTW ASKSRACRTI VD // ID Q5F864_NEIG1 Unreviewed; 54 AA. AC Q5F864; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89623.1}; GN ORFNames=NGO_0927 {ECO:0000313|EMBL:AAW89623.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89623.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89623.1; -; Genomic_DNA. DR RefSeq; WP_003688384.1; NC_002946.2. DR RefSeq; YP_208035.1; NC_002946.2. DR EnsemblBacteria; AAW89623; AAW89623; NGO_0927. DR GeneID; 3282583; -. DR KEGG; ngo:NGO0927; -. DR PATRIC; 20335037; VBINeiGon24812_1088. DR HOGENOM; HOG000071281; -. DR OMA; AGKFSHC; -. DR OrthoDB; EOG6PCQ35; -. DR BioCyc; NGON242231:GI2G-865-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 54 AA; 6105 MW; CEEF00CDCB30A649 CRC64; MNKCRLKAFQ TAFCPELRRR GAVAGKSFHC SLFFSNSALY VGNRQIGVVF DSFK // ID Q5F8G3_NEIG1 Unreviewed; 205 AA. AC Q5F8G3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89524.1}; GN ORFNames=NGO_0812 {ECO:0000313|EMBL:AAW89524.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89524.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89524.1; -; Genomic_DNA. DR RefSeq; WP_003691161.1; NC_002946.2. DR RefSeq; YP_207936.1; NC_002946.2. DR ProteinModelPortal; Q5F8G3; -. DR EnsemblBacteria; AAW89524; AAW89524; NGO_0812. DR GeneID; 3281894; -. DR KEGG; ngo:NGO0812; -. DR PATRIC; 20334780; VBINeiGon24812_0960. DR HOGENOM; HOG000022575; -. DR OMA; VRYGFVS; -. DR OrthoDB; EOG64FKBH; -. DR BioCyc; NGON242231:GI2G-766-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 15 131 PGA_cap. {ECO:0000259|Pfam:PF09587}. SQ SEQUENCE 205 AA; 22699 MW; DA0877DDB09FED75 CRC64; MNIKYSGIEN RFETAILKKN GVRYGFVSFA PNLAAVKLND YAKFKKLIRK TKQKTDIVIV MFHGGAEGKQ AEHLPFDTEI FYGENRGNVV EFARLAVDSG ADVVFGQGAH VTRAVELYHD RFISYSGGNF ATYGISGIAP IFKIITDKQG RFVSGNIIPI TQVGDKIPKI DPEKTVIERI IYLNHSDFPN GNGLDVSPGG DITRR // ID Q5F810_NEIG1 Unreviewed; 169 AA. AC Q5F810; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Cation-binding protein {ECO:0000313|EMBL:AAW89677.1}; GN ORFNames=NGO_0993 {ECO:0000313|EMBL:AAW89677.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89677.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89677.1; -; Genomic_DNA. DR RefSeq; WP_003695091.1; NC_002946.2. DR RefSeq; YP_208089.1; NC_002946.2. DR ProteinModelPortal; Q5F810; -. DR SMR; Q5F810; 9-169. DR EnsemblBacteria; AAW89677; AAW89677; NGO_0993. DR GeneID; 3281387; -. DR KEGG; ngo:NGO0993; -. DR PATRIC; 20335190; VBINeiGon24812_1163. DR HOGENOM; HOG000219026; -. DR OMA; NQAVKND; -. DR OrthoDB; EOG6B09V1; -. DR BioCyc; NGON242231:GI2G-920-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF01814; Hemerythrin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 141 Hemerythrin. {ECO:0000259|Pfam:PF01814}. SQ SEQUENCE 169 AA; 19335 MW; 5E83186C8F86FDEC CRC64; MNPFETQSVT FAEPIEMLYA CHGKVRRFCG QIAMLSGYIA ENGCNQLVLQ TIRQISRYFN VAAPLHHEDE EENFFPLLLQ YAPQAREGVD ELLRQHIGLY DNWAAVSAEF AKLEADNAYI PDAEAFKRFV EGYDVHLAIE EPLFDMGKTF IPEEKLTEIG KIMAARRCK // ID Q5F634_NEIG1 Unreviewed; 618 AA. AC Q5F634; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 86. DE SubName: Full=Multidrug ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90353.1}; GN ORFNames=NGO_1732 {ECO:0000313|EMBL:AAW90353.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90353.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90353.1; -; Genomic_DNA. DR RefSeq; WP_010951336.1; NC_002946.2. DR RefSeq; YP_208765.1; NC_002946.2. DR ProteinModelPortal; Q5F634; -. DR EnsemblBacteria; AAW90353; AAW90353; NGO_1732. DR GeneID; 3281146; -. DR KEGG; ngo:NGO1732; -. DR PATRIC; 20337062; VBINeiGon24812_2071. DR KO; K18893; -. DR OMA; IKFEHVD; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1628-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90353.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90353.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 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; 67887 MW; 94908A7D6C616D4C CRC64; MLNKIFSWFE SRIDPYPEAA PKTPEKGLCR FVWSSMDGVR KWIAALAALT AGIGIMEALI FQFMGKIVEW LGKYAPAELF AEKGWELAAM AAMMVFSVVW AFAASNVRLQ TLQGVFPMRL RWNFHRLMLN QSLGFYQDEF AGRVSAKVMQ TALALRDAVM TVADMVVYVS VYFITSGVIL ASLDSWLLLP FIGWIIGFAS VMRLLIPRLG QTAARQANAR SLMTGRITDA YSNIATVKLF FHGAREAVYA KQSMEEFMVT VRAQMRLATL LHSCNFIVNT SLTLSTAALG IWLWHNGQVG VGAVATATAM ALRANGLSQY IMWESARLFE NIGIVNDGMA TLSKPHTILD KPQALPLNVP QGAIKFEHVD FCYEAGKPLL NGFNLNIKPG EKVGLIGRSG AGKSTIVNLL LRFYEPQSGT VSIDGQDISG VTQESLRAQI GLVTQDTSLL HRSVRDNIIY GRPDATDAEM VSAAERAEAA GFIPDLSDAK GRSGYDAHVG ERGVKLSGGQ RQRIAIARVM LKDAPILLLD EATSALDSEV EAAIQESLDK MMEGKTVIAI AHRLSTIAAM DRLVVLDKGR IIEEGTHAEL LEKRGLYAKL WAHQSGGFLS EHVEWQHD // ID Q5F8J2_NEIG1 Unreviewed; 640 AA. AC Q5F8J2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AAW89495.1}; GN ORFNames=NGO_0781 {ECO:0000313|EMBL:AAW89495.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89495.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89495.1; -; Genomic_DNA. DR RefSeq; WP_003691184.1; NC_002946.2. DR RefSeq; YP_207907.1; NC_002946.2. DR ProteinModelPortal; Q5F8J2; -. DR EnsemblBacteria; AAW89495; AAW89495; NGO_0781. DR GeneID; 3282192; -. DR KEGG; ngo:NGO0781; -. DR PATRIC; 20334708; VBINeiGon24812_0926. DR HOGENOM; HOG000271640; -. DR KO; K06158; -. DR OMA; FYLVHDK; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NGON242231:GI2G-735-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 246 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 313 527 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT COILED 591 632 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 640 AA; 71830 MW; 09A01B16F430C961 CRC64; MIEIKNLTLQ RGLKVLLDKA SAAVNPGQRV GLIGKNGTGK SSLFALIKGE ITQDGGDISI PKNWRLASVS QETPDLDISA LDYVLQGDAE LQAFQTALRQ AEVQNDGMKQ AEYHAKLEEI DAYTAPARAA KLLNGLGFSQ EEHSRPVKSF SGGWRMRLNL AQALICRADL LLLDEPTNHL DLETVLWLEN HLASLPCTQI IISHDRDFLN AATTQTIELS QQKLTQYSGN YDFYQTERAQ RLAQQQAAYV KQQAQIKHLQ SFIDRFKAKA TKAVQAQSRM KALAKLERIA PAHLDSEFSF EFYNPDHLPN PLLKLEHADL GYEGKTVLHD ITLSLESGAR YGLLGVNGSG KSTFIKALAG KIDLLSGSIV HSEKLNIGYF AQHQLDTIRA DQSPVWHIQQ LSPEVREQEI RNFLGGFDFV GDMALQKTEP FSGGEKARLA LAMIIWQKPN LLLLDEPTNH LDLDMRHALT LALQSFQGAL IVVSHDRSLL EATTDSFLLI DKGRLKNFDG DLNDYRQWRL AQENAATAPA ASTQSQNRKD TKRIEAQIRQ EKARRSKPIQ QKIDKAEKEM VQLSEIQTGC EAFLTQEDAY LEANKEKLQN TLSELAKVKT QLAQIEETWL ACQEELERIE TEIEKQFAER // ID Q5F960_NEIG1 Unreviewed; 308 AA. AC Q5F960; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 59. DE SubName: Full=Cobalamin biosynthesis protein CobW {ECO:0000313|EMBL:AAW89277.1}; GN ORFNames=NGO_0543 {ECO:0000313|EMBL:AAW89277.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89277.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89277.1; -; Genomic_DNA. DR RefSeq; WP_003706094.1; NC_002946.2. DR RefSeq; YP_207689.1; NC_002946.2. DR ProteinModelPortal; Q5F960; -. DR DNASU; 3282909; -. DR EnsemblBacteria; AAW89277; AAW89277; NGO_0543. DR GeneID; 3282909; -. DR KEGG; ngo:NGO0543; -. DR PATRIC; 20334136; VBINeiGon24812_0640. DR HOGENOM; HOG000294929; -. DR OMA; WHKELYN; -. DR OrthoDB; EOG6N3CQV; -. DR BioCyc; NGON242231:GI2G-517-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 221 307 CobW C-terminal. FT {ECO:0000259|SMART:SM00833}. SQ SEQUENCE 308 AA; 33997 MW; 8B892F01416631FD CRC64; MSEVKKTKVH LISGFLGTGK TTALKSLMAQ KDPNEKWVII VNEFGEIGID GAVLSDNGIP VAEIAGGCLC CTAGPQMGVT VQKMLRDAKP DRLMIEASGL AHAASVIDEL KAKPLDSLLE IGAVFTVVDP RQFINPDYAQ QALYKDQIGI CDVLAASKTD LCTPEQLAEF HDKAAKLFPP KAKVVEVQNA QLDIQWLDIP VVEKSRYRLK ALPDNTMGFQ SQGFTFPAGR DFNGEKLTNF FNDLPKMTEG LVRAKGVFQV LGTWVWLNWV DGQWGANQVS WRRDSRFELI AKSFDADLIE QKLKDALE // ID Q5F555_NEIG1 Unreviewed; 128 AA. AC Q5F555; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=Ribosomal silencing factor RsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN Name=rsfS {ECO:0000256|HAMAP-Rule:MF_01477}; GN ORFNames=NGO_2081 {ECO:0000313|EMBL:AAW90682.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90682.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90682.1; -; Genomic_DNA. DR RefSeq; WP_003687037.1; NC_002946.2. DR RefSeq; YP_209094.1; NC_002946.2. DR ProteinModelPortal; Q5F555; -. DR SMR; Q5F555; 8-124. DR EnsemblBacteria; AAW90682; AAW90682; NGO_2081. DR GeneID; 3282836; -. DR KEGG; ngo:NGO2081; -. DR PATRIC; 20337995; VBINeiGon24812_2520. DR HOGENOM; HOG000016051; -. DR KO; K09710; -. DR OMA; FVICTAN; -. DR OrthoDB; EOG6J48TR; -. DR BioCyc; NGON242231:GI2G-1976-MONOMER; -. DR Proteomes; UP000000535; 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 TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01477}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_01477}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_01477}. SQ SEQUENCE 128 AA; 14016 MW; DB24719A91F82955 CRC64; MNEQELQDLQ KMVGVAVNAL EDIKAKDISV LETQDKTSLF ARMIIASGDS TRQVKALANN VAVDLKEAGF EILSTEGDSG EWTLVDAGDL VVHVMLPAVR DFYDIDTIWG GEKPSFHAGM QKPWHAAD // ID Q5F5Z9_NEIG1 Unreviewed; 387 AA. AC Q5F5Z9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:AAW90388.1}; GN ORFNames=NGO_1769 {ECO:0000313|EMBL:AAW90388.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90388.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR000294-2}; CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-2}; CC -!- PTM: Binds 2 heme groups per subunit. CC {ECO:0000256|PIRSR:PIRSR000294-1}. 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; AE004969; AAW90388.1; -; Genomic_DNA. DR RefSeq; WP_003705279.1; NC_002946.2. DR RefSeq; YP_208800.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z9; -. DR PeroxiBase; 5054; NgDiHCcP. DR EnsemblBacteria; AAW90388; AAW90388; NGO_1769. DR GeneID; 3281141; -. DR KEGG; ngo:NGO1769; -. DR PATRIC; 20337164; VBINeiGon24812_2122. DR HOGENOM; HOG000173945; -. DR KO; K00428; -. DR OMA; YKFANVG; -. DR OrthoDB; EOG6VF30V; -. DR BioCyc; NGON242231:GI2G-1663-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; -; 2. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae. DR InterPro; IPR026259; MauG/Cytc_peroxidase. DR Pfam; PF03150; CCP_MauG; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1. DR SUPFAM; SSF46626; SSF46626; 2. DR PROSITE; PS51007; CYTC; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Heme {ECO:0000256|PIRSR:PIRSR000294-1}; KW Iron {ECO:0000256|PIRSR:PIRSR000294-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000294-1}; KW Oxidoreductase {ECO:0000313|EMBL:AAW90388.1}; KW Peroxidase {ECO:0000313|EMBL:AAW90388.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 387 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256036. FT DOMAIN 89 198 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. FT DOMAIN 242 361 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. FT METAL 115 115 Iron (heme 1 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT METAL 131 131 Iron (heme 1 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT METAL 260 260 Iron (heme 2 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT METAL 336 336 Iron (heme 2 axial ligand). FT {ECO:0000256|PIRSR:PIRSR000294-2}. FT BINDING 111 111 Heme 1 (covalent). FT {ECO:0000256|PIRSR:PIRSR000294-1}. FT BINDING 114 114 Heme 1 (covalent). FT {ECO:0000256|PIRSR:PIRSR000294-1}. FT BINDING 256 256 Heme 2 (covalent). FT {ECO:0000256|PIRSR:PIRSR000294-1}. FT BINDING 259 259 Heme 2 (covalent). FT {ECO:0000256|PIRSR:PIRSR000294-1}. SQ SEQUENCE 387 AA; 41954 MW; B5B0936F761859BE CRC64; MSFKLRYLAS VLALSSLLAA CGGQEKSAAG DASPASETEA ASQVQASEAV PSASSASPED QDLLKRAQGV FQPLPTVEEM QKIRPFTEEQ VKLGHQLWYE PRLSKGNTVS CNSCHNLASA GVDNMPTSQG HKGQFGGRNS PTALNAALLG SQFWDGRAAD VEEQAGGPLV NPVEMANDSQ EAAAAKIAKV PEYQEMFKKA FPEDGAVSFK NITTALGAFE RTLLTPTKWD EYLKGNVNAL SEQERKGVRA FMDNGCIACH NGVNLGGTTF QKFGLVQGPY WKFIEDPKRD KGRADVTKKT EDEFFFRVPG LRNVAKTYPY FHNGSVWELD KAVTIMGKAQ LGKDIPKEDV DNIVVFLNAL SGNVSESART MPELPLTAPM ESKPDNK // ID Q5F946_NEIG1 Unreviewed; 62 AA. AC Q5F946; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89291.1}; GN ORFNames=NGO_0557 {ECO:0000313|EMBL:AAW89291.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89291.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89291.1; -; Genomic_DNA. DR RefSeq; WP_003706114.1; NC_002946.2. DR RefSeq; YP_207703.1; NC_002946.2. DR EnsemblBacteria; AAW89291; AAW89291; NGO_0557. DR GeneID; 3282455; -. DR KEGG; ngo:NGO0557; -. DR PATRIC; 20334168; VBINeiGon24812_0656. DR HOGENOM; HOG000071303; -. DR OrthoDB; EOG61CM9P; -. DR BioCyc; NGON242231:GI2G-531-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 7002 MW; 072CBD923C7270C0 CRC64; MAEHNPPKDI LAAGGACRKV RKVTTENNVS RFQTAYDMDN FIRAGIVFVL LRHLSDGAFF QY // ID Q5FAC8_NEIG1 Unreviewed; 371 AA. AC Q5FAC8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Pilus assembly protein PilM {ECO:0000313|EMBL:AAW88859.1}; GN ORFNames=NGO_0098 {ECO:0000313|EMBL:AAW88859.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88859.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88859.1; -; Genomic_DNA. DR RefSeq; WP_003696683.1; NC_002946.2. DR RefSeq; YP_207271.1; NC_002946.2. DR ProteinModelPortal; Q5FAC8; -. DR DNASU; 3282223; -. DR EnsemblBacteria; AAW88859; AAW88859; NGO_0098. DR GeneID; 3282223; -. DR KEGG; ngo:NGO0098; -. DR PATRIC; 20333093; VBINeiGon24812_0130. DR HOGENOM; HOG000218782; -. DR KO; K02662; -. DR OMA; IGPSETE; -. DR OrthoDB; EOG66QM0S; -. DR BioCyc; NGON242231:GI2G-88-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 371 AA; 41311 MW; DC6CAEA3903133BC CRC64; MRLFKSLKNP KKTDAKLPKK SSGLNNRAAI GIDIDQHSIK MVQLSGRSLN QIQLEKYVIA KLPKNIIQGN KVQNYDQLVT YLQQAYAKLG TSCKNIVASV PQNLATIEQL TYTAKDAELD LQGFVESSIS EASSISLEEA NYDYQVLSQS AVGEAVLSVA SRKDEIEPLI DAFNAAGMKL SALDVDIFGQ YNAYALWINH FAPELADEKV AIFGVYAAQT YALVIQDGKI LYKQETSVSE EQLNQLIQRT YQVTAEKAEE IINSPQKPSD YQESVANYFN QQITQEIQRV LQFYYTTQTA DDMTDIKHIL LTGEAVRQKG IAQTVASQTN ADVQCVHPAR YFANDLKTDE QQFELDAPTL TKAFGLAVRG L // ID Q5F6N2_NEIG1 Unreviewed; 122 AA. AC Q5F6N2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90155.1}; GN ORFNames=NGO_1517 {ECO:0000313|EMBL:AAW90155.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90155.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90155.1; -; Genomic_DNA. DR RefSeq; WP_003689404.1; NC_002946.2. DR RefSeq; YP_208567.1; NC_002946.2. DR EnsemblBacteria; AAW90155; AAW90155; NGO_1517. DR GeneID; 3281503; -. DR KEGG; ngo:NGO1517; -. DR PATRIC; 20336516; VBINeiGon24812_1806. DR HOGENOM; HOG000219096; -. DR OMA; EHVRFEE; -. DR OrthoDB; EOG69KTW5; -. DR BioCyc; NGON242231:GI2G-1421-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 122 AA; 14051 MW; DF1C0D799188766C CRC64; MKPLKRHSAL VGLSREHHHS LSLCVRMLRT PGADHRAELE LHFAELETHF REEEAKFAPI WQNVAPELKT RFEGDHAKLR QMMASPECGN AAWNTAFATT LRDHARFEER ELFPAVEPFL PA // ID Q5F926_NEIG1 Unreviewed; 316 AA. AC Q5F926; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003881}; DE EC=1.8.1.9 {ECO:0000256|RuleBase:RU003881}; GN ORFNames=NGO_0580 {ECO:0000313|EMBL:AAW89311.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89311.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89311.1; -; Genomic_DNA. DR RefSeq; WP_003688968.1; NC_002946.2. DR RefSeq; YP_207723.1; NC_002946.2. DR ProteinModelPortal; Q5F926; -. DR SMR; Q5F926; 2-311. DR EnsemblBacteria; AAW89311; AAW89311; NGO_0580. DR GeneID; 3282257; -. DR KEGG; ngo:NGO0580; -. DR PATRIC; 20334226; VBINeiGon24812_0685. DR HOGENOM; HOG000072912; -. DR KO; K00384; -. DR OMA; GQLEMNN; -. DR OrthoDB; EOG65XN2W; -. DR BioCyc; NGON242231:GI2G-551-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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 Redox-active center {ECO:0000256|RuleBase:RU003880}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 300 FAD/NAD-binding_dom. FT {ECO:0000259|Pfam:PF07992}. SQ SEQUENCE 316 AA; 33654 MW; D88A7C4D61A62EB4 CRC64; MSQHRKLIIL GSGPAGYTAA VYAARANLNP VIITGIAQGG QLMTTTEVDN WPADADGVQG PELMARFLAH AERFGTEIIF DQINAVDLQK RPFALKGDMG EYTCDALIVA TGASAKYLGL PSEEAFAGKG VSACATCDGF FYKNQDVAVV GGGNTAVEEA LYLANIAKTV TLIHRRSEFR AEKIMIDKLM KRVEEGKIIL KLESNLQEVL GDDRGVNGAL LKNNDGSDQQ IAVSGIFIAI GHKPNTDIFK GQLEMDEAGY LKTKGGTADN VGATNIEGVW AAGDVKDHTY RQAITSAASG CQAALDAERW LGSQNI // ID Q5F8I8_NEIG1 Unreviewed; 142 AA. AC Q5F8I8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89499.2}; GN ORFNames=NGO_0785 {ECO:0000313|EMBL:AAW89499.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89499.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89499.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89499; AAW89499; NGO_0785. DR BioCyc; NGON242231:GI2G-739-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 142 AA; 16039 MW; 8FD02CE9B91063D8 CRC64; MKMPACREFL RHCRFDGQCL RRNSEHQGIR PMPNLVTAVL AGRFLRWRIP YPTHQTDNIS SRILTARICW YESSAQAEKA VAPKTVARIN CLNFMMLLLL HKAFGIVKPA AYGFAAVAAL QAVLQETLKH DHCIKSCSNS AK // ID Q5FAG7_NEIG1 Unreviewed; 1004 AA. AC Q5FAG7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 49. DE SubName: Full=Pilus assembly protein {ECO:0000313|EMBL:AAW88820.2}; GN ORFNames=NGO_0055 {ECO:0000313|EMBL:AAW88820.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88820.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88820.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88820; AAW88820; NGO_0055. DR PATRIC; 20332952; VBINeiGon24812_0061. DR HOGENOM; HOG000218767; -. DR OMA; DFPVTAD; -. DR OrthoDB; EOG679T75; -. DR BioCyc; NGON242231:GI2G-48-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008707; PilC_beta_prop_dom. DR Pfam; PF05567; Neisseria_PilC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 480 815 Neisseria_PilC. FT {ECO:0000259|Pfam:PF05567}. SQ SEQUENCE 1004 AA; 110290 MW; C2411C09ADCE376E CRC64; MDERNQPEVK WEGSYSTLRE KDGERKFIYT NQRNKLNQQN NFISFDNTDT LVSRQSGTAV FGTATYLPPY GKVSGFDTAE LNKRGNAVNW IHTTRAGLAG YVYTGVICRD TGQCPQLVYK TRFSFDNTGL AKNTGRLDRH TEPSRENSPI YKLSDYPWLG VSFNLGSEGT AKDGRSSNKL VSSFDENNSN SNQNLVYTTE GHRISLGDWQ RESTAMAYYL NAKLHLLDKQ RIENIAPGKT VDLGTLRPRV ETKTNNWGNL LSFWATWKIE DKGNITVRLG LPEVKAGRCT NTAHPNPNAK APSPALTAPA LWFGPVQNGK VQMYSASVST YPGSSSSRIF LQELKTRTDP ARPGRHSLAA LDTQNIKSRE PNFNSRQTVI RLPGGVYKIN SGKNGGRVAG INGNDGKNDT FGIYKDRLVT PEADEWSNIL LPWTARYYGN DDIFKTFNQP NSKTQNGKKQ YSQKYRIRTK EDDNDKPRDL GDIVNSPIVA VGGYLATSAN DGMVHLFKRN GTDQRGYELK LSYIPGTMER KDIEGNDSDL AKELRAFAEK GYVGDRYGVD GGFVLRRITD DQDKQKHFFM FGAMGLGGRG AYALDLSKID GNYPAAAPLF DVKNGDNNGK NRVKVELGYT VGTPQIGKTQ NGKYAAFLAS GYAAKNIGSG DNKTALYVYD LENGSGSLIK KIEVQGGKGG LSSPTLVDKD LDGTVDIAYA GDRGGNMYRF DLSDSNPDKW SVRTIFEGDK PITSAPAVSR LADKRVVIFG TGSDLTEDDV LNTGEQYIYG IFDDDKGTVK VTVQNGTGGG LLEQVLKEEN KTLFLNKGSD GSGSKGWVVK LKEGQRVTVK PTVVLRTAFV TIRSYTGNDK CGAQTAILGI NTADGGALTP RSARPIVPDN QVAQYSGHQK MNGKSIPIGC MWKNGKTVCP NGYVYDKPVN VRYLDEKKTD DFPVTADGDA GGSGTFKEGK KPARNNRCFS GKGVRTLLMN DLDSLDITGP MCGIKRLSWR EVFF // ID Q5F6R5_NEIG1 Unreviewed; 344 AA. AC Q5F6R5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 58. DE SubName: Full=L,D-transpeptidase catalytic domain protein {ECO:0000313|EMBL:AAW90122.2}; GN ORFNames=NGO_1484 {ECO:0000313|EMBL:AAW90122.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90122.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90122.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6R5; -. DR EnsemblBacteria; AAW90122; AAW90122; NGO_1484. DR PATRIC; 20336419; VBINeiGon24812_1757. DR HOGENOM; HOG000219087; -. DR OMA; AMRARSQ; -. DR OrthoDB; EOG64V2GW; -. DR BioCyc; NGON242231:GI2G-1388-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 344 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364486. FT DOMAIN 33 162 YkuD. {ECO:0000259|Pfam:PF03734}. SQ SEQUENCE 344 AA; 36812 MW; 8BCB66E92C9E61BA CRC64; MNKTICRTAA LLISGFSYAN TVIPDVSPVA QGQHVFINIP QQRLFLYTDG KLTKVYPVAV GRAMTQTNLG EHKIGAKAYN PVWHIPKSIQ KERGDGVKTI AAGPDNPLGP VFVRLGDPKL GLGIHGTNAP ASVPGIRSHG CVRMKSPDAL EFAKTIATGS PASVIYQMAG LNEDADRNLW LAAFRDPYGK NNLDTASLKK SIGQWAKTQG KTIAPEKVDA VLKDRTGSAV CLTCGKNGKM KMPLKSLAWI QGSSSYSQAE VIEQTEETNS AEVSETRTPE VPDVHTPEAQ AHLNTQSDGT PTAYTEPAAD SSPQVESPDQ AASEPVDVLF SIDVIRQGNL RLGN // ID Q5F848_NEIG1 Unreviewed; 375 AA. AC Q5F848; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89639.2}; GN ORFNames=NGO_0948 {ECO:0000313|EMBL:AAW89639.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89639.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89639.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89639; AAW89639; NGO_0948. DR PATRIC; 20335079; VBINeiGon24812_1109. DR HOGENOM; HOG000259527; -. DR OMA; EVYISHR; -. DR OrthoDB; EOG6BCSRW; -. DR BioCyc; NGON242231:GI2G-881-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010653; NlpB/DapX. DR Pfam; PF06804; Lipoprotein_18; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 375 AA; 41337 MW; A5FB25BA1A9DB624 CRC64; MTHIKPVIAA LALIGLAACS GSKTEQPKLD YQSRSHRLIK LEVPPDLNNP DQGNLYRLPA GSGAVRASDL EKRRTPAVQQ PADAEVLKSV KGVRLERDGS QRWLVVDGKS PAEIWPLLKA FWQENGFDIE SEEPAIGQME TEWAENRAKI PQDSLRRLFD TVGLGGIYST GERDKFIVRI EQGKNGVSDI FFAHKAMKEV YGDKNKDTTM WQPSASDPNL EAAFLTRFMQ YLGVDGRQAE NALAKKPTLP AANEMARIEG KSLIVFGDYG RNWRRTGLAL DRIGLTVVGQ NTERHAFLVQ KAPNESNAVT EQKPGLFKRL LGKGKAEKPA EQPELIVYAE PVADGSRIVL LNKDGSAYAG KDASALLGKL HSELR // ID Q5F6Z8_NEIG1 Unreviewed; 182 AA. AC Q5F6Z8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Suppressor of fused family protein {ECO:0000313|EMBL:AAW90039.1}; GN ORFNames=NGO_1391 {ECO:0000313|EMBL:AAW90039.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90039.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3K5J} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS). RX PubMed=20836087; DOI=10.1002/pro.497; RA Das D., Finn R.D., Abdubek P., Astakhova T., Axelrod H.L., RA Bakolitsa C., Cai X., Carlton D., Chen C., Chiu H.J., Chiu M., RA Clayton T., Deller M.C., Duan L., Ellrott K., Farr C.L., Feuerhelm J., RA Grant J.C., Grzechnik A., Han G.W., Jaroszewski L., Jin K.K., RA Klock H.E., Knuth M.W., Kozbial P., Krishna S.S., Kumar A., Lam W.W., RA Marciano D., Miller M.D., Morse A.T., Nigoghossian E., Nopakun A., RA Okach L., Puckett C., Reyes R., Tien H.J., Trame C.B., RA van den Bedem H., Weekes D., Wooten T., Xu Q., Yeh A., Zhou J., RA Hodgson K.O., Wooley J., Elsliger M.A., Deacon A.M., Godzik A., RA Lesley S.A., Wilson I.A.; RT "The crystal structure of a bacterial Sufu-like protein defines a RT novel group of bacterial proteins that are similar to the N-terminal RT domain of human Sufu."; RL Protein Sci. 19:2131-2140(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; AE004969; AAW90039.1; -; Genomic_DNA. DR RefSeq; WP_002227008.1; NC_002946.2. DR RefSeq; YP_208451.1; NC_002946.2. DR PDB; 3K5J; X-ray; 1.40 A; A=1-182. DR PDBsum; 3K5J; -. DR DNASU; 3281298; -. DR EnsemblBacteria; AAW90039; AAW90039; NGO_1391. DR GeneID; 3281298; -. DR KEGG; ngo:NGO1391; -. DR HOGENOM; HOG000220706; -. DR OMA; PIGEPWL; -. DR OrthoDB; EOG6XDGVH; -. DR BioCyc; NGON242231:GI2G-1304-MONOMER; -. DR EvolutionaryTrace; Q5F6Z8; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR020941; SUFU-like_domain. DR Pfam; PF05076; SUFU; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3K5J}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 78 174 SUFU. {ECO:0000259|Pfam:PF05076}. SQ SEQUENCE 182 AA; 21419 MW; 969B3834879E2463 CRC64; MDYNQTVLSH LQKFWKHHDI KGFTWTLGRI VEELPDFQVF QVIPNHEDEP WVYVSSGIGQ FLGQEFFIIS PFETPEHIET LAMLASASMH YPDQFQLGKT VNIGRPWVEQ SSFRHFLISL PYPYGQELEY MDNVRFFWLL PITQTERLFL NTHSVEELET KFDEAGIDYL DINRASTVWQ AG // ID Q5F7M0_NEIG1 Unreviewed; 256 AA. AC Q5F7M0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89817.1}; GN ORFNames=NGO_1150 {ECO:0000313|EMBL:AAW89817.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89817.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89817.1; -; Genomic_DNA. DR RefSeq; WP_003689746.1; NC_002946.2. DR RefSeq; YP_208229.1; NC_002946.2. DR EnsemblBacteria; AAW89817; AAW89817; NGO_1150. DR GeneID; 3282159; -. DR KEGG; ngo:NGO1150; -. DR PATRIC; 20335562; VBINeiGon24812_1346. DR HOGENOM; HOG000219045; -. DR OMA; QLNILNP; -. DR OrthoDB; EOG6CZQJ9; -. DR BioCyc; NGON242231:GI2G-1063-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 256 AA; 29249 MW; 97C352D63E295661 CRC64; MDTNNQDKEP NWEKRLENLR QTRRMNTAPA YVPLTKPSEV GKEEPIPKLD DANRDRVLKA YLKKWQEEHN SAVADCGEEV ETDPMIVLQE NWLNAQASLQ MPVSEKHIES RRRIRFDAKK DSAEFETAQI EGGENADAAE SGTAADGVAE NGEGGAEEAL MPVQINILNP KAVNRREVFC LSEQELTERL IKRLRPHLTD TVNGMIRTAV QKQMALFTYQ LQQMLHEQAG AVVEDVLEHD VRKILNDIKY ELKYKR // ID Q5FA75_NEIG1 Unreviewed; 293 AA. AC Q5FA75; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 63. DE SubName: Full=Lipid A biosynthesis lauroyl acyltransferase {ECO:0000313|EMBL:AAW88912.2}; GN ORFNames=NGO_0154 {ECO:0000313|EMBL:AAW88912.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88912.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88912.2; -; Genomic_DNA. DR RefSeq; WP_003704869.1; NC_002946.2. DR RefSeq; YP_207324.2; NC_002946.2. DR ProteinModelPortal; Q5FA75; -. DR EnsemblBacteria; AAW88912; AAW88912; NGO_0154. DR GeneID; 3281330; -. DR KEGG; ngo:NGO0154; -. DR PATRIC; 20333231; VBINeiGon24812_0198. DR HOGENOM; HOG000265960; -. DR KO; K02517; -. DR OMA; EMKFIFF; -. DR OrthoDB; EOG657J8B; -. DR BioCyc; NGON242231:GI2G-142-MONOMER; -. DR Proteomes; UP000000535; 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; IPR004960; LipA_acyltrans. DR Pfam; PF03279; Lip_A_acyltrans; 1. DR PIRSF; PIRSF026649; MsbB; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000313|EMBL:AAW88912.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88912.2}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 293 AA; 34302 MW; E48B6A937B3D5819 CRC64; MCTEMKFIFF VLYVLQFLPF ALLHKIAGLI GSLAYLLVKP RRRIGEINLA KCFPEWDEEK RKTVLKQHFK HMAKLMLEYG LYWYASAKCL KSLVRYRNKH YLDDALAAGE KVIILYPHFT AFEMAVYALN QDVPLISMYS HQKNKILDEQ ILKGRNRYHN VFLIGRTEGL RALVKQFRKS SAPFLYLPDQ DFGRNNSVFV DFFGIQTATI TGLSRIAALA NAKVIPAIPV READNTVTLQ FYPAWKSFPS EDAQADAQRM NRFIEERVRE HPEQYFWLHK RFKTRPEGSP DFY // ID Q5F8E4_NEIG1 Unreviewed; 223 AA. AC Q5F8E4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89543.1}; GN ORFNames=NGO_0834 {ECO:0000313|EMBL:AAW89543.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89543.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89543.1; -; Genomic_DNA. DR RefSeq; WP_003693243.1; NC_002946.2. DR RefSeq; YP_207955.1; NC_002946.2. DR EnsemblBacteria; AAW89543; AAW89543; NGO_0834. DR GeneID; 3282240; -. DR KEGG; ngo:NGO0834; -. DR PATRIC; 20334824; VBINeiGon24812_0982. DR HOGENOM; HOG000265565; -. DR OMA; MNIQTRR; -. DR OrthoDB; EOG600DTR; -. DR BioCyc; NGON242231:GI2G-785-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. 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. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 223 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256619. SQ SEQUENCE 223 AA; 23711 MW; AB143C1C3BABFF73 CRC64; MKTVSAAIAF AAAAVSLTGC ATESSRSLEV AKVASCNTQY HGVRTPISVG TFDNRSSFQK GIFSDSEDRL GSQAKTILVT HLQQTNRFNV LNRTNLSALK QESGISGKAQ NLKGADYVVT GDVTEFGRRD VGDHQLFGIL GRGKSQIAYA KVALNIVNVN TSEIVYSTQG AGEYALSNRE IIGFGGTSGY DATLNGKVLD LAIREAVDNL VQAVDNGAWQ SNR // ID Q5F7X8_NEIG1 Unreviewed; 207 AA. AC Q5F7X8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Transglycosylase {ECO:0000313|EMBL:AAW89709.1}; GN ORFNames=NGO_1033 {ECO:0000313|EMBL:AAW89709.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89709.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89709.1; -; Genomic_DNA. DR RefSeq; WP_003688215.1; NC_002946.2. DR RefSeq; YP_208121.1; NC_002946.2. DR ProteinModelPortal; Q5F7X8; -. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR DNASU; 3281132; -. DR EnsemblBacteria; AAW89709; AAW89709; NGO_1033. DR GeneID; 3281132; -. DR KEGG; ngo:NGO1033; -. DR PATRIC; 20335286; VBINeiGon24812_1209. DR HOGENOM; HOG000219015; -. DR OMA; QVMPFWT; -. DR OrthoDB; EOG6S52QZ; -. DR BioCyc; NGON242231:GI2G-954-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256611. FT DOMAIN 95 189 SLT. {ECO:0000259|Pfam:PF01464}. SQ SEQUENCE 207 AA; 23375 MW; CED8C75637B9512F CRC64; MKKPTDTLPV NLQRRRLLCA AGALLISPLA HAGAQREETL ADDVASVMRS SVGSVNPPRL VFDNPKEGER WLSAMSARLA RFVPDEGERR RLLVNIQYES SRAGLDTQIV LGLIEVESAF RQYAISGVGA RGLMQVMPFW KNYIGKPAHN LFDIRTNLRY GCTILRHYRN LEKGDIVRAL ARFNGSLGSN KYPNAVLGAW RNRWQWR // ID Q5F548_NEIG1 Unreviewed; 252 AA. AC Q5F548; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 82. DE SubName: Full=Iron ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90689.1}; GN ORFNames=NGO_2088 {ECO:0000313|EMBL:AAW90689.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90689.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90689.1; -; Genomic_DNA. DR RefSeq; WP_003687045.1; NC_002946.2. DR RefSeq; YP_209101.1; NC_002946.2. DR ProteinModelPortal; Q5F548; -. DR EnsemblBacteria; AAW90689; AAW90689; NGO_2088. DR GeneID; 3282829; -. DR KEGG; ngo:NGO2088; -. DR PATRIC; 20338009; VBINeiGon24812_2527. DR KO; K02013; -. DR OMA; EQDHQVV; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NGON242231:GI2G-1983-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90689.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90689.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 236 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 252 AA; 28202 MW; 7FBFCDE48217B8F6 CRC64; MITIRNVSYR IGTHPILDNV SLDIPEGGIT ALIGPNGAGK STLFSFMARL RPLESGSIAY RGKNLAGTPT AELARTLSIL TQENSIMSRI TVRDLLMFGR YPYHQGRPTA ECRRIVNGAI EEFHLQDLSD RYLTELSGGQ RQRAMIAMVF CQSTDYVLLD EPLNNLDMYH ARSLMQILQK LTHEHKRTTV AVLHDINQAA AYADHVVAMK NGKAALTGTP EEVFTVHNIK ELFDMDVDVL DYEGKKLIVH HI // ID Q5F9E5_NEIG1 Unreviewed; 203 AA. AC Q5F9E5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 52. DE SubName: Full=Pilus assembly protein PilV {ECO:0000313|EMBL:AAW89192.1}; GN ORFNames=NGO_0453 {ECO:0000313|EMBL:AAW89192.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89192.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89192.1; -; Genomic_DNA. DR RefSeq; WP_010951045.1; NC_002946.2. DR RefSeq; YP_207604.1; NC_002946.2. DR EnsemblBacteria; AAW89192; AAW89192; NGO_0453. DR GeneID; 3282991; -. DR KEGG; ngo:NGO0453; -. DR PATRIC; 20333938; VBINeiGon24812_0543. DR HOGENOM; HOG000218894; -. DR KO; K02671; -. DR OMA; IHYAVCK; -. DR OrthoDB; EOG680X1B; -. DR BioCyc; NGON242231:GI2G-430-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 17 38 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 203 AA; 22077 MW; 81D3A210CEE6D861 CRC64; MKNNDCLRLK NPQSGMALIE VLVAMLVLTI GILALLSVQL RTVASVREAE TQTIVSQITQ NLMEGMLMNP TIDLDSNKKN YSLYMGKQTL SAVDGEFMLD AEKSKAQLAE EQLKRFSHEL KNALPDAVAI HYAVCKDSSG DAPTLSDSGA FSSNCDNKAN GDTLIKVLWV NDSAGDSDIS RTNLEVSGDN IVYTYQARVG GRE // ID Q5F5E8_NEIG1 Unreviewed; 186 AA. AC Q5F5E8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90589.1}; GN ORFNames=NGO_1981 {ECO:0000313|EMBL:AAW90589.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90589.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90589.1; -; Genomic_DNA. DR RefSeq; WP_010951375.1; NC_002946.2. DR RefSeq; YP_209001.1; NC_002946.2. DR EnsemblBacteria; AAW90589; AAW90589; NGO_1981. DR GeneID; 3282643; -. DR KEGG; ngo:NGO1981; -. DR PATRIC; 20337727; VBINeiGon24812_2390. DR HOGENOM; HOG000218710; -. DR OMA; RPPYPAC; -. DR OrthoDB; EOG618QSW; -. DR BioCyc; NGON242231:GI2G-1879-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 186 AA; 20357 MW; C11A4C78D74E5100 CRC64; MPSETPDRPP YPACRPCLKP PNRPNPPFYK LYPISCLFQD TPTLECQTVR NGQTPHPSKG IKMKLLTTAI LSSAIALSSM AAAAGTNNPT VAKKTVSYVC QQGKKVKVTY GFNKQGLTTY ASAVINGKRV QMPINLDKSD NMDTFYGKEG GYVLSTGAMD SKSYRKQPIM ITAPDNQIVF KDCSPR // ID Q5F712_NEIG1 Unreviewed; 144 AA. AC Q5F712; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Biopolymer transporter ExbD {ECO:0000313|EMBL:AAW90025.1}; GN ORFNames=NGO_1377 {ECO:0000313|EMBL:AAW90025.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90025.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU003879}; Single-pass type II membrane CC protein {ECO:0000256|RuleBase:RU003879}. CC -!- SIMILARITY: Belongs to the exbD/tolR family. CC {ECO:0000256|RuleBase:RU003879}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90025.1; -; Genomic_DNA. DR RefSeq; WP_003693740.1; NC_002946.2. DR RefSeq; YP_208437.1; NC_002946.2. DR ProteinModelPortal; Q5F712; -. DR EnsemblBacteria; AAW90025; AAW90025; NGO_1377. DR GeneID; 3281762; -. DR KEGG; ngo:NGO1377; -. DR PATRIC; 20336143; VBINeiGon24812_1620. DR HOGENOM; HOG000134906; -. DR KO; K03559; -. DR OMA; RAMASIE; -. DR OrthoDB; EOG6TJ80C; -. DR BioCyc; NGON242231:GI2G-1290-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protein transport {ECO:0000256|RuleBase:RU003879}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003879}. FT TRANSMEM 20 40 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 144 AA; 15514 MW; 4819D6B5138E9339 CRC64; MAFGSMNSSD DSPMSDINVT PLVDVMLVLL IVFMITMPVL THSIPLELPT ASEQANKQDK QPKDPLRLTI DANGGYYVGG DSASKVEIGE VESRLKAAKE QNENVIVAIA ADKAVEYDYV NKALEAARQA GITKIGFVTE TKAQ // ID Q5F9W2_NEIG1 Unreviewed; 1593 AA. AC Q5F9W2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW89025.1}; GN ORFNames=NGO_0275 {ECO:0000313|EMBL:AAW89025.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89025.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89025.1; -; Genomic_DNA. DR RefSeq; WP_010951019.1; NC_002946.2. DR RefSeq; YP_207437.1; NC_002946.2. DR ProteinModelPortal; Q5F9W2; -. DR MEROPS; S06.001; -. DR EnsemblBacteria; AAW89025; AAW89025; NGO_0275. DR GeneID; 3281612; -. DR KEGG; ngo:NGO0275; -. DR PATRIC; 20333521; VBINeiGon24812_0341. DR HOGENOM; HOG000218846; -. DR KO; K01347; -. DR OMA; AAPQDYM; -. DR OrthoDB; EOG66F02T; -. DR BioCyc; NGON242231:GI2G-257-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 1593 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255564. FT DOMAIN 28 322 Peptidase S6. FT {ECO:0000259|PROSITE:PS51691}. FT DOMAIN 1341 1593 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. FT COILED 1021 1048 {ECO:0000256|SAM:Coils}. FT COILED 1097 1187 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1593 AA; 175914 MW; 979A623D6FBD7994 CRC64; MKAKRFKINA ISLSIFLAYA LTPYSEAALV RDDVDYQIFR DFAENKGKFF VGATDLSVKN KRGQNIGNAL SNVPMIDFSV ADVNKRIATV VDPQYAVSVK HAKAEVHTFY YGQYNGHNDV ADKENEYRVV EQNNYEPHKA WSASNLGRLE DYNMARFNKF VTEVAPIAPT DAGGGLDTYK DKNRFSSFVR IGAGRQLVYE KGVYHQEGNE KGYDLRDLSQ AYRYAIAGTP YKDINIDQTM NTEGLIGFGN HNKQYSAEEL KQALSQDALT NYGVLGDSGS PLFAFDKQKN QWVFLGTYDY WAGYGKKSWQ EWNIYKKEFA DKIKQHDNAG TVKGNGEHHW KTTGTNSHIG STAVRLANNE GDANNGQNVT FEDNGTLVLD QNINQGAGGL FFKGDYTVKG ANNDITWLGA GIDVADGKKV VWQVKNPNGD RLAKIGKGTL EINGTGVNQG QLKVGDGTVI LNQKADSNQK VQAFSQVGIV SGRGTLVLNS PDQINPNNLY FGFRGGRLDA NGNDLTFEHI RNVDEGARIV NHNTDHASTI TLTGKSLITN PNSLSVHSIQ NDYDEDNYSY YYRPRRPIPQ GKDLYYKNYR YYALKSGGSV NAPMPENGQT ENNDWILMGS TQEEAKKNAM NHKNNQRISG FSGFFGEENG KGHNGALNLN FNGKSAQNRF LLTGGANLNG KISVTQGNVL LSGRPTPHAR DFVNKSSARK DAHFSKNNEV VFEDDWINRT FKAAEIAVNQ SASFSSGRNV SDITANITAT DNAKVNLGYK NGDEVCVRSD YTGYVTCNTG NLSDKALNSF DATRINGNVN LNQNAALVLG KAALWGQIQG QGNSRVSLNQ HSKWHLTGDS QVHNLSLADS HIHLNNASDA QSANKYHTIK INHLSGNGHF HYLTDLAKNL GDKVLVKESA SGHYQLHVQN KTGEPNQEGL DLFDASSVQD RSRLFVSLAN HYVDLGALRY TIKTENGITR LYNPYAGNRR PVKPAPSPAA NTASQAQKAT QTDGAQIAKP QDIVVAPPSP QANQAEEAKR QQAKAEQVKR QQAEAGRKSA ELSAKQRAGE EERRQTAQSQ PQRRKRRAAP QDYMAVSQDR PKRRGHRSVQ QNNVEIAQAQ AELARRQQEE RKAAELLAKQ RAEAEREAQA LAARRKAEAE EAKHQAAELA HRQEAKRKAA ESAKRKAEEE EHRQTAQSQP QRRKRRAAPQ DYMAVSQDRP KRRGRRSTLP APPSPSFDSS AYAAPRALHN PDWYENDYEE IPLDALEDED VSESVDTSDK QPQDNTELHE KVEAVSLQPR AAQPRTQAAA QADAVSTNTN SALSDAMAST QSILLDTGAS LTRHIAQKSR ADAEKNSVWM SNTGYGRDYA SAQYRRFSSK RTQTQIGIDR SLSENMQIGG VLTYSDSQHT FDQAGGKNTF VQANLYGKYY LNDAWYVAGD IGAGSLRSRL QTQQKANFNR TSIQTGLTLG NTLKINQFEI VPSAGIRYSR LSSADYKLGD DSVKVSSMAV KTLTAGLDFA YRFKVGNLTV KPLLSAAYFA NYGKGGVNVG GKSFAYKADN QQQYSAGAAL LYRNVTLNVN GSITKGKQLE KQKSGQIKIQ IRF // ID Q5F891_NEIG1 Unreviewed; 54 AA. AC Q5F891; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89596.1}; GN ORFNames=NGO_0897 {ECO:0000313|EMBL:AAW89596.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89596.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89596.1; -; Genomic_DNA. DR RefSeq; WP_003688479.1; NC_002946.2. DR RefSeq; YP_208008.1; NC_002946.2. DR EnsemblBacteria; AAW89596; AAW89596; NGO_0897. DR GeneID; 3281116; -. DR KEGG; ngo:NGO0897; -. DR PATRIC; 20334967; VBINeiGon24812_1053. DR OrthoDB; EOG6TBHRH; -. DR BioCyc; NGON242231:GI2G-838-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 54 AA; 5918 MW; A61C73A93B7C4E19 CRC64; MFNPNLKREA VCEIPSEAQS GLQTGFAIFI AAFLPYPDFC LGLKQIGSQI AIEE // ID Q5F680_NEIG1 Unreviewed; 507 AA. AC Q5F680; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 81. DE SubName: Full=Multidrug resistance protein B {ECO:0000313|EMBL:AAW90307.1}; GN Name=emrB {ECO:0000313|EMBL:AAW90307.1}; GN ORFNames=NGO_1682 {ECO:0000313|EMBL:AAW90307.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90307.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90307.1; -; Genomic_DNA. DR RefSeq; WP_010951322.1; NC_002946.2. DR RefSeq; YP_208719.1; NC_002946.2. DR ProteinModelPortal; Q5F680; -. DR EnsemblBacteria; AAW90307; AAW90307; NGO_1682. DR GeneID; 3281262; -. DR KEGG; ngo:NGO1682; -. DR PATRIC; 20336922; VBINeiGon24812_2005. DR HOGENOM; HOG000112190; -. DR KO; K03446; -. DR OMA; SSEQSTW; -. DR OrthoDB; EOG6ZH2DN; -. DR BioCyc; NGON242231:GI2G-1577-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00461639, KW ECO:0000256|SAAS:SAAS00461653, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 269 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 302 322 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 507 AA; 54784 MW; C52CB1B747048172 CRC64; MDYPPLKGAA LAWVTLSLGL AVFMEVLDTT IANVAVPVIA GNLGAATTQG TWVITSFSVA NAVSVPLTGF LAKRIGEVKL FTAAAAGFVI ASWLCGIAPN LQSLVVFRIL QGFIAGPLIP LSQSLLMASY PPAKRMLALA LWAMTVVVAP VLGPILGGWI SGNWHWGWIF FINIPIGIIS AWITWKHLKH RETATVRTPT DYVGLTLMMV GIGALQMMLD RGKELDWFAS GEIITLGITA LVCLSYFIVW ELGEKYPIVD LSLFKDRNFT VGVIATSLGF MVYMGTLTLL PLVLQTNLGY TSAWAGLAAA PVGILPVFLS PLIGRFGNKI DMRLLVTASF LTFAFTFYWR TDFYADMDIG NVIWPQFWQG VGVAMFFLPL TTITLSHMKG GQIAAAGSLS NFLRVLMGGV GVSVVSTLWE RREALHHTRF AEHITPYSAT LHETAAHLSQ QGISDGQTLG IINNTITQQG FIIGSNEIFL AGSILFIVLI PIGWLAKPPF HSGGGGH // ID Q5F6I4_NEIG1 Unreviewed; 161 AA. AC Q5F6I4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. 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 ORFNames=NGO_1574 {ECO:0000313|EMBL:AAW90203.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90203.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90203.1; -; Genomic_DNA. DR RefSeq; WP_003705668.1; NC_002946.2. DR RefSeq; YP_208615.1; NC_002946.2. DR ProteinModelPortal; Q5F6I4; -. DR EnsemblBacteria; AAW90203; AAW90203; NGO_1574. DR GeneID; 3281096; -. DR KEGG; ngo:NGO1574; -. DR PATRIC; 20336674; VBINeiGon24812_1883. DR HOGENOM; HOG000256113; -. DR KO; K01095; -. DR OMA; VWDEIAG; -. DR OrthoDB; EOG6P5ZM2; -. DR BioCyc; NGON242231:GI2G-1471-MONOMER; -. DR UniPathway; UPA00084; UER00504. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006162}; 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:UP000000535}; 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; 17756 MW; 19E3E6CB8A1D8747 CRC64; MADFKPDFAW LLKRPLCFLA FGFGSGLVPF APGTFGTLAA LPLAFVLILL GIDGLLLAFV CIVLFMWGIR ICACAERETG VSDHGGIVWD EIVAMLFVLA FVPFRWTWWL AAFVLFRLFD ALKPPPVGWF DKNLHGGLGI MADDMAAAVM TLIVLRIAML F // ID Q5F963_NEIG1 Unreviewed; 365 AA. AC Q5F963; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Conjugal transfer protein {ECO:0000313|EMBL:AAW89274.1}; GN ORFNames=NGO_0539 {ECO:0000313|EMBL:AAW89274.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89274.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89274.1; -; Genomic_DNA. DR RefSeq; WP_003689027.1; NC_002946.2. DR RefSeq; YP_207686.1; NC_002946.2. DR EnsemblBacteria; AAW89274; AAW89274; NGO_0539. DR GeneID; 3282912; -. DR KEGG; ngo:NGO0539; -. DR PATRIC; 20334128; VBINeiGon24812_0636. DR HOGENOM; HOG000218981; -. DR OMA; EGSHTRQ; -. DR OrthoDB; EOG6KQ6C6; -. DR BioCyc; NGON242231:GI2G-514-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 365 AA; 40330 MW; 28481DE3D0162FA2 CRC64; MNQTFTLPDT RPYPQNPIKN HLLLNAYQLA HNSSQASRKL SSGQLQTEIR GMLEQNHYIN LSLALTMSPD AGTYAALLSS VNAVLDCEKE GEVQWFALPV VLVSGCKKER AIEMKLPTEA LFACLQNYPH LRALTQETQW LPYLVHSSDL SAVAPDEWWR AKQNTEAAAQ HLRRFAPRPL LLPEGQSVHV VYVLGFGSGK VQAALGQNLL QAGLPLMQVW QENLASEGIT LFANPLSPDT PARALSDGSH TRQRMAMDVF AANAIRAVRM QGPRVGVVAA AKAGGQILFG FNATDGAFEV VPQVFCWQLS FTDNIAVIQQ NFLDLMAECR VEHVYLLHNP LGEQENIPSY AEALKREGRN PFFSA // ID Q5F9S2_NEIG1 Unreviewed; 557 AA. AC Q5F9S2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 86. DE RecName: Full=DNA repair protein RecN {ECO:0000256|PIRNR:PIRNR003128}; DE AltName: Full=Recombination protein N {ECO:0000256|PIRNR:PIRNR003128}; GN ORFNames=NGO_0318 {ECO:0000313|EMBL:AAW89065.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89065.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89065.1; -; Genomic_DNA. DR RefSeq; WP_010951028.1; NC_002946.2. DR RefSeq; YP_207477.1; NC_002946.2. DR ProteinModelPortal; Q5F9S2; -. DR EnsemblBacteria; AAW89065; AAW89065; NGO_0318. DR GeneID; 3281718; -. DR KEGG; ngo:NGO0318; -. DR PATRIC; 20333619; VBINeiGon24812_0389. DR HOGENOM; HOG000009327; -. DR KO; K03631; -. DR OMA; QVICVTH; -. DR OrthoDB; EOG6WQD34; -. DR BioCyc; NGON242231:GI2G-298-MONOMER; -. DR Proteomes; UP000000535; 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; -; 2. 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; 2. DR TIGRFAMs; TIGR00634; recN; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA damage {ECO:0000256|PIRNR:PIRNR003128}; KW DNA repair {ECO:0000256|PIRNR:PIRNR003128}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 508 SMC_N. {ECO:0000259|Pfam:PF02463}. FT COILED 161 195 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 557 AA; 61132 MW; 20177B5B0064CF46 CRC64; MLLTLSLRDF VIVENLNLDF QSGFTVLTGE TGAGKSITLD AIGLLLGDKA DYSQVRSGAK EAQLSALFDI SHLPALKAEL REQGLLDEGG EELSIRRIID AKGKSRSFIN NQAATLAQLK AVGGQLIDIH GQNDHHSLNQ EAAQRELLDA FVGGRVQAET VRQLYQNWAN AKKALQEAQE HADAVIIERE RLEWQFNELN QLDIKQGEWE AFSQSHDSLA HSAELLQAAE EVGSKIDGDN GIQRHIYQCQ KLLANLQNIE PRFAESLNML ASIEAELGEI SANMRDVAGH SDINPNELAA QEQRMGELMG MARKYRIEPE ELPAKLAEIE ERLQSLQAAA DLDALEHNVA HNFAEYQEAA HILSAMRHQA AGRLSSDTTE HMQHLAMKGA RFDIVLLPSS PTAHGLEQVQ FQVAANKGNP PRPLNKVASG GELARISLAL QVVASQYTQV PTLIFDEVDT GIGGGVAEMV GKALRALGRK HQVLAVTHLP QVASCGENHW RVRKHSEGEQ TVSEISILDE IQRIEEVARM LGGEVITDTT RQHAAELLQL ASKNSLF // ID Q5F7J7_NEIG1 Unreviewed; 99 AA. AC Q5F7J7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Competence protein ComE {ECO:0000313|EMBL:AAW89840.1}; GN ORFNames=NGO_1178 {ECO:0000313|EMBL:AAW89840.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89840.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89840.1; -; Genomic_DNA. DR RefSeq; WP_010361840.1; NC_002946.2. DR RefSeq; YP_208252.1; NC_002946.2. DR ProteinModelPortal; Q5F7J7; -. DR EnsemblBacteria; AAW89840; AAW89840; NGO_1178. DR GeneID; 3281994; -. DR KEGG; ngo:NGO1178; -. DR PATRIC; 20335639; VBINeiGon24812_1383. DR HOGENOM; HOG000257817; -. DR KO; K02237; -. DR OMA; MIKKWFA; -. DR OrthoDB; EOG6GFGQQ; -. DR BioCyc; NGON242231:GI2G-1087-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 99 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256055. FT DOMAIN 29 48 HhH1. {ECO:0000259|SMART:SM00278}. FT DOMAIN 59 78 HhH1. {ECO:0000259|SMART:SM00278}. SQ SEQUENCE 99 AA; 10266 MW; 5ECD2BE4D0EF9107 CRC64; MKKMFVLFCM LFSCAFSLAA VNINAASQQE LEALPGIGPA KAKAIAEYRA QNGAFKSVDD LIKVKGIGPA VLAKLKDQAS VGAPAPKGPA KPVLPAVKK // ID Q5F5D3_NEIG1 Unreviewed; 176 AA. AC Q5F5D3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Serine hydrolase family protein {ECO:0000313|EMBL:AAW90604.1}; GN ORFNames=NGO_1996 {ECO:0000313|EMBL:AAW90604.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90604.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90604.1; -; Genomic_DNA. DR RefSeq; WP_003686894.1; NC_002946.2. DR RefSeq; YP_209016.1; NC_002946.2. DR ProteinModelPortal; Q5F5D3; -. DR DNASU; 3282628; -. DR EnsemblBacteria; AAW90604; AAW90604; NGO_1996. DR GeneID; 3282628; -. DR KEGG; ngo:NGO1996; -. DR PATRIC; 20337761; VBINeiGon24812_2407. DR HOGENOM; HOG000218714; -. DR OMA; HGWAQRQ; -. DR OrthoDB; EOG64JFP2; -. DR BioCyc; NGON242231:GI2G-1894-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR010662; Hydrolase_RBBP9/YdeN. DR Pfam; PF06821; Ser_hydrolase; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90604.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 176 AA; 19594 MW; 8D68E1C98B17927B CRC64; MESFELEDLT LWLIRDADEA EMWIDRWAVS YPVVQMSEAS ANGSTEAWQS ALQTAFERIQ GRHIAVVAHG AGAAAFLAWL YRADILTQKK LAGIILVSPR PDIFPDDAEH TFQRVRCPCR AALVVSEHGG VPHGWAQKQA DLWNARLLVS PHSGSLNGML GGWQWGMKLM QEMLLA // ID Q5F5K7_NEIG1 Unreviewed; 324 AA. AC Q5F5K7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90530.1}; GN ORFNames=NGO_1917 {ECO:0000313|EMBL:AAW90530.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90530.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90530.1; -; Genomic_DNA. DR RefSeq; WP_003688067.1; NC_002946.2. DR RefSeq; YP_208942.1; NC_002946.2. DR EnsemblBacteria; AAW90530; AAW90530; NGO_1917. DR GeneID; 3282859; -. DR KEGG; ngo:NGO1917; -. DR PATRIC; 20337568; VBINeiGon24812_2312. DR HOGENOM; HOG000230189; -. DR OMA; HLRMTDS; -. DR OrthoDB; EOG6RC3R0; -. DR BioCyc; NGON242231:GI2G-1819-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 298 318 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 324 AA; 35852 MW; 6CE13187A44D1EF2 CRC64; MTEYPGIGSP LFYGVFFAAV LVMIALDMFS LKKNGSHKVG IKETLAWSGL WVAVSCLFAG WLYFELAGNP GYGAAAAKEK VLEFFTGYIL EKSLAVDNIF VFLMIFGYFK VAPQFQHRVL LYGVLGALVL RTVMIFVGAA LVRQFEWILY LFGAFLLYTG IHMMKPEGDE EEDLANSRLL NAVKKVVPVG TAFHGEKFFT VENGKKIATP LFLVLIMIEL SDVVFAVDSI PAVFAVTTDP FIVLTSNIFA ILGLRAMYFL LADVAERFIF LKYGLAFVLG FIGVKMLVMH WVHIPISVSL SVVFGALGAS ILTSLIYTKK QPDK // ID Q5F655_NEIG1 Unreviewed; 456 AA. AC Q5F655; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. 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 ORFNames=NGO_1711 {ECO:0000313|EMBL:AAW90332.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90332.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90332.1; -; Genomic_DNA. DR RefSeq; WP_010951328.1; NC_002946.2. DR RefSeq; YP_208744.1; NC_002946.2. DR ProteinModelPortal; Q5F655; -. DR SMR; Q5F655; 2-449. DR EnsemblBacteria; AAW90332; AAW90332; NGO_1711. DR GeneID; 3281154; -. DR KEGG; ngo:NGO1711; -. DR PATRIC; 20337014; VBINeiGon24812_2047. DR HOGENOM; HOG000252916; -. DR KO; K01756; -. DR OMA; TFGKEMA; -. DR OrthoDB; EOG686NDB; -. DR BioCyc; NGON242231:GI2G-1607-MONOMER; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:AAW90332.1}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 13 312 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 331 446 ASL_C. {ECO:0000259|Pfam:PF08328}. SQ SEQUENCE 456 AA; 50337 MW; 10949E2BAA2A60AF CRC64; MINPIASLSP LDGRYAQSVE ALRPIFSEYG LMKARVKVEL NWLKALAAEP EIAEVPPFSA ETLAEIDKVI ENFSLEDAAA VKAIEATTNH DVKAIEYWLK KRFAEVPEVA AVSEFIHFAC TSEDINNLSH ALMLQEARET VILPKLAEII GKLTAMAHDL AAVPMMSRTH GQPATPTTLG KETANVVYRL QRQFKILQAQ EFLGKINGAV GNYNAHMAAY PDVDWETHCR NFVEISLGLT FNPYTIQIEP HDYMAEFFQT LSRINTILID FSRDVWGYIS LGYFKQKVKA GEVGSSTMPH KVNPIDFENS EGNLGMANAV LGFLAEKLPV SRWQRDLTDS TVLRNMGVGV GYAVLGFAAH LRGLNKLEPN PAALAADLDV TWELLAEPIQ TVMRRYGVAN PYEKLKDLTR GKGGITPEVL KGFIGSLEIP AEAKAKLLEL TPALYVGKAE ALAKRI // ID Q5F9E4_NEIG1 Unreviewed; 326 AA. AC Q5F9E4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Pilus assembly protein PilW {ECO:0000313|EMBL:AAW89193.1}; GN ORFNames=NGO_0454 {ECO:0000313|EMBL:AAW89193.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89193.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89193.1; -; Genomic_DNA. DR RefSeq; WP_010951046.1; NC_002946.2. DR RefSeq; YP_207605.1; NC_002946.2. DR EnsemblBacteria; AAW89193; AAW89193; NGO_0454. DR GeneID; 3282990; -. DR KEGG; ngo:NGO0454; -. DR PATRIC; 20333940; VBINeiGon24812_0544. DR HOGENOM; HOG000218895; -. DR KO; K02672; -. DR OMA; GGNVCAN; -. DR OrthoDB; EOG6DC6G8; -. DR BioCyc; NGON242231:GI2G-431-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 43 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 326 AA; 35949 MW; E89851293E4574EF CRC64; MKRKMLNVPK GGYDGMKGFT IVEFLVAGLL SIIVLIAVVS SYFTSRKLND VANERLAIQQ DLRNAATLIV RDARMAGSFG CFNMSEHTKD DIVDSSNQTQ SNLAKPGAKQ ENPLFSLKRS GMDKQLIPVA ESIDIKYPGF IQRLNALVFQ YGIDDLDASA ETVVVSSCSK IAKPGKKIST LQEAKSALQI TNDDKQNGNI TRQKHVVNAY AVGRFGNNEE SLFRFQLDDK GKWGNPQLLV KKVKRMDVRY IYVSGCPEDE DAGKEEKFRY TNKFDKSKNA VTPAGVEVLL DSGLNAKIAA SSDNSIYAYR INATIRGGNV CANRTL // ID Q5F607_NEIG1 Unreviewed; 111 AA. AC Q5F607; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90380.1}; GN ORFNames=NGO_1759 {ECO:0000313|EMBL:AAW90380.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90380.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90380.1; -; Genomic_DNA. DR RefSeq; WP_003690361.1; NC_002946.2. DR RefSeq; YP_208792.1; NC_002946.2. DR EnsemblBacteria; AAW90380; AAW90380; NGO_1759. DR GeneID; 3281092; -. DR KEGG; ngo:NGO1759; -. DR PATRIC; 20337132; VBINeiGon24812_2106. DR HOGENOM; HOG000027898; -. DR OMA; IMGFWGS; -. DR OrthoDB; EOG6P338J; -. DR BioCyc; NGON242231:GI2G-1655-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 111 AA; 12337 MW; 6DC5D010A16CD053 CRC64; MPSEALSGVQ TAFCFPTVYK LSLFLDRNND LIYLKRLEDM IMGFWGSVGK AAKAVGEGLI EAGNQHKALK MEYAEKSSEE LHEIVKSDGF FKNSTREKGA AYAVLKERGE V // ID Q5F9S7_NEIG1 Unreviewed; 149 AA. AC Q5F9S7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 67. DE SubName: Full=PTS sugar transporter subunit IIA {ECO:0000313|EMBL:AAW89060.1}; GN ORFNames=NGO_0313 {ECO:0000313|EMBL:AAW89060.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89060.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89060.1; -; Genomic_DNA. DR RefSeq; WP_003687701.1; NC_002946.2. DR RefSeq; YP_207472.1; NC_002946.2. DR ProteinModelPortal; Q5F9S7; -. DR SMR; Q5F9S7; 2-147. DR EnsemblBacteria; AAW89060; AAW89060; NGO_0313. DR GeneID; 3281731; -. DR KEGG; ngo:NGO0313; -. DR PATRIC; 20333607; VBINeiGon24812_0383. DR HOGENOM; HOG000227559; -. DR KO; K02806; -. DR OMA; QSETTFE; -. DR OrthoDB; EOG6XDGX2; -. DR BioCyc; NGON242231:GI2G-293-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sugar transport {ECO:0000313|EMBL:AAW89060.1}; KW Transport {ECO:0000313|EMBL:AAW89060.1}. FT DOMAIN 6 149 PTS EIIA type-2. FT {ECO:0000259|PROSITE:PS51094}. SQ SEQUENCE 149 AA; 16064 MW; 10E6BA626E33083D CRC64; MSLIGEILPL SHIVLDMEVG SKKRLFEEAG LLLERESSLS HADVFECLFA REKLGSTGLG QGVAIPHGRH ASVKQATGAF IRTREPVGFD APDGKPVSLV FILLVPENAT GEHLEVLSKL AGKFSQKSIR ESLMTVASAE EARAILTEE // ID Q5F9Y5_NEIG1 Unreviewed; 290 AA. AC Q5F9Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 70. 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 ORFNames=NGO_0249 {ECO:0000313|EMBL:AAW89002.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89002.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89002.1; -; Genomic_DNA. DR RefSeq; WP_003706663.1; NC_002946.2. DR RefSeq; YP_207414.1; NC_002946.2. DR ProteinModelPortal; Q5F9Y5; -. DR SMR; Q5F9Y5; 27-281. DR EnsemblBacteria; AAW89002; AAW89002; NGO_0249. DR GeneID; 3281537; -. DR KEGG; ngo:NGO0249; -. DR PATRIC; 20333453; VBINeiGon24812_0307. DR HOGENOM; HOG000021670; -. DR KO; K01963; -. DR OMA; PEGLWIK; -. DR OrthoDB; EOG6HQSSF; -. DR BioCyc; NGON242231:GI2G-234-MONOMER; -. DR UniPathway; UPA00655; UER00711. DR Proteomes; UP000000535; 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: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:UP000000535}; 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}; 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:UP000000535}; 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; 31775 MW; 4568948F19BACD6D CRC64; MSWLDKILPP KIKNRGKDGA SNVPEGLWRK CPSCSATVYS TELQQNNQVC PKCNHHNPLS ARQRLNLLLD EEGREEVAGN VKPTDPLKFK DSKKYPDRLS AARKLTGEDD ALVVMKGMMN GLPVVVAAFE FRFIGGSMGS VVGERFVQGV RRAVADNCPF VCVAASGGAR MQEGVNSLMQ MTKTSAALHL LTEKRLPFIS VLTDPTMGGV SASFAFLGDV VLAEPNALIG FAGPRVIEQT VRETLPEGFQ RAEFLLEKGA IDQIVDRRDM KRRISDLITL LCRQDKVSAT // ID Q5FA82_NEIG1 Unreviewed; 361 AA. AC Q5FA82; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 58. DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AAW88905.1}; GN ORFNames=NGO_0147 {ECO:0000313|EMBL:AAW88905.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88905.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88905.1; -; Genomic_DNA. DR ProteinModelPortal; Q5FA82; -. DR EnsemblBacteria; AAW88905; AAW88905; NGO_0147. DR PATRIC; 20333213; VBINeiGon24812_0189. DR HOGENOM; HOG000286057; -. DR OMA; NTFRTYV; -. DR OrthoDB; EOG6X10T3; -. DR BioCyc; NGON242231:GI2G-135-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR006905; Trp_halogenase. DR Pfam; PF04820; Trp_halogenase; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 361 AA; 40503 MW; 9C04D9E912EDB282 CRC64; MEMLEEAGFA DAVRTGPGFQ LKNGAAFSWG SRYTEFDFTD KFSDGPGTVY QVRRAVFDKI LIEEAAKQGV EVRFGHGVTA FDNSGDFARL NIETDTGESY ELTAKFVLDA SGYGRVLPRL LNLETPSHLP PRQTHFTHID DNITHPKFDR NKILITTHPQ HRDVWIWLIP FGDNRCSVGV VGTPDKLAGE SETVLKKFVY ECPMLSEILD KAVWENDFPF RSIQGYSANV KSLHGRHFAL LGNAAEFLDP VFSSGVTIAL HSAELAADLL TKQLKGEAAD WQTEFAEPLM IGVDAFRTYV DGWYDFRFQN VVYAPDRSPE ISRMLSSILA GYAWDTENPF VAKSEQRLTA LSEWVGQLES E // ID Q5FAE5_NEIG1 Unreviewed; 278 AA. AC Q5FAE5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 60. DE SubName: Full=Phosphoesterase {ECO:0000313|EMBL:AAW88842.1}; GN ORFNames=NGO_0081 {ECO:0000313|EMBL:AAW88842.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88842.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88842.1; -; Genomic_DNA. DR RefSeq; WP_003687335.1; NC_002946.2. DR RefSeq; YP_207254.1; NC_002946.2. DR ProteinModelPortal; Q5FAE5; -. DR EnsemblBacteria; AAW88842; AAW88842; NGO_0081. DR GeneID; 3282263; -. DR KEGG; ngo:NGO0081; -. DR PATRIC; 20333049; VBINeiGon24812_0108. DR HOGENOM; HOG000248104; -. DR KO; K07053; -. DR OMA; TRAHYAR; -. DR OrthoDB; EOG6KMB5P; -. DR BioCyc; NGON242231:GI2G-71-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00467137}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 67 POLIIIAc. {ECO:0000259|SMART:SM00481}. SQ SEQUENCE 278 AA; 30084 MW; 7EF563B733FA8E22 CRC64; MIDLHCHSTV SDGMLPPAEV VRLAHQNGCT LLALTDHDHT GGISEARAEA DRLGLRLING VEISVTWRGR TIHVVGLDFD EQDENLQNLL ADVRKGRLKR LEAIAAKLEK KGIGGAYDGA LALAANKEMV SRTHVAEFLI KNGHVKNKQQ AFTKYLGDGK SCAVRHEWAT LADCVSAVNG AGGMAVIAHP MRYDLSATAK RNLFEEFKNL GGAGIEVHSG NCCKNDRLNY ALLADRFGLL ASAGSDFHRL DDFSGGILGA CPDLPENCKP VRAHFSRH // ID Q5F5Z5_NEIG1 Unreviewed; 461 AA. AC Q5F5Z5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Serine dehydratase {ECO:0000313|EMBL:AAW90392.1}; GN ORFNames=NGO_1773 {ECO:0000313|EMBL:AAW90392.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90392.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90392.1; -; Genomic_DNA. DR RefSeq; WP_003697660.1; NC_002946.2. DR RefSeq; YP_208804.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z5; -. DR EnsemblBacteria; AAW90392; AAW90392; NGO_1773. DR GeneID; 3281143; -. DR KEGG; ngo:NGO1773; -. DR PATRIC; 20337178; VBINeiGon24812_2129. DR HOGENOM; HOG000036732; -. DR KO; K01752; -. DR OMA; LENELTW; -. DR OrthoDB; EOG64V2GZ; -. DR BioCyc; NGON242231:GI2G-1667-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 150 SDH_beta. {ECO:0000259|Pfam:PF03315}. FT DOMAIN 180 444 SDH_alpha. {ECO:0000259|Pfam:PF03313}. SQ SEQUENCE 461 AA; 49186 MW; CF4ACCAEB5509754 CRC64; MISIFDIFKI GIGPSSSHTV GPMKAAAAFA AGLDAQTARI AIDIYGSLAL TGYGHGTFDA LMLGLEGSLP HDIPLAGIPE RLGRIRTQHI LRLNGQEIRF IPDRDLNIRG NQVLPKHPNG LRFTAYASDG TVLKEQVYYS VGGGFVVTEE DFEWQSETEK AVPYPYNSCA GLLARCRLNR LDISEVVLAN EAALAGCGEA EIRRRVAGVA EIMEECIKRG LNAGGELPGG LNVRRRAPQL AAKLKVLRET EIVNTRLWPM VYAMAVNEEN AAGGRVVTAP TNGAAGIIPA VLHYFRKFNP HATQERVENF LLTAGAIGIL YKTNASISGA DVGCQGEVGV ACSMAAGAYA EVIGGTPKQV ENAAEMAMEH HLGLTCDPVG GLVQIPCIER NGIAAEKALK LGTLALLEDG TDKKVSLDEV IRTMLQTGRD MKATYKETSL AGLAATLRKK AVPVSVRVVE C // ID Q5F597_NEIG1 Unreviewed; 596 AA. AC Q5F597; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 58. DE SubName: Full=Recombinase RmuC {ECO:0000313|EMBL:AAW90640.1}; GN ORFNames=NGO_2032 {ECO:0000313|EMBL:AAW90640.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90640.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90640.1; -; Genomic_DNA. DR RefSeq; WP_010356003.1; NC_002946.2. DR RefSeq; YP_209052.1; NC_002946.2. DR ProteinModelPortal; Q5F597; -. DR EnsemblBacteria; AAW90640; AAW90640; NGO_2032. DR GeneID; 3282715; -. DR KEGG; ngo:NGO2032; -. DR PATRIC; 20337847; VBINeiGon24812_2447. DR HOGENOM; HOG000270056; -. DR KO; K09760; -. DR OMA; VANLWRI; -. DR OrthoDB; EOG6T4S02; -. DR BioCyc; NGON242231:GI2G-1933-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR003798; DNA_recombination_RmuC. DR Pfam; PF02646; RmuC; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 53 87 {ECO:0000256|SAM:Coils}. FT COILED 172 216 {ECO:0000256|SAM:Coils}. FT COILED 287 321 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 596 AA; 66974 MW; 0A45F2590F4E50F6 CRC64; MELMTVLLPL AALVSGVLFT WLLMKGRFQG EFAGLNAQLA EKAARCDFIE QAHAEIASEL AALDGKYEHL QDENYALSNR FSAAEKQIAH LQEKEAESVR LKQSYIDLQE KAQGLAVENE RLATQLGQER KAFAEQYALE RQIRQRVETD LEESRQTVRD VQNDLSDVGN RFAAAEKQIA YLQEKEAEAE RLRQSHTELQ EKAQGLAVEN ERLATQIEQE RLASEEKLSL LGEARKSLSD QFQNLANTIL EEKSRRFTEQ NREQLHQVLN PLNERIHGFG ELVRQTYDKE SRERLTLENE LKRLQGLNAQ LHSEAKALTN ALTGTQNKVQ GNWGEMILET VLENSGLQKG REYVVQAASV RKEEDGGTRR LQPDVLVNLP DNKQIVIDSK VSLTAYVRYT QAADADEAAR ELAAYIASIR AHMKGLSLKD YTDLEGVNTL DFVFMFIPVE PAYLLALQND AGLFQECFDK RIMLVGPSTL LATLRTVANI WRNEQQNQNA LAIADEGGKL YDKFVGFVQT LESVGKGIDQ AQNSFQTAFK QLAEGRGNLV GRAEKLRLLG VKAGKQLQRD LVERANEQTA FALGKPSEQE AADEAE // ID Q5F5B5_NEIG1 Unreviewed; 284 AA. AC Q5F5B5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 67. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW90622.1}; GN ORFNames=NGO_2014 {ECO:0000313|EMBL:AAW90622.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90622.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:2YJP} RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 18-284 IN COMPLEX WITH ZINC. RX PubMed=22138345; DOI=10.1016/j.jmb.2011.11.030; RA Bulut H., Moniot S., Licht A., Scheffel F., Gathmann S., Saenger W., RA Schneider E.; RT "Crystal structures of two solute receptors for L-cystine and L- RT cysteine, respectively, of the human pathogen Neisseria gonorrhoeae."; RL J. Mol. Biol. 415:560-572(2012). 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; AE004969; AAW90622.1; -; Genomic_DNA. DR RefSeq; WP_003704691.1; NC_002946.2. DR RefSeq; YP_209034.1; NC_002946.2. DR PDB; 2YJP; X-ray; 2.26 A; A/B/C=18-284. DR PDBsum; 2YJP; -. DR ProteinModelPortal; Q5F5B5; -. DR SMR; Q5F5B5; 40-284. DR EnsemblBacteria; AAW90622; AAW90622; NGO_2014. DR GeneID; 3282698; -. DR KEGG; ngo:NGO2014; -. DR PATRIC; 20337809; VBINeiGon24812_2428. DR HOGENOM; HOG000031895; -. DR KO; K02030; -. DR OMA; NIELRDW; -. DR OrthoDB; EOG6JQH58; -. DR BioCyc; NGON242231:GI2G-1915-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2YJP}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Metal-binding {ECO:0000213|PDB:2YJP}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000213|PDB:2YJP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 284 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256570. FT DOMAIN 49 271 PBPb. {ECO:0000259|SMART:SM00062}. FT METAL 98 98 Zinc. {ECO:0000213|PDB:2YJP}. FT METAL 185 185 Zinc. {ECO:0000213|PDB:2YJP}. SQ SEQUENCE 284 AA; 30201 MW; 11306129F05E3C90 CRC64; MKLNAKLKAL LASAAIAVGL TACGGGSGDA QSSQSSGAAT VAAIKEKGVI RIGVFGDKPP FGYVDANGKN QGFDVEIAKD LAKDLLGSPD KVEFVLTEAA NRVEYVRSGK VDLILANFTQ TPERAEAVDF ADPYMKVALG VVSPKNKPIT DMAQLKDQTL LVNKGTTADA FFTKSHPEVK LLKFDQNTET FDALKDGRGV ALAHDNALLW AWAKENPNFE VAIGNLGPAE FIAPAVQKGN ADLLNWVNGE IAAMKKDGRL KAAYEKTLLP VYGEKVKPEA LLAE // ID Q5F9S0_NEIG1 Unreviewed; 122 AA. AC Q5F9S0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89067.2}; GN ORFNames=NGO_0320 {ECO:0000313|EMBL:AAW89067.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89067.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89067.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89067; AAW89067; NGO_0320. DR PATRIC; 20333627; VBINeiGon24812_0391. DR HOGENOM; HOG000261620; -. DR OMA; TAINLHK; -. DR OrthoDB; EOG6DNTDC; -. DR BioCyc; NGON242231:GI2G-302-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010376; DUF971. DR Pfam; PF06155; DUF971; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 91 DUF971. {ECO:0000259|Pfam:PF06155}. SQ SEQUENCE 122 AA; 13650 MW; B91E9A850775C5C3 CRC64; MNNIPVEIRL LKNRAVLVLT YGDEPKNLPA EFLRVYSPSA EVRGHGVGQD VLQTGKADVQ ITDLQPVGQY ALKISFSDGH DSGLYDWAYL HRLAYGYDAM WQEYLDKLAA AGASRFEKQS DC // ID Q5F6S6_NEIG1 Unreviewed; 127 AA. AC Q5F6S6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90111.1}; GN ORFNames=NGO_1471 {ECO:0000313|EMBL:AAW90111.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90111.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90111.1; -; Genomic_DNA. DR RefSeq; WP_003689346.1; NC_002946.2. DR RefSeq; YP_208523.1; NC_002946.2. DR ProteinModelPortal; Q5F6S6; -. DR EnsemblBacteria; AAW90111; AAW90111; NGO_1471. DR GeneID; 3281645; -. DR KEGG; ngo:NGO1471; -. DR PATRIC; 20336375; VBINeiGon24812_1736. DR HOGENOM; HOG000168796; -. DR OMA; NHFEAFP; -. DR OrthoDB; EOG6DRPJH; -. DR BioCyc; NGON242231:GI2G-1376-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256046. FT TRANSMEM 84 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 126 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 127 AA; 13464 MW; 5F6508FF7516D40C CRC64; MTFAYWCILI ACLLPLFCAA YAKKAGGFRF KDNHNPRGFL AHTQGAAARA HAAQQNGFEA FAPFAAAVLT AHATGNAGQA TVNTLAGLFI LFRLAFIWCY IADKAALRSL MWAGGFACTV GLFVAAA // ID Q5F6G9_NEIG1 Unreviewed; 132 AA. AC Q5F6G9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90218.1}; GN ORFNames=NGO_1590 {ECO:0000313|EMBL:AAW90218.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90218.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90218.1; -; Genomic_DNA. DR RefSeq; WP_003691611.1; NC_002946.2. DR RefSeq; YP_208630.1; NC_002946.2. DR EnsemblBacteria; AAW90218; AAW90218; NGO_1590. DR GeneID; 3281100; -. DR KEGG; ngo:NGO1590; -. DR PATRIC; 20336706; VBINeiGon24812_1899. DR HOGENOM; HOG000219105; -. DR OMA; DYSEWND; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NGON242231:GI2G-1486-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 132 AA; 16357 MW; 0AA7785396F7D3E2 CRC64; MCEFKDFRRN IPCFEEYDEN SFIGKWYDDG VWDDEEYWKL ENALIEVRKK YPYPMDIPRD IVIGIGTIID FLMVQNWKLF EIKASPWLPK SVKINERYER FRVMLRYIFT DLDAEDWKFF YFPIQHSKGR LR // ID Q5F8B0_NEIG1 Unreviewed; 160 AA. AC Q5F8B0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=GNAT family acetyltransferase {ECO:0000313|EMBL:AAW89577.1}; GN ORFNames=NGO_0876 {ECO:0000313|EMBL:AAW89577.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89577.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89577.1; -; Genomic_DNA. DR RefSeq; WP_003688513.1; NC_002946.2. DR RefSeq; YP_207989.1; NC_002946.2. DR ProteinModelPortal; Q5F8B0; -. DR EnsemblBacteria; AAW89577; AAW89577; NGO_0876. DR GeneID; 3282150; -. DR KEGG; ngo:NGO0876; -. DR PATRIC; 20334925; VBINeiGon24812_1032. DR HOGENOM; HOG000218926; -. DR OMA; PAKESDR; -. DR OrthoDB; EOG65XN44; -. DR BioCyc; NGON242231:GI2G-819-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89577.1}. FT DOMAIN 5 160 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 160 AA; 18165 MW; 92A4F000C2AA44C3 CRC64; MSLLTLLRPA TVQDCKDIFK VHLHSVQYTC ILSYNEHALK VWEGLLNTES YLPTISDPDK ALWVAEYKGN IQGFFQIDCQ EAQLDALYVH PLFHNLGLGT ALLRQAETIA HKSGLSFLKL YASLNSVPFY LLNRYESLGS AVLQLDPSIK IKCELMRKHL // ID Q5F7Y8_NEIG1 Unreviewed; 594 AA. AC Q5F7Y8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 57. DE SubName: Full=Integrase core domain protein {ECO:0000313|EMBL:AAW89699.2}; GN ORFNames=NGO_1020 {ECO:0000313|EMBL:AAW89699.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89699.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89699.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7Y8; -. DR EnsemblBacteria; AAW89699; AAW89699; NGO_1020. DR PATRIC; 20335244; VBINeiGon24812_1190. DR HOGENOM; HOG000218098; -. DR OMA; LHPNHVW; -. DR OrthoDB; EOG60SCG2; -. DR BioCyc; NGON242231:GI2G-942-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR001584; Integrase_cat-core. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00665; rve; 1. DR SUPFAM; SSF53098; SSF53098; 2. DR PROSITE; PS50994; INTEGRASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 145 347 Integrase catalytic. FT {ECO:0000259|PROSITE:PS50994}. SQ SEQUENCE 594 AA; 66698 MW; 26CFEAFC71F605A1 CRC64; MIERLKAVEN QAEAMGRGAR SAYLKQQAQE LGISLATLYR KLEAVSVKPT RKRRSDAGKT ELKPEEAKLI SAVLAEAMRR NGKRLMPVRQ AVEMLRANGK IEAARIDGET GEVIPLSENT ITRALREYKL HSDQLLQPDP VSRMKSEHPN HCWQIDPSLC VLYCLPRQGK DTGLRVMKEE EFYKNKPKNV VKIENDRVWR YTGTDHASGT ISVRYYFGGE TSANLCDFFI YMMQAKKDIG KDPFRTVPRM VMLDPGSANT SAAFKNLCKP LDVHVQINKP GNPRAKGQVE KANDIVETAF ESGLRFTEVH DIDQLNALSE RWMRYYNGTQ KHSRHGMTRY QAWNKIKPEQ LILPPPAEYC RELAVSAPKE AKVSADLEIR FGGRVYSVKG IKGILVGKKV LVGKKVLVGK NPWEANGARV ATYDAEGNEV WVSVPEVVFD EMGFKADAAV IGAEYKAPAD TDAQRHRKEL DKLAMGAETL EAAAAKRKGK AVPFGGKIDP YKHQEDTLAA SNTLFMPKQG QQMDYNKMEV AEQVLSKVEI AKRLKPRVEA DGGDWKQAVS VILKHYPEGV TEGRLEEAFE RTRTRCRLKL LKTG // ID Q5F7V7_NEIG1 Unreviewed; 261 AA. AC Q5F7V7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Fimb protein {ECO:0000313|EMBL:AAW89730.1}; GN ORFNames=NGO_1060 {ECO:0000313|EMBL:AAW89730.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89730.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89730.1; -; Genomic_DNA. DR RefSeq; WP_003688173.1; NC_002946.2. DR RefSeq; YP_208142.1; NC_002946.2. DR EnsemblBacteria; AAW89730; AAW89730; NGO_1060. DR GeneID; 3281970; -. DR KEGG; ngo:NGO1060; -. DR PATRIC; 20335354; VBINeiGon24812_1243. DR HOGENOM; HOG000219018; -. DR OMA; YPYREIS; -. DR OrthoDB; EOG6Q8J3F; -. DR BioCyc; NGON242231:GI2G-975-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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}. SQ SEQUENCE 261 AA; 29150 MW; 4ACDFD7F53E8D2BE CRC64; MMENGKTFPR WRFALKSAGW HLLISLLVAG LAALLVFKVW YPYPYAELTG GLSLYQLVVA VDIVCGPLLT LILASPKKKT KARMVDFSMV GIIQLAALAY GLHSVSLARP VVEAFEQDRM TIVTAAEVVV EDLHKAPEGL QSLSWFGIRR IALKEPEDAD EKNKTLDLSL KGIEPSMRPD RWLPYSDKEA EKIRKHLKPL KVLADARKTT VADILKQAGL AEGEELYYLP FTSSRQKEWI VITDKEGNTK GYAPIDGFII P // ID Q5F920_NEIG1 Unreviewed; 248 AA. AC Q5F920; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase {ECO:0000313|EMBL:AAW89317.1}; GN ORFNames=NGO_0586 {ECO:0000313|EMBL:AAW89317.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89317.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89317.1; -; Genomic_DNA. DR RefSeq; WP_002213318.1; NC_002946.2. DR RefSeq; YP_207729.1; NC_002946.2. DR EnsemblBacteria; AAW89317; AAW89317; NGO_0586. DR GeneID; 3282297; -. DR KEGG; ngo:NGO0586; -. DR PATRIC; 20334244; VBINeiGon24812_0694. DR HOGENOM; HOG000229370; -. DR KO; K17103; -. DR OMA; SGPIQYL; -. DR OrthoDB; EOG65XN45; -. DR BioCyc; NGON242231:GI2G-557-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003750, KW ECO:0000313|EMBL:AAW89317.1}; 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 Q5F5X1_NEIG1 Unreviewed; 265 AA. AC Q5F5X1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 64. DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|RuleBase:RU003938}; DE EC=2.7.7.41 {ECO:0000256|RuleBase:RU003938}; GN ORFNames=NGO_1798 {ECO:0000313|EMBL:AAW90416.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90416.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90416.1; -; Genomic_DNA. DR RefSeq; WP_003690029.1; NC_002946.2. DR RefSeq; YP_208828.1; NC_002946.2. DR EnsemblBacteria; AAW90416; AAW90416; NGO_1798. DR GeneID; 3282424; -. DR KEGG; ngo:NGO1798; -. DR PATRIC; 20337246; VBINeiGon24812_2158. DR HOGENOM; HOG000006168; -. DR KO; K00981; -. DR OMA; WEWGRLN; -. DR OrthoDB; EOG6TBHJT; -. DR BioCyc; NGON242231:GI2G-1696-MONOMER; -. DR UniPathway; UPA00557; UER00614. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003938, KW ECO:0000313|EMBL:AAW90416.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003938, KW ECO:0000313|EMBL:AAW90416.1}; 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; 29146 MW; FF6008E49D947F74 CRC64; MLKQRVITAM WLLPLMLGML FYAPQWLWAA FCGLIALTAL WEYARMAGLC KTETNHYLAA TLVFGVVAYA GGWMLPNLVW YVVLAFWLAV MPLWLRFKWR LNGGWQVYAV GWLLLMPFWF ALVSLRPHPD DALPLLAVMG LVWVADVCAY FSGKALGKHK IAPAISPGKS WEGAIGGAVC VAVYMTAVRS AGWLAFDTGW FDTVLIGLVL TVVSVCGDLL ESWLKRAAGI KDSSNLLPGH GGVFDRTDSL IAVISVYAAI MSVLN // ID Q5F6H6_NEIG1 Unreviewed; 65 AA. AC Q5F6H6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90211.1}; GN ORFNames=NGO_1582 {ECO:0000313|EMBL:AAW90211.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90211.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90211.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90211; AAW90211; NGO_1582. DR PATRIC; 20336692; VBINeiGon24812_1892. DR HOGENOM; HOG000027891; -. DR OMA; IMSVADT; -. DR OrthoDB; EOG6PCQ60; -. DR BioCyc; NGON242231:GI2G-1479-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7069 MW; 56B217DFA4DC7B9A CRC64; MSVADTVLLP PVELPFRDMA DASFLLNRIR IPPNLTECKT AAGNGLYDTS TTGCCGRIII FFHPS // ID Q5F7I4_NEIG1 Unreviewed; 230 AA. AC Q5F7I4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Murein hydrolase transporter LrgB {ECO:0000313|EMBL:AAW89853.1}; GN ORFNames=NGO_1193 {ECO:0000313|EMBL:AAW89853.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89853.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89853.1; -; Genomic_DNA. DR RefSeq; WP_003692267.1; NC_002946.2. DR RefSeq; YP_208265.1; NC_002946.2. DR EnsemblBacteria; AAW89853; AAW89853; NGO_1193. DR GeneID; 3282031; -. DR KEGG; ngo:NGO1193; -. DR PATRIC; 20335683; VBINeiGon24812_1400. DR HOGENOM; HOG000253604; -. DR OMA; QMHQIRA; -. DR OrthoDB; EOG6NPMDR; -. DR BioCyc; NGON242231:GI2G-1105-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR InterPro; IPR007300; CidB/LrgB. DR Pfam; PF04172; LrgB; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89853.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 38 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 91 113 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; 24555 MW; BC113B279D0D0A8B CRC64; MSEILRQPSV LLFLTLAVYA LAIIVRTRTG NIFCNPVLVS TIVLIAYLKI LGIDYAVYHN AAQFIDFRLK PAVVVLAVPL YQNRRKIFNQ WLPVIVSQLA GSVTGIVTGM YFAKWLGAER EVVLPLASKS VTNPIAIEIT RSIGGIPAIT AATVIIAGLV GQIAGYKMLK NTVVMPSSVG MSLGTASHAM GIAASLERSR RMAAYAGMGL TFNGVLTALI APLLIPVLGF // ID Q5F5N6_NEIG1 Unreviewed; 183 AA. AC Q5F5N6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90501.1}; GN ORFNames=NGO_1880 {ECO:0000313|EMBL:AAW90501.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90501.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90501.1; -; Genomic_DNA. DR RefSeq; WP_003690145.1; NC_002946.2. DR RefSeq; YP_208913.1; NC_002946.2. DR EnsemblBacteria; AAW90501; AAW90501; NGO_1880. DR GeneID; 3282356; -. DR KEGG; ngo:NGO1880; -. DR PATRIC; 20337458; VBINeiGon24812_2260. DR HOGENOM; HOG000218675; -. DR OMA; RPDIAFN; -. DR OrthoDB; EOG6HQSPF; -. DR BioCyc; NGON242231:GI2G-1785-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 66 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 121 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 183 AA; 19500 MW; 865E519E46F8E5AB CRC64; MKVLNGWSDR KMWRVLSALP IGVVFFDLIY GFVLNVLQGL DLQRAVPDSE GVLAVTPDIA FNSLQIVANG GMAAVVCFGL AVVFLLNRSV RRRQVLEIGV FRMLGLVAVL AFSAPSLWEW ANALPLLLKG ADVVNTGNAR YVLTALCMPF PAVSCIIGLV GRFRLQTASG RVAKAGGAVK AGG // ID Q5F883_NEIG1 Unreviewed; 484 AA. AC Q5F883; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 77. DE SubName: Full=(Fe-S)-binding protein {ECO:0000313|EMBL:AAW89604.1}; GN ORFNames=NGO_0906 {ECO:0000313|EMBL:AAW89604.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89604.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89604.1; -; Genomic_DNA. DR RefSeq; WP_003688412.1; NC_002946.2. DR RefSeq; YP_208016.1; NC_002946.2. DR ProteinModelPortal; Q5F883; -. DR EnsemblBacteria; AAW89604; AAW89604; NGO_0906. DR GeneID; 3281363; -. DR KEGG; ngo:NGO0906; -. DR PATRIC; 20334993; VBINeiGon24812_1066. DR HOGENOM; HOG000262102; -. DR KO; K18929; -. DR OMA; HCPVYDK; -. DR OrthoDB; EOG6JTC5N; -. DR BioCyc; NGON242231:GI2G-846-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 53921 MW; A661DBAE86366558 CRC64; MTTQTIKFHM KPETFKQNAA ISLQDKPLRK SLRTAMDMLM TKRKAVLTDE EELQSLRDLC EHIRQRSLSK LPALLEQLEE NLTKLGVKVH WAETPAEACQ IIHDIITAKN GKLMVKGKSM VSEEIELNHY LEAKGIKAVE SDLGEFIVQM AGEKPTHIVM PAIHKTKEQV SELFHQNLGT PLTDDVDQLT GFARKALRDI YSTADVGLSG VNFAVAETGT LCLVENEGNG RLSTTVPPVH IVITGIEKVV AKLSDVPPLY SLLPRSAIGQ NITTYFNMIT GPRRSEELDG PQEMHLVLLD NGRSQAYAED QMRRTLQCIR CGACMNHCPV YTRIGGAAYG TTYPGPIGEI ISPHLLGLDA TRDLPTACTM CGACVEVCPV RIPITEQMQR LRVEAQRSPT ETVPHPIRGQ GASHTFGEQM AWRTFNGIFS GSKTYRAFGW AATKFRNLTP RKQLGWTQNR VPMKPAKKTL HELMAEKMRQ KEQA // ID Q5F6D0_NEIG1 Unreviewed; 272 AA. AC Q5F6D0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90257.1}; GN ORFNames=NGO_1629 {ECO:0000313|EMBL:AAW90257.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90257.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90257.1; -; Genomic_DNA. DR RefSeq; WP_003705996.1; NC_002946.2. DR RefSeq; YP_208669.1; NC_002946.2. DR EnsemblBacteria; AAW90257; AAW90257; NGO_1629. DR GeneID; 3281373; -. DR KEGG; ngo:NGO1629; -. DR PATRIC; 20336794; VBINeiGon24812_1942. DR HOGENOM; HOG000071320; -. DR OMA; EHCDSWV; -. DR OrthoDB; EOG6FZ4FC; -. DR BioCyc; NGON242231:GI2G-1526-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR021398; DUF3037. DR Pfam; PF11236; DUF3037; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 272 AA; 31295 MW; 64D9F0323342F630 CRC64; MNRYAMRFAV IRFMPYVQTR EFANIGIIIT HPQSGCFDFK IEHRYSRLSR FFRRFDPPAY KAATRAFEKE LQRIRNLAAH SAPDQIRAMP DHLTRPREAL IMAAQPGVTL APDRGQELNR LFDYFVARSF AKNQPEAELT RQIQAMLKPL QTAYPFKEST IGDPSGFHAS IPLVQKAENG EIRKIIKPIY FGRKDPADIY YKSDKRIAGI KRLRRGGYID RSEILFAYEP PERPDKAQEK ALLDVSGDLE EQGIQLADNR SEGKIIRNFA CG // ID Q5F8Z7_NEIG1 Unreviewed; 103 AA. AC Q5F8Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Stress response protein {ECO:0000313|EMBL:AAW89340.1}; GN ORFNames=NGO_0613 {ECO:0000313|EMBL:AAW89340.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89340.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89340.1; -; Genomic_DNA. DR RefSeq; WP_003688925.1; NC_002946.2. DR RefSeq; YP_207752.1; NC_002946.2. DR EnsemblBacteria; AAW89340; AAW89340; NGO_0613. DR GeneID; 3281192; -. DR KEGG; ngo:NGO0613; -. DR PATRIC; 20334306; VBINeiGon24812_0725. DR HOGENOM; HOG000218989; -. DR OrthoDB; EOG6CP3ZJ; -. DR BioCyc; NGON242231:GI2G-580-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 103 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256239. SQ SEQUENCE 103 AA; 11848 MW; 91C7E00664BC677F CRC64; MLAILLSAIL GLVSTTAAAG TSEPAHRHTK HISKANKQML HPECRKYLER RAAWYRSQGN VQELRENKKA RKAFRTLPYA EQKIQCRAAY EAFDDFDGGR FRR // ID Q5F5M9_NEIG1 Unreviewed; 93 AA. AC Q5F5M9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90508.1}; GN ORFNames=NGO_1891 {ECO:0000313|EMBL:AAW90508.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90508.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90508.1; -; Genomic_DNA. DR RefSeq; WP_003690158.1; NC_002946.2. DR RefSeq; YP_208920.1; NC_002946.2. DR EnsemblBacteria; AAW90508; AAW90508; NGO_1891. DR GeneID; 3282295; -. DR KEGG; ngo:NGO1891; -. DR PATRIC; 20337486; VBINeiGon24812_2274. DR OrthoDB; EOG6V7BW4; -. DR BioCyc; NGON242231:GI2G-1792-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 93 AA; 10396 MW; 432CEA30B07DB68F CRC64; MKQIKASDFT DEHFGLPTIL DILSELEKPQ PRTDSRPQTT TQRACPNQFG DGGCVCEVEA VSPTAGMYSD RCSGGFCPRF FCYFKYVYSH DAV // ID Q5F8Y7_NEIG1 Unreviewed; 39 AA. AC Q5F8Y7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89350.1}; GN ORFNames=NGO_0622 {ECO:0000313|EMBL:AAW89350.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89350.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89350.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89350; AAW89350; NGO_0622. DR PATRIC; 20334328; VBINeiGon24812_0736. DR OrthoDB; EOG693GZG; -. DR BioCyc; NGON242231:GI2G-590-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 39 AA; 4563 MW; FD94D7B0BBECDC1E CRC64; MSIFHPYFQQ LSTEGFDGEE DVLWEDELTV KGNLVEVFL // ID Q5FA92_NEIG1 Unreviewed; 49 AA. AC Q5FA92; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88895.1}; GN ORFNames=NGO_0137 {ECO:0000313|EMBL:AAW88895.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88895.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88895.1; -; Genomic_DNA. DR RefSeq; WP_003690597.1; NC_002946.2. DR RefSeq; YP_207307.1; NC_002946.2. DR EnsemblBacteria; AAW88895; AAW88895; NGO_0137. DR GeneID; 3282110; -. DR KEGG; ngo:NGO0137; -. DR PATRIC; 20333185; VBINeiGon24812_0175. DR HOGENOM; HOG000027883; -. DR OrthoDB; EOG6GTZQ9; -. DR BioCyc; NGON242231:GI2G-125-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5367 MW; 1747CF9B8B2C6859 CRC64; MGGYLSASGL GFVGKMGGNI FCRKKYLFKI NQLIFVKCPL IGIDGHFII // ID Q5F9P3_NEIG1 Unreviewed; 71 AA. AC Q5F9P3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89094.1}; GN ORFNames=NGO_0350 {ECO:0000313|EMBL:AAW89094.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89094.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89094.1; -; Genomic_DNA. DR RefSeq; WP_003690799.1; NC_002946.2. DR RefSeq; YP_207506.1; NC_002946.2. DR EnsemblBacteria; AAW89094; AAW89094; NGO_0350. DR GeneID; 3281211; -. DR KEGG; ngo:NGO0350; -. DR PATRIC; 20333697; VBINeiGon24812_0426. DR HOGENOM; HOG000137695; -. DR KO; K09712; -. DR OMA; MFLSRAP; -. DR OrthoDB; EOG622PTX; -. DR BioCyc; NGON242231:GI2G-329-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR005590; DUF333. DR Pfam; PF03891; DUF333; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 7990 MW; 38ACB64557598A4B CRC64; MKAIHPYACP RCCRLPANTF RTGMANSASK FCIAKGGRRE VKKDESGGGY ALCHLPDSRI VEEWEYCRSQ H // ID Q5F7P2_NEIG1 Unreviewed; 163 AA. AC Q5F7P2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89795.1}; GN ORFNames=NGO_1128 {ECO:0000313|EMBL:AAW89795.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89795.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89795.1; -; Genomic_DNA. DR RefSeq; WP_010951194.1; NC_002946.2. DR RefSeq; YP_208207.1; NC_002946.2. DR EnsemblBacteria; AAW89795; AAW89795; NGO_1128. DR GeneID; 3281905; -. DR KEGG; ngo:NGO1128; -. DR PATRIC; 20335514; VBINeiGon24812_1323. DR HOGENOM; HOG000071216; -. DR OrthoDB; EOG66HVG5; -. DR BioCyc; NGON242231:GI2G-1040-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008840; Sipho_Gp157. DR Pfam; PF05565; Sipho_Gp157; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 163 AA; 18218 MW; 36B80760ED851596 CRC64; MTALTLYRCA ADVQAGLDYY FDSETEREDT LEAVIGQFEV KAQSVIAYIK NQEITEKMLE GHIRQMTGKL KAAKARNQSL KDYLARNMQA AGITEIKADD GTFKASFRKS EAVVILDEAQ IPAEFMREAV KTEPDKTAIR KAIESGRQVA GAKIEGRKNL QIR // ID Q5FAB8_NEIG1 Unreviewed; 161 AA. AC Q5FAB8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 60. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW88869.1}; GN ORFNames=NGO_0108 {ECO:0000313|EMBL:AAW88869.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88869.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88869.1; -; Genomic_DNA. DR ProteinModelPortal; Q5FAB8; -. DR EnsemblBacteria; AAW88869; AAW88869; NGO_0108. DR PATRIC; 20333115; VBINeiGon24812_0141. DR HOGENOM; HOG000263119; -. DR OMA; HEKMDES; -. DR OrthoDB; EOG6XHC2W; -. DR BioCyc; NGON242231:GI2G-98-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 126 FMN_red. {ECO:0000259|Pfam:PF03358}. SQ SEQUENCE 161 AA; 17861 MW; 7A86090DE1A275E1 CRC64; MFPEGWQAEI VEIGHLPLYN FDYDDPEVED VPLPESYTAF RETIKASDGI LFVTSENNRT IPACLKNAVD IGSKPNADVA WKNKPAGIIS HSVGKMGGYS SQKNLRLALS YFDMPVTGQP EVFLGNSPTL FDENGKLIDS ARDFVQSYIN QFVGLIERNA K // ID Q5F7Y6_NEIG1 Unreviewed; 163 AA. AC Q5F7Y6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89701.2}; GN ORFNames=NGO_1025 {ECO:0000313|EMBL:AAW89701.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89701.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89701.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89701; AAW89701; NGO_1025. DR PATRIC; 20335264; VBINeiGon24812_1198. DR HOGENOM; HOG000277953; -. DR OMA; DDYYKQG; -. DR OrthoDB; EOG6NKR09; -. DR BioCyc; NGON242231:GI2G-946-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008620; FixH. DR Pfam; PF05751; FixH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5005364414. SQ SEQUENCE 163 AA; 18100 MW; 16A34BBC1BAD7B00 CRC64; MAGPIFVVIA SVAMFFVAQQ HATDLVTDDY YKDGKHIDIQ LHRDEEAVRR HIGVQVLISP DMNAAKVFVG GEFDGKQPLN LLLMHPTRKA DDQTVALKPV GSAQNGRAEY EAVFKTLPPA NHWYVRVEDA AGVWRVENKW ITSQGNAVDL TPMDKLFNNA GSK // ID Q5FA88_NEIG1 Unreviewed; 48 AA. AC Q5FA88; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88899.1}; GN ORFNames=NGO_0141 {ECO:0000313|EMBL:AAW88899.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88899.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88899.1; -; Genomic_DNA. DR RefSeq; WP_003692597.1; NC_002946.2. DR RefSeq; YP_207311.1; NC_002946.2. DR EnsemblBacteria; AAW88899; AAW88899; NGO_0141. DR GeneID; 3281965; -. DR KEGG; ngo:NGO0141; -. DR PATRIC; 20333193; VBINeiGon24812_0179. DR OrthoDB; EOG6T7NFG; -. DR BioCyc; NGON242231:GI2G-129-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5500 MW; 1D916F002FC42EE1 CRC64; MPRCGISEFS GYGGGFSFYW ERFLQARRNF LKSIKTYANN CKILISAA // ID Q5FA34_NEIG1 Unreviewed; 794 AA. AC Q5FA34; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|PIRNR:PIRNR000854}; DE Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854}; DE EC=2.7.9.2 {ECO:0000256|PIRNR:PIRNR000854}; DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|PIRNR:PIRNR000854}; GN ORFNames=NGO_0200 {ECO:0000313|EMBL:AAW88953.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88953.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to CC phosphoenolpyruvate. {ECO:0000256|PIRNR:PIRNR000854}. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + H(2)O = AMP + CC phosphoenolpyruvate + phosphate. {ECO:0000256|PIRNR:PIRNR000854}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR000854}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|PIRNR:PIRNR000854}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000256|PIRNR:PIRNR000854}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88953.1; -; Genomic_DNA. DR RefSeq; WP_010951009.1; NC_002946.2. DR RefSeq; YP_207365.1; NC_002946.2. DR ProteinModelPortal; Q5FA34; -. DR SMR; Q5FA34; 4-792. DR PRIDE; Q5FA34; -. DR EnsemblBacteria; AAW88953; AAW88953; NGO_0200. DR GeneID; 3281742; -. DR KEGG; ngo:NGO0200; -. DR PATRIC; 20333331; VBINeiGon24812_0248. DR HOGENOM; HOG000230913; -. DR KO; K01007; -. DR OMA; DELHTAC; -. DR OrthoDB; EOG632CZ4; -. DR BioCyc; NGON242231:GI2G-183-MONOMER; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000854}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|PIRNR:PIRNR000854}; KW Magnesium {ECO:0000256|PIRNR:PIRNR000854}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR000854}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000854}; KW Pyruvate {ECO:0000313|EMBL:AAW88953.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR000854}. FT DOMAIN 18 346 PPDK_N. {ECO:0000259|Pfam:PF01326}. FT DOMAIN 387 458 PEP-utilizers. FT {ECO:0000259|Pfam:PF00391}. FT DOMAIN 483 787 PEP-utilizers_C. FT {ECO:0000259|Pfam:PF02896}. SQ SEQUENCE 794 AA; 87236 MW; 3B5E764A5DC9834F CRC64; MADNYVIWFE NLRMTDVERV GGKNASLGEM ISQLTEKGVR VPGGFATTAD AYRAFLAHNG LNERISAALA KLDVEDVSEL ARVGKEIRQW ILDTPFPEQL DAEIEAAWNK MITDADGADI SVAVRSSATA EDLPDASFAG QQETFLNING LDNVKKAMRH VFASLYNDRA ISYRVHKGFE HDIVALSAGV QRMVRSDSGA SGVMFTLDTE SGYNQVVFVT SSYGLGENVV QGAVNPDEFY VFKPTLKAGK PAILRKTMGS KHIKMIFTDK AEAGKSVTNV EVPEEDRNRF SITDEEITEL AHYALTIEKH YGRPMDIEWG RDGLDGKLYI LQARPETVKS QEEGSRNLRR YAINGEKTVL CEGRAIGQKV GQGKVRLIKD ASEMDSVEAG DVLVTDMTDP DWEPVMKRAS AIVTNRGGRT CHAAIIAREL GIPAVVGCGN ATELLENGQE VTVSCAEGDT GFIYAGLLDV QITDVALDNM PKAPVKVMMN VGNPELAFSF ANLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDDELKA EIIRRIAGYA SPVDFYVDKI AEGVATLAAS VYPRKTIVRM SDFKSNEYAN LVGGSVYEPH EENPMLGFRG AARYVAESFK DCFALECKAL KRVRDEMGLT NVEIMIPFVR TLGEAEAVVK ALKENGLERG KNGLRLIMMC ELPSNAVLAE QFLQYFDGFS IGSNDMTQLT LGLDRDSGLV SESFDERNPA VKVMLHLAIS ACRKQNKYVG ICGQGPSDHP DFAKWLVGEG IESVSLNPDT VIETWLYLAN ELNK // ID Q5F6S7_NEIG1 Unreviewed; 512 AA. AC Q5F6S7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 68. 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:AAW90110.1}; GN ORFNames=NGO_1470 {ECO:0000313|EMBL:AAW90110.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90110.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90110.1; -; Genomic_DNA. DR RefSeq; WP_010951278.1; NC_002946.2. DR RefSeq; YP_208522.1; NC_002946.2. DR ProteinModelPortal; Q5F6S7; -. DR SMR; Q5F6S7; 2-376. DR EnsemblBacteria; AAW90110; AAW90110; NGO_1470. DR GeneID; 3281654; -. DR KEGG; ngo:NGO1470; -. DR PATRIC; 20336373; VBINeiGon24812_1735. DR HOGENOM; HOG000022121; -. DR KO; K00324; -. DR OMA; AGNNFGR; -. DR OrthoDB; EOG61P6S9; -. DR BioCyc; NGON242231:GI2G-1375-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW90110.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 425 444 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 456 473 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 479 501 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 137 AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}. FT DOMAIN 146 311 AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}. SQ SEQUENCE 512 AA; 53776 MW; 08217415E4AC4F75 CRC64; MKIGIPRESL SGETRVACTP ATVALLGKLG FETVVESGAG LAASLDDAAY QTAGATVADK AAVWACPLIY KVNAPSEGEL PLLKEGQTIV SFLWPRQNEA LVEALRAKKV NALAMDMVPR ISRAQALDAL SSMANISGYR AVIEAANAFG RFFTGQITAA GKVPPAQVLV IGAGVAGLAA IGTANSLGAV VRAFDTRLEV AEQIESMGGK FLKLDFLQES GGSGDGYAKV MSDEFIAAEM KLFAEQAKEV DIIITTAAIP GKPAPKLITK EMVESMKSGS VIVDLAATGG NCELTRPGEL SVTGNGVKII GYTDMANRLA GQSSQLYATN LVNLTKLLSP NKDGEITLDF EDVIIRNMTV TRDGEITFPP PPIQVSARPQ QTPSEKAAPA AKPEPKPVPL WKKLAPAAIA AVLVLWVRAV APAAFLNHFI VFVLACVIGY HVVWNVSHSL HTPLMSVTNA ISGIIVVGAL LQIGQGNGFV SLLSFVAILI AGINIFGGFA VTRRMLNMFK KG // ID Q5F8H2_NEIG1 Unreviewed; 791 AA. AC Q5F8H2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 79. 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 ORFNames=NGO_0801 {ECO:0000313|EMBL:AAW89515.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89515.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89515.1; -; Genomic_DNA. DR RefSeq; WP_003695198.1; NC_002946.2. DR RefSeq; YP_207927.1; NC_002946.2. DR ProteinModelPortal; Q5F8H2; -. DR EnsemblBacteria; AAW89515; AAW89515; NGO_0801. DR GeneID; 3282029; -. DR KEGG; ngo:NGO0801; -. DR PATRIC; 20334752; VBINeiGon24812_0948. DR HOGENOM; HOG000071120; -. DR KO; K12573; -. DR OMA; YRVHEGP; -. DR OrthoDB; EOG6Q5NRD; -. DR BioCyc; NGON242231:GI2G-755-MONOMER; -. DR Proteomes; UP000000535; 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; 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; 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:UP000000535}; 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:UP000000535}; 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; 89053 MW; B33ED9F2480D8A5A CRC64; MNKNIKSLNL REKDPFLSRE KQRYEHPLPS REWIIELLER KGVPSKIESL ARELSITEDE YVFFERRLKA MARDGQVLIN RRGAVCAADK LDLVKCRVEA HKDGFGFAVP LMPMDEGDFV LYERQMRGVM HGDTVTVRPA GIDRRGRREG TVLDIVERAQ SKVVGRFYMD RGVAILEPED KRLNQSIVLE PDGVARFKPE SGQVIVGKIE VYPEQNRPAV AKIIEVLGDY ADSGMEIEIA VRKHHLPHRF SEACAKSAKK IPDHVRKSDL KGRVDLCDLP LVTIDGETAR DFDDAVFAEK VGRNYRLVVA IADVSHYVRP DDAIDADAQE RSTSVYFPRR MIPMLPENLS NGICSLNPDV ERLCMVCDMV VTYAGNIKEY RFYPAVMRSH ARLTYNQVWK WLSDGIGNPH KAQIDTLYKL FKILQKKRLA RGAVEFESVE TQMIFDDNGK IEKIVPVVRN DAHKLIEECM LAANVCAADF LLKNKHTALF RNHLGPTPEK LATLREQLGL LGLQLGGGDN PSPKDYAALA EQFKGRPDAE LLQVMMLRSM QQAVYEPHCE GHFGLAYEAY AHFTSPIRRY PDLTVHRAIK AVLNRKTYTP NKSWQALGVH TSFCERRADD AGRDVENWLK TYYMRDKVGE IFEGKISGVA NFGIFVTLDD IHIDGLVHIS DLGEDYFNFR PEIMAIEGER SGIRFNMGDR VAVRVARADL DDGKIDFVLI AGESGRRRKV KLSASAKPAG AAGKGKSKTT AEKKTARCGK VRGRGVPAVA ESGKKAKKPV PIKVKKRKGK S // ID Q5F9G3_NEIG1 Unreviewed; 180 AA. AC Q5F9G3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89174.1}; GN ORFNames=NGO_0432 {ECO:0000313|EMBL:AAW89174.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89174.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89174.1; -; Genomic_DNA. DR RefSeq; WP_003690884.1; NC_002946.2. DR RefSeq; YP_207586.1; NC_002946.2. DR EnsemblBacteria; AAW89174; AAW89174; NGO_0432. DR GeneID; 3281996; -. DR KEGG; ngo:NGO0432; -. DR PATRIC; 20333879; VBINeiGon24812_0517. DR OrthoDB; EOG6SNDQS; -. DR BioCyc; NGON242231:GI2G-409-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 180 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256247. SQ SEQUENCE 180 AA; 20046 MW; 042D3EEC7215C6E2 CRC64; MKRIFLPALP AILPLSAYAD LPLTIEDIMT DKGKWKLETS LTYLNSENSR AALAAPVYIQ TGATSFIPIP TEIQENGSNT DMLAGTLGLR YGLTGNTDIY GSGSYLWHEE RKLDGNGKTR NKRMSDISAG ISHTFLKDGK NPALISFLES TVYEKSRNKA SLIKKRGLCP FYNLRINYEY // ID Q5F5F0_NEIG1 Unreviewed; 196 AA. AC Q5F5F0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AAW90587.1}; GN ORFNames=NGO_1978 {ECO:0000313|EMBL:AAW90587.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90587.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90587.1; -; Genomic_DNA. DR RefSeq; WP_003699277.1; NC_002946.2. DR RefSeq; YP_208999.1; NC_002946.2. DR ProteinModelPortal; Q5F5F0; -. DR EnsemblBacteria; AAW90587; AAW90587; NGO_1978. DR GeneID; 3282645; -. DR KEGG; ngo:NGO1978; -. DR PATRIC; 20337723; VBINeiGon24812_2388. DR HOGENOM; HOG000078520; -. DR OMA; LWKLWYT; -. DR OrthoDB; EOG64FKJW; -. DR BioCyc; NGON242231:GI2G-1877-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90587.1}. FT DOMAIN 15 176 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 196 AA; 22046 MW; A2F06B8D2428A9E0 CRC64; MSERIILPVL SLGGVRFEPL DVHHETGLRE AVCDGEVWKL GVTSAPHPDR VADYIGTALA TRLAFAVVDE EADRVVGTTA YYHFEPQIPR LDIGFTWYAA SARRKRINTC CKIMLLDYAF DVLVCCCAGW RTDILNLASQ RAIERLGAEK DGVLRMHMLR KDGSVRDTVV YSMLREDWCK NREILTGRLA GYGVQV // ID Q5F8U9_NEIG1 Unreviewed; 310 AA. AC Q5F8U9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89388.1}; GN ORFNames=NGO_0661 {ECO:0000313|EMBL:AAW89388.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89388.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89388.1; -; Genomic_DNA. DR RefSeq; WP_003695394.1; NC_002946.2. DR RefSeq; YP_207800.1; NC_002946.2. DR EnsemblBacteria; AAW89388; AAW89388; NGO_0661. DR GeneID; 3281139; -. DR KEGG; ngo:NGO0661; -. DR PATRIC; 20334418; VBINeiGon24812_0781. DR HOGENOM; HOG000218998; -. DR KO; K09824; -. DR OMA; PLHIERK; -. DR OrthoDB; EOG6TBHCV; -. DR BioCyc; NGON242231:GI2G-628-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007488; DUF535. DR Pfam; PF04393; DUF535; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 310 AA; 36214 MW; 5BE1C69DE5EE30D6 CRC64; MKQNRTFTFP DFRTVYSYAP LYRLQHLKYT LRKFFGKKEI YAFEQFVNAS PIRQGLFLHC PQDAYPLLRE FVDRRFNCKR RLDAMTADFL MAEKLFGTDV LCQMEDCRFH LVLAHLSDGI SLWLNRNDNC VEEGAWSLSL RDEAGNRLYM ATFAFVGTHL LTASVQGPSG EEAKDTVRRI TKQLHGLRPQ QLMVTALQYF AAALKLDGAI GIAQKHQVKL RWKLKKRVKM NYDAFWQEYG ASLERDGYWH LPQTPARKDL ADIESKKRSM YRKRYEMLDD MVAKMKDSLK TEARGISDGI QTEKPLRRTV // ID Q5F6J2_NEIG1 Unreviewed; 93 AA. AC Q5F6J2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE SubName: Full=ArsR family transcriptional regulator {ECO:0000313|EMBL:AAW90195.1}; GN ORFNames=NGO_1562 {ECO:0000313|EMBL:AAW90195.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90195.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90195.1; -; Genomic_DNA. DR RefSeq; WP_003689479.1; NC_002946.2. DR RefSeq; YP_208607.1; NC_002946.2. DR ProteinModelPortal; Q5F6J2; -. DR EnsemblBacteria; AAW90195; AAW90195; NGO_1562. DR GeneID; 3281458; -. DR KEGG; ngo:NGO1562; -. DR PATRIC; 20336632; VBINeiGon24812_1862. DR HOGENOM; HOG000144506; -. DR OMA; DIFCATA; -. DR OrthoDB; EOG679TGC; -. DR BioCyc; NGON242231:GI2G-1463-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000711}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 10577 MW; E067ACF0680AC8ED CRC64; MNTIPLHTIL KLMAHPERMA ILIQLLDSER NIVELAKSLS LTATAVSCHL NRLRAGGLVD FTRYHRIIEY RLVSEDAATI LRTIRDLENK RAA // ID Q5F870_NEIG1 Unreviewed; 587 AA. AC Q5F870; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000256|RuleBase:RU362051}; DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051}; GN ORFNames=NGO_0921 {ECO:0000313|EMBL:AAW89617.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89617.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89617.1; -; Genomic_DNA. DR RefSeq; WP_003688397.1; NC_002946.2. DR RefSeq; YP_208029.1; NC_002946.2. DR ProteinModelPortal; Q5F870; -. DR SMR; Q5F870; 1-587. DR PRIDE; Q5F870; -. DR EnsemblBacteria; AAW89617; AAW89617; NGO_0921. DR GeneID; 3281104; -. DR KEGG; ngo:NGO0921; -. DR PATRIC; 20335025; VBINeiGon24812_1082. DR HOGENOM; HOG000160475; -. DR KO; K00239; -. DR OMA; PSVYEIG; -. DR OrthoDB; EOG6M3PC4; -. DR BioCyc; NGON242231:GI2G-859-MONOMER; -. DR UniPathway; UPA00223; UER01005. DR Proteomes; UP000000535; 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:UP000000535}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 64449 MW; FDADB2AC5F7FE6E3 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 QGDEYEVPVK GLYAAGECAC ASVHGANRLG TNSLLDLVVF GKAAGDSMIK FIKEQSDWKP LPANAGELTR QRIERLDSQT DGENVDALRR ELQRSVQLHA GVFRTDEILS KGVQEIMAIA ERVKRTEIKD KSKVWNTARI EALELDNLIE VAKATLVSAE ARKESRGAHA SDDHPERDDE NWMKHTLYHS DTNTLSYKPV HTKPLSVEYI KPAKRVY // ID Q5F9P1_NEIG1 Unreviewed; 38 AA. AC Q5F9P1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89096.1}; GN ORFNames=NGO_0352 {ECO:0000313|EMBL:AAW89096.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89096.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89096.1; -; Genomic_DNA. DR RefSeq; WP_010357306.1; NC_002946.2. DR RefSeq; YP_207508.1; NC_002946.2. DR EnsemblBacteria; AAW89096; AAW89096; NGO_0352. DR GeneID; 3281226; -. DR KEGG; ngo:NGO0352; -. DR PATRIC; 20333701; VBINeiGon24812_0428. DR HOGENOM; HOG000027902; -. DR OrthoDB; EOG6TBHPH; -. DR BioCyc; NGON242231:GI2G-331-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 38 AA; 4411 MW; E6402EBC40D68D06 CRC64; MDSAMPSERV SDGIFFSGKL KKSIMTRLKI TLEHRDER // ID Q5F896_NEIG1 Unreviewed; 93 AA. AC Q5F896; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89591.1}; GN ORFNames=NGO_0892 {ECO:0000313|EMBL:AAW89591.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89591.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89591.1; -; Genomic_DNA. DR RefSeq; WP_010951145.1; NC_002946.2. DR RefSeq; YP_208003.1; NC_002946.2. DR EnsemblBacteria; AAW89591; AAW89591; NGO_0892. DR GeneID; 3281145; -. DR KEGG; ngo:NGO0892; -. DR PATRIC; 20334957; VBINeiGon24812_1048. DR HOGENOM; HOG000027915; -. DR OMA; VKEMPSE; -. DR OrthoDB; EOG65QWNC; -. DR BioCyc; NGON242231:GI2G-833-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 93 AA; 10312 MW; 50C96E238A0B8A60 CRC64; MMRYGKVKEM PSERLSDGIG AIRERRNIEA PAFQIGRRTK PPALAHRSGL LASAPDPVFR FAMRGDPQRR NGIITGFLKN STVLIRSYAG NTA // ID Q5F621_NEIG1 Unreviewed; 753 AA. AC Q5F621; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525}; DE EC=1.6.5.11 {ECO:0000256|RuleBase:RU003525}; GN ORFNames=NGO_1745 {ECO:0000313|EMBL:AAW90366.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90366.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90366.1; -; Genomic_DNA. DR RefSeq; WP_003705265.1; NC_002946.2. DR RefSeq; YP_208778.1; NC_002946.2. DR ProteinModelPortal; Q5F621; -. DR DNASU; 3281216; -. DR EnsemblBacteria; AAW90366; AAW90366; NGO_1745. DR GeneID; 3281216; -. DR KEGG; ngo:NGO1745; -. DR PATRIC; 20337088; VBINeiGon24812_2084. DR HOGENOM; HOG000031442; -. DR KO; K00336; -. DR OMA; SAYEHES; -. DR OrthoDB; EOG6CVV7G; -. DR BioCyc; NGON242231:GI2G-1641-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 81392 MW; B83D6B3EA49AABE4 CRC64; MLQIEIDGKQ VSVEQGATVI EAAHKLGTYI PHFCYHKKLS IAANCRMCLV DVEKAPKPLP ACATPVTDGM IVRTHSAKAR EAQEGVMEFL LINHPLDCPT CDQGGECQLQ DLAVGYGKTT SRYTEEKRSV VGKDMGPLVS AEEMSRCIHC TRCVRFTEEI AGLQEIAMVN RGEHSEIMPF IGKAVETELS GNVIDLCPVG ALTSKPFRFN ARTWELNRRK SVSAHDALGS NLIVQTKDHT VRRVLPLENE AINECWLSDR DRFAYEGLYH ESRLKNPKIK QGGEWMDVDW KTALEYVRSA IECIAKDGNQ NQVGVWANPM NTVEELYLAK KFADGLGVKN FATRLRQQDK RLSDGLKGAQ WLGQSIESLA DNDAVLVVGA NLRKEQPLLT ARLRRAAKDR MALSVLAGSK EELFMPLLSQ EAAHPDEWAG RLKNLSADAE HAVTASLKNA EKAAVILGAE VQNHPDYAAI YAAAQELADA TGAVLGILPQ AANSVGADVL GVNSGESVAE MANTPKQAVL LLNVEPEIDT VDGAKAVAAL KQAKSVMAFT PFVSETLLDV CDVLLPIAPF TETSGSFINM EGRLQSFHGV VQGFGDSRPM WKVLRVLGNL FDLKGFEYHD TAAILKDALD AESLPSKLDN RSTWAGEGVQ TASNRLVRVG GVGIYHTDSI VRRSAPLQET SHAAVPAARV NPNTLARLGL QDGQTAVAKQ NGASVSVAVK ADAGLPENVV HLPLHTENAA LGALMGIIEL AGA // ID Q5F5L9_NEIG1 Unreviewed; 138 AA. AC Q5F5L9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. 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 ORFNames=NGO_1904 {ECO:0000313|EMBL:AAW90518.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90518.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90518.1; -; Genomic_DNA. DR RefSeq; WP_003692108.1; NC_002946.2. DR RefSeq; YP_208930.1; NC_002946.2. DR ProteinModelPortal; Q5F5L9; -. DR PRIDE; Q5F5L9; -. DR EnsemblBacteria; AAW90518; AAW90518; NGO_1904. DR GeneID; 3282281; -. DR KEGG; ngo:NGO1904; -. DR PATRIC; 20337528; VBINeiGon24812_2291. DR HOGENOM; HOG000178408; -. DR KO; K06204; -. DR OMA; AQERHEK; -. DR OrthoDB; EOG6JDWD6; -. DR BioCyc; NGON242231:GI2G-1807-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00926}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 15963 MW; 36E5EFD46EC871F2 CRC64; MVKLTEQDIL NWIGPEDDYM NDDHLAFFRE LLVKMQDELI ENASVTTGHL QEHESAPDPA DRATQEEEYA LELRTRDRER KLLSKIQATI RNIDEGDYGF CADTGEPIGL KRLLARPTAT LSVEAQERRE RMKKQFAD // ID Q5F7A4_NEIG1 Unreviewed; 392 AA. AC Q5F7A4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:AAW89933.1}; GN ORFNames=NGO_1276 {ECO:0000313|EMBL:AAW89933.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89933.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89933.1; -; Genomic_DNA. DR RefSeq; WP_003705926.1; NC_002946.2. DR RefSeq; YP_208345.1; NC_002946.2. DR ProteinModelPortal; Q5F7A4; -. DR SMR; Q5F7A4; 53-354. DR EnsemblBacteria; AAW89933; AAW89933; NGO_1276. DR GeneID; 3282097; -. DR KEGG; ngo:NGO1276; -. DR PATRIC; 20335885; VBINeiGon24812_1497. DR HOGENOM; HOG000217143; -. DR KO; K00368; -. DR OMA; MPISEGV; -. DR BioCyc; NGON242231:GI2G-1191-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:InterPro. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.420; -; 2. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR001287; NO2-reductase_Cu. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; SSF49503; 2. DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 392 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255506. FT DOMAIN 87 198 Plastocyanin-like. FT {ECO:0000259|Pfam:PF07732}. FT DOMAIN 206 338 Plastocyanin-like. FT {ECO:0000259|Pfam:PF00394}. SQ SEQUENCE 392 AA; 40934 MW; 0B8F6634CD46C625 CRC64; MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGAI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN VQSTIVPAGG SAIVEFKVDI PGNYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD TAYAGSGAAS APAASAPAAS APAASASEKS VY // ID Q5F7C5_NEIG1 Unreviewed; 381 AA. AC Q5F7C5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 60. DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574}; GN ORFNames=NGO_1253 {ECO:0000313|EMBL:AAW89912.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89912.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89912.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7C5; -. DR EnsemblBacteria; AAW89912; AAW89912; NGO_1253. DR PATRIC; 20335839; VBINeiGon24812_1474. DR HOGENOM; HOG000263815; -. DR OMA; VEYYIPK; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NGON242231:GI2G-1170-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Periplasm {ECO:0000256|PIRNR:PIRNR019574}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|PIRNR:PIRNR019574}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 381 Putrescine-binding periplasmic protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364417. SQ SEQUENCE 381 AA; 42544 MW; 2F47C6952C4A1F43 CRC64; MQGMIMVKHL PLAVLTALLL AACGGSDKPP AEKPAPAENQ NVLKIYNWSE YVDPETVADF EKKNGIKVTY DVYDSDETLE SKVLTGKSGY DIVAPSNAFV GRQIKAGAYQ KIDKSMIPNY KHLNPEMMRL MDGVDPDHEY AVPFYWGTNT FAINTERVKK ALGTDKLPDN QWDLVFNPEY TFKLKQCGIS YLDSAAEIYP MVLNYLGKNP NSSNTEDIRE ATALLKKNRP NIKRFTSSGF IDDLARGDTC VTIGFGGDLN IAKRRAEEAG GKEKIRVMMP KEGVGIWVDS FVIPKDAKNV ANAHKYINDF LDPEVSAKNG NFVTYAPSSK PARDLMEDEF KNDNTIFPSG EDLKNSFIMV PIRPAALKFM VRQWQDVKAG K // ID Q5F6J3_NEIG1 Unreviewed; 256 AA. AC Q5F6J3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AAW90194.1}; GN ORFNames=NGO_1561 {ECO:0000313|EMBL:AAW90194.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90194.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90194.1; -; Genomic_DNA. DR RefSeq; WP_010951295.1; NC_002946.2. DR RefSeq; YP_208606.1; NC_002946.2. DR ProteinModelPortal; Q5F6J3; -. DR SMR; Q5F6J3; 1-255. DR EnsemblBacteria; AAW90194; AAW90194; NGO_1561. DR GeneID; 3281442; -. DR KEGG; ngo:NGO1561; -. DR PATRIC; 20336630; VBINeiGon24812_1861. DR HOGENOM; HOG000034587; -. DR KO; K01142; -. DR OMA; CTSCEVD; -. DR OrthoDB; EOG60SCPF; -. DR BioCyc; NGON242231:GI2G-1462-MONOMER; -. DR Proteomes; UP000000535; 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: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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 247 Endo/exonuclease/phosphatase. FT {ECO:0000259|Pfam:PF03372}. SQ SEQUENCE 256 AA; 29182 MW; A429D55983968B3F CRC64; MKITTWNVNS LNVRLPQVQN LLVDNPPDIL VLQELKLDQD KFPAAALQMM GWHCVWSGQK TYNGVAIVSR SVPQDVHFGL PSLPDDPQRR VIAATVGGVR VINVYCVNGE ALDSPKFKYK EQWFAALTEF VRDEMSRHGK LVLLGDFNIA PADADCYDPE KWYEKIHCSS VERQWFQNLL DLGLTDSLRQ VHPEGAFYTW FDYRGAMFQR KLGLRIDHIL VTSEMAAVLK DVRIDLETRA LERPSDHAPV AAEFDL // ID Q5F821_NEIG1 Unreviewed; 270 AA. AC Q5F821; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 58. DE SubName: Full=Phytoene synthase {ECO:0000313|EMBL:AAW89666.2}; GN ORFNames=NGO_0980 {ECO:0000313|EMBL:AAW89666.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89666.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89666.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F821; -. DR DNASU; 3282869; -. DR EnsemblBacteria; AAW89666; AAW89666; NGO_0980. DR PATRIC; 20335160; VBINeiGon24812_1149. DR HOGENOM; HOG000003801; -. DR OMA; YAYCRIS; -. DR OrthoDB; EOG63FW00; -. DR BioCyc; NGON242231:GI2G-908-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 270 AA; 30263 MW; 26C838A009992692 CRC64; MSVGHYENFP VGSLILPRRL RKPVHAVYAF ARTADDMADE GSMPSEARLS GLEGLRRELD VLASGGRSAH PLIARLDAEA VVPFGLDLQP FYDLLSAFSQ DVVKTRYAHF GDLTDYCRRS ANPVGRIMLA LYGKTDAVCV AQSDGICTAL QLVNFWQDVA VDWQKGRVYI PQDDLLKFGV SEEQIAAGRA DAAFQRLMAY ECRRAFRMLK AGSPLARELK GRIGLELRMI VLGAQLILQK LDACRYDVFA QRPVLDKKDW LIMLKRALWK // ID Q5F8U6_NEIG1 Unreviewed; 217 AA. AC Q5F8U6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=UPF0056 inner membrane protein {ECO:0000256|RuleBase:RU362048}; GN ORFNames=NGO_0664 {ECO:0000313|EMBL:AAW89391.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89391.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89391.1; -; Genomic_DNA. DR RefSeq; WP_003688829.1; NC_002946.2. DR RefSeq; YP_207803.1; NC_002946.2. DR EnsemblBacteria; AAW89391; AAW89391; NGO_0664. DR GeneID; 3282063; -. DR KEGG; ngo:NGO0664; -. DR PATRIC; 20334424; VBINeiGon24812_0784. DR HOGENOM; HOG000112971; -. DR OMA; AIILWTS; -. DR OrthoDB; EOG6KWZ3Q; -. DR BioCyc; NGON242231:GI2G-631-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU362048}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 64 Helical. {ECO:0000256|RuleBase:RU362048}. FT TRANSMEM 70 91 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; 5C9B9830F74D0C18 CRC64; MGLGMEIGKL IVAFLVLINP FSALSLYLDL TNGHSTKERR KVARTAAVAV FAVIAVFALI GGALLKVLGI SVGSFQVGGG ILVLLIAISM MNGNDNPAKQ NLGAQPETGQ ARPARNAGAI AVVPIAIPIT IGPGGISTVI IYASAAKTYS DIALIIAAGL VVSAICYAIL IVAGKVSRLL GATGLTILNR IMGMMLAAVS VEIIVSGLKT IFPQLAG // ID Q5F7X1_NEIG1 Unreviewed; 181 AA. AC Q5F7X1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89716.1}; GN ORFNames=NGO_1044 {ECO:0000313|EMBL:AAW89716.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89716.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89716.1; -; Genomic_DNA. DR RefSeq; WP_003690987.1; NC_002946.2. DR RefSeq; YP_208128.1; NC_002946.2. DR EnsemblBacteria; AAW89716; AAW89716; NGO_1044. DR GeneID; 3282565; -. DR KEGG; ngo:NGO1044; -. DR PATRIC; 20335312; VBINeiGon24812_1222. DR HOGENOM; HOG000071265; -. DR OMA; SENMAEQ; -. DR OrthoDB; EOG6K4016; -. DR BioCyc; NGON242231:GI2G-961-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 181 AA; 19358 MW; EC2E60839ECB2151 CRC64; MLKIPFAVLG GCLLLAACGK SENTAEQPQN AAQSAPKPVF KVKYIDNTAI AGLALGQSSE GKTNDGKKQI SYPIKGLPEQ NAVRLTGKHP NDLEAVVGKC METDGKDAPS GWAENGVCHT LFAKLVGNIA EDGGKLTDYL ISHSALQPYQ AGKSGYAAVQ NGRYVLEIDS EGAFYFRRRH Y // ID Q5F6B1_NEIG1 Unreviewed; 179 AA. AC Q5F6B1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90276.1}; GN ORFNames=NGO_1649 {ECO:0000313|EMBL:AAW90276.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90276.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90276.1; -; Genomic_DNA. DR RefSeq; WP_010951317.1; NC_002946.2. DR RefSeq; YP_208688.1; NC_002946.2. DR DNASU; 3281332; -. DR EnsemblBacteria; AAW90276; AAW90276; NGO_1649. DR GeneID; 3281332; -. DR KEGG; ngo:NGO1649; -. DR PATRIC; 20336838; VBINeiGon24812_1964. DR HOGENOM; HOG000148526; -. DR OMA; MTELPWI; -. DR OrthoDB; EOG66TG4K; -. DR BioCyc; NGON242231:GI2G-1545-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR013423; CHP02594. DR TIGRFAMs; TIGR02594; TIGR02594; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 179 AA; 19310 MW; 385C2078393B8B83 CRC64; MTELPWIAEA RRHIGLKEIP GAKHNPTIVQ WLKETGGFPG AAKSWYFEDE TPWCGLFVGY CLGKSGRAVI RDWYRAKAWS MSGLTKLEAP AYGCIAVKPR RGGGHVFFVV GKDAEGRILG LGGNQGNMVS IIPFDPADID GYFWPSKLIG GKAVPSSPAE GRYRLSDVAA TAKQGAGEA // ID Q5F9X1_NEIG1 Unreviewed; 346 AA. AC Q5F9X1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 51. DE SubName: Full=Cell division protein FtsN {ECO:0000313|EMBL:AAW89016.1}; GN ORFNames=NGO_0265 {ECO:0000313|EMBL:AAW89016.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89016.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89016.1; -; Genomic_DNA. DR RefSeq; WP_003690743.1; NC_002946.2. DR RefSeq; YP_207428.1; NC_002946.2. DR EnsemblBacteria; AAW89016; AAW89016; NGO_0265. DR GeneID; 3281561; -. DR KEGG; ngo:NGO0265; -. DR PATRIC; 20333499; VBINeiGon24812_0330. DR HOGENOM; HOG000218843; -. DR OMA; NTKSDET; -. DR OrthoDB; EOG6ZPSZ5; -. DR BioCyc; NGON242231:GI2G-248-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. 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 Cell cycle {ECO:0000313|EMBL:AAW89016.1}; KW Cell division {ECO:0000313|EMBL:AAW89016.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 42 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 268 346 SPOR. {ECO:0000259|PROSITE:PS51724}. SQ SEQUENCE 346 AA; 37006 MW; F412F457FFF57D00 CRC64; MSENKQNEVL TGYEQLKRRN RRRLVTASSL VAASCILLAA ALSSDPADSN PAPQAGETGA TESQTANTAQ TPALKSAAEN GETAADKPQD LAGEDKPSAA DSEISEPENV GAPLVLINDR LEDSNIKGLE ESEKLQQAET AKTEPKQAKQ RAAEKVSATA DSTDTVAVEK PKRTAEPKPQ KAERTAEAKP KAKETKTAEK VADKPKTAAE KTKPDTAKSD SAVKEAKKAD KAEGKKTAEK DRSDGKKHET AQKTDKADKT KTAEKEKSGK AGKKAAIQAG YAEKERALSL QRKMKAAGID STITEIMTDN GKVYRVKSSN YKNARDAERD LNKLRVHGIA GQVTNE // ID Q5F699_NEIG1 Unreviewed; 104 AA. AC Q5F699; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90288.1}; GN ORFNames=NGO_1663 {ECO:0000313|EMBL:AAW90288.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90288.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90288.1; -; Genomic_DNA. DR RefSeq; WP_010359134.1; NC_002946.2. DR RefSeq; YP_208700.1; NC_002946.2. DR EnsemblBacteria; AAW90288; AAW90288; NGO_1663. DR GeneID; 3281307; -. DR KEGG; ngo:NGO1663; -. DR PATRIC; 20336876; VBINeiGon24812_1983. DR HOGENOM; HOG000257794; -. DR KO; K08992; -. DR OMA; FIYGANM; -. DR OrthoDB; EOG6G7R5G; -. DR BioCyc; NGON242231:GI2G-1557-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 65 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 23 80 DUF1049. {ECO:0000259|Pfam:PF06305}. SQ SEQUENCE 104 AA; 11345 MW; 7FFD53B05D89B12F CRC64; MKLIYTVIKI IILLLFLLLA VINMDAVTFS YLPGQSVNLP LIVVLFGAFV VGIVFGMFAL FGRLLSLRGE NSRLRAEVKK SARLSGQKLT APPIQNAAES AKQP // ID Q5F6V8_NEIG1 Unreviewed; 729 AA. AC Q5F6V8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 87. 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 ORFNames=NGO_1437 {ECO:0000313|EMBL:AAW90079.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90079.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90079.1; -; Genomic_DNA. DR RefSeq; WP_010951264.1; NC_002946.2. DR RefSeq; YP_208491.1; NC_002946.2. DR ProteinModelPortal; Q5F6V8; -. DR EnsemblBacteria; AAW90079; AAW90079; NGO_1437. DR GeneID; 3281691; -. DR KEGG; ngo:NGO1437; -. DR PATRIC; 20336293; VBINeiGon24812_1695. DR HOGENOM; HOG000037413; -. DR KO; K04066; -. DR OMA; DMDTARI; -. DR OrthoDB; EOG6KT2K4; -. DR BioCyc; NGON242231:GI2G-1344-MONOMER; -. DR Proteomes; UP000000535; 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; 3. 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:UP000000535}; 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:UP000000535}; 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; 81124 MW; 79A2AE7FD19EA714 CRC64; MIYHRIAVNV PLSDGLLTYS HSEPLPPGTR VLVPFRNKTV VGMVWETDIA PDMDAARILS VQTVFVEEKP LSQSWRDLLA FTSRYYHYPT GQAVFAALPQ GLKETRAVEM PQPPLFYALN EAGRAQTPPP ARFNKKAALW DALLSGEMTM AALKQANAQA AKLIEDWAEQ GWIETTEAAK PVLRPYRGQA SHSEFVLNTG QQKASDEIQT ALGRFRSFLL YGITGSGKTE VYFDAMAKVL AQGRQVLFLL PEINLTPQLL KRVENRFADV PTAVLHSRMA AGRRTQDYLR AMLGQAKLVI GTRLAVFTPL PDVGLIVVDE EHDGSFKQDN ELRYHARDLA VWRAKQGGCP VVLGSATPSL ESWHKAQSGA YRLLQLTERA HASAQLPQVD ILNIGRLKLD NGFSPQALQL LKQNFEAGGM SLVYLNRRGF APALFCGDCG HTFGCPNCSA KMVLHQRARQ LRCHHCDHRE PIPFKCPDCG NQDLTAVGHG TQRVEETLRA FLPKAAVVRV DRDSTAHKND WADLYRRIAN DEIDILVGTQ MLAKGHDFAR LNLVIVLNAD GSLYSADFRA PERLFAELMQ VSGRAGRADK PGKVLIQTQL PEHPVFAAVK AQDYAVFAEN ELNERQMFAM PPFGFQTAVR ADAPRVADAM EFLNAAKETL APLLPESVSR FGAAPMLMVR LAERERAQVF LESTSRQDLH RAVSLWVQVL QQNRDGKIRW SVDVDPQEA // ID Q5F5E5_NEIG1 Unreviewed; 216 AA. AC Q5F5E5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Periplasmic protein {ECO:0000313|EMBL:AAW90592.1}; GN ORFNames=NGO_1984 {ECO:0000313|EMBL:AAW90592.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90592.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90592.1; -; Genomic_DNA. DR RefSeq; WP_003696353.1; NC_002946.2. DR RefSeq; YP_209004.1; NC_002946.2. DR EnsemblBacteria; AAW90592; AAW90592; NGO_1984. DR GeneID; 3282640; -. DR KEGG; ngo:NGO1984; -. DR PATRIC; 20337735; VBINeiGon24812_2394. DR HOGENOM; HOG000218712; -. DR OMA; NTPAKPH; -. DR OrthoDB; EOG6D2KT6; -. DR BioCyc; NGON242231:GI2G-1882-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 58 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 216 AA; 23274 MW; 5F25CD99B6F06EA3 CRC64; MPSEPPSDGI ARHPKSTIKM AKKPNKPFRL TPKLLIRAVL LICITAIGAL AVGIVSTFNP NGDKTLQTEP QHTDSPRETE FWLPNGAVGQ DAAQPEHHHA ASSEPAQPDG TEESGSGLPS PAAPKKNRVK PRPSDAARAA DSLTGTGTQA ENTLKETPVL PTNAPHPEPR KETPEKQAQP KETPKEKETP KENHTKPDTP KNTPAKPHKE ILDNLF // ID Q5F6K2_NEIG1 Unreviewed; 289 AA. AC Q5F6K2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Cell division protein FtsN {ECO:0000313|EMBL:AAW90185.1}; GN ORFNames=NGO_1549 {ECO:0000313|EMBL:AAW90185.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90185.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90185.1; -; Genomic_DNA. DR RefSeq; WP_003689467.1; NC_002946.2. DR RefSeq; YP_208597.1; NC_002946.2. DR ProteinModelPortal; Q5F6K2; -. DR EnsemblBacteria; AAW90185; AAW90185; NGO_1549. DR GeneID; 3281481; -. DR KEGG; ngo:NGO1549; -. DR PATRIC; 20336600; VBINeiGon24812_1846. DR HOGENOM; HOG000219100; -. DR OMA; AFKIPVP; -. DR OrthoDB; EOG6SR90S; -. DR BioCyc; NGON242231:GI2G-1453-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. 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 Cell cycle {ECO:0000313|EMBL:AAW90185.1}; KW Cell division {ECO:0000313|EMBL:AAW90185.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 31543 MW; 0B8618DC32F5D8AE CRC64; MFMNKFSQSG KGLSGFFFGL ILATVIIAGI LLYLNQGGQN AFKIPAPSKQ PAETEILKLK NQPKEDIQPE PADQNALSEP DVAKEAEQSD AEKAADKQPV ADKADEVEEK AGEPEREEPD GQAVRKKALT EEREQTVREK AQKKDAETVK KQAVKPSKET EKKASKEEKK AAKEKVAPKP TPEQILNSGS IEKARSAAAK EVQKMKTFGK AEATHYLQMG AYADRRSAEG QRAKLAILGI SSEVVGYQAG HKTLYRVQSG NMSADAVKKM QDELKKHGVA SLIRAIEGK // ID Q5F9C2_NEIG1 Unreviewed; 153 AA. AC Q5F9C2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 61. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89215.2}; GN ORFNames=NGO_0477 {ECO:0000313|EMBL:AAW89215.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89215.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3KXA} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 13-145, AND DISULFIDE BONDS. RX PubMed=20196080; DOI=10.1002/prot.22698; RA Ren J., Sainsbury S., Nettleship J.E., Saunders N.J., Owens R.J.; RT "The crystal structure of NGO0477 from Neisseria gonorrhoeae reveals a RT novel protein fold incorporating a helix-turn-helix motif."; RL Proteins 78:1798-1802(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; AE004969; AAW89215.2; -; Genomic_DNA. DR PDB; 3KXA; X-ray; 2.80 A; A/B/C/D=21-153. DR PDBsum; 3KXA; -. DR ProteinModelPortal; Q5F9C2; -. DR EnsemblBacteria; AAW89215; AAW89215; NGO_0477. DR PATRIC; 20333990; VBINeiGon24812_0567. DR OMA; QSHIARI; -. DR OrthoDB; EOG63JRB4; -. DR BioCyc; NGON242231:GI2G-455-MONOMER; -. DR EvolutionaryTrace; Q5F9C2; -. DR Proteomes; UP000000535; 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:3KXA}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 85 139 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. FT DISULFID 28 37 {ECO:0000213|PDB:3KXA}. SQ SEQUENCE 153 AA; 16585 MW; 63D12E2D990BAE63 CRC64; MGATLTVAVA ACTVSTPTSA IPVTHIKCLR INGQIKCVKP ISPNTTPAAE HIEHVRKNPR RKAAMDRAAA RIADKIALKA GGETFVSLRM KKGFTQSELA TAAGLPQPYL SRIENSKQSL QDKTVQKLAN ALGVSPLEVR AAFERRYEYM EQA // ID Q5F675_NEIG1 Unreviewed; 322 AA. AC Q5F675; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90312.2}; GN ORFNames=NGO_1687 {ECO:0000313|EMBL:AAW90312.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90312.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90312.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90312; AAW90312; NGO_1687. DR PATRIC; 20336932; VBINeiGon24812_2010. DR HOGENOM; HOG000219117; -. DR OMA; FTEYGWQ; -. DR OrthoDB; EOG6X6RD6; -. DR BioCyc; NGON242231:GI2G-1582-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR016631; Regulatory_RpfE. DR PIRSF; PIRSF015283; Regulatory_RpfE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 322 AA; 36875 MW; 89556F41F071718B CRC64; MKLTLALPSL NLDEDEIRIP LCLPAFNKIL QYGSPHRQSC TASAFYARYL WCGRLAQRPA QSLNMPSETV ALATPVWQKM GLHQANVLTA EYLDVGTDEA ERLCRDLSAF YGDIPWRFVP VLPELWLVSL PRAYRWGAKP VLDLGGLLGA DDQPDGEDAL EWLRVQTEIQ MWLNAHPVNH NRKKRGLPEL NGLWLWDSLH GSAQGGTLFA DTVWSRFHPN RRALPDSFRA YAETAAHLPD THHILFMDDL RLTALTGDRE RYAAILQQWE ERWFAPLYEA VRTGKIKRLD IATDGQHGGT LTFKPTDRRK FWRCTKTFDG IW // ID Q5F754_NEIG1 Unreviewed; 661 AA. AC Q5F754; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 90. 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 ORFNames=NGO_1333 {ECO:0000313|EMBL:AAW89983.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89983.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89983.1; -; Genomic_DNA. DR RefSeq; WP_010951242.1; NC_002946.2. DR RefSeq; YP_208395.1; NC_002946.2. DR ProteinModelPortal; Q5F754; -. DR EnsemblBacteria; AAW89983; AAW89983; NGO_1333. DR GeneID; 3282022; -. DR KEGG; ngo:NGO1333; -. DR PATRIC; 20336035; VBINeiGon24812_1567. DR HOGENOM; HOG000075154; -. DR KO; K02622; -. DR OMA; VEVARFK; -. DR OrthoDB; EOG6P334W; -. DR BioCyc; NGON242231:GI2G-1247-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; 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:UP000000535}; 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; 72099 MW; 1FCFDF70ACD6B299 CRC64; MAKNNQYSES SITVLKGLEP VKERPGMYTR TDSPTHICQE VIDNAADEAL GGFATEIDVQ IHEDGSLSVR DNGRGIPVGL HPEEGVPVVE LVFTRLHAGG KFNKKDGGSA YAFSGGLHGV GVSVTNALST RLEVSVKRDG KVHRIVFAGG DVVEPLAQVG KCAVKDSGTE VRVWPDGKYF ESPNYSIPEL ERLLRAKAVL LPGVRVSLTR PVKGEDEAHT QTWHYPDGLK SYLTDLIADA QEAVPLFSCE NYISDGHNGD FSIGEGAAFA LTWLEEGSCA NESYVNLIPT SLGGTHEAGL KQAVFNAVNN FINLHNLLPR GVKVQSDDVF GKTAFVLSAR VLDPQFQGQT KDKLTNRDAL KLVAAVSGDP LELWLNQNVD FGKKIAELAI RQAQARIRSV KKIEKKKGSG VAILPGKLTD CESEDIRENE LFLVEGDSAG GSAKLARDKA TQAILPLRGK VLNSFEVHPD QLFGNAEIHD ISVAVGVDPH AINDHPDLSG LRYGKIAILS DADVDGSHIQ VLLLTLFYRH FPKLVADGHI YVAQPPLFRV DVNAQGKSKP ARKFYALDQN ELDGILERLQ KEGVKETAYS ISRFKGLGEM NPDQLKDTTM HPDTRRLLQV QIPEGADDET RDIFVKLMGK GEAAARRAWM EREGDTAQLD I // ID Q5FAB9_NEIG1 Unreviewed; 469 AA. AC Q5FAB9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Peptidase S13 {ECO:0000313|EMBL:AAW88868.1}; GN ORFNames=NGO_0107 {ECO:0000313|EMBL:AAW88868.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88868.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88868.1; -; Genomic_DNA. DR RefSeq; WP_003700891.1; NC_002946.2. DR RefSeq; YP_207280.1; NC_002946.2. DR ProteinModelPortal; Q5FAB9; -. DR MEROPS; S13.003; -. DR EnsemblBacteria; AAW88868; AAW88868; NGO_0107. DR GeneID; 3282411; -. DR KEGG; ngo:NGO0107; -. DR PATRIC; 20333113; VBINeiGon24812_0140. DR HOGENOM; HOG000263952; -. DR KO; K07259; -. DR OMA; AHSKPMK; -. DR OrthoDB; EOG6NGVQ4; -. DR BioCyc; NGON242231:GI2G-97-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256643. SQ SEQUENCE 469 AA; 50520 MW; 5210DB1ECA9FFCDE CRC64; MNFPKTAASL LLLLASLAAH ALDTGRIPQN EIAVYVQELD SGKVIIDHRA GIPVNPASTM KLVTAFAAFK TFGSNYRWAT EFKSNGTVND GTLDGNLYWA GSGDPVFNQE NLLAVQRQLR DKGIRNITGR LMLDHSLWGE VGSPDHFEAD SGSPFMTPPN PTMLSAGMVM VRAERNAAGS TDILTDPPLP HIFAQNNLKI TASQAACPSV KKLMRASFSG NTLKLRGNIP ESCLGKPVGV RMFALDELIR QSFTNRWLLG GGRISDGIGI ADTPEGAQTL AVAHSKPMKE ILTDMNKRSD NLIARSVFLK LGGDGKLPAV SEQAASAVRR ELAVSGIDVA DLVLENGSGL SRKERVTARM MAQMLETAYF SPFAQDFIDT LPIAGTDGTL RNRFKQSGGL LRLKTGTLNN VRALAGYWLG DKPMAVVVII NSGRAVSLLP DLDNFVAKNI ISGGDGWLDA KLMCKERRA // ID Q5F901_NEIG1 Unreviewed; 658 AA. AC Q5F901; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:AAW89336.1}; GN ORFNames=NGO_0608 {ECO:0000313|EMBL:AAW89336.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89336.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89336.1; -; Genomic_DNA. DR RefSeq; WP_003706149.1; NC_002946.2. DR RefSeq; YP_207748.1; NC_002946.2. DR ProteinModelPortal; Q5F901; -. DR CAZy; CBM50; Carbohydrate-Binding Module Family 50. DR CAZy; GH23; Glycoside Hydrolase Family 23. DR EnsemblBacteria; AAW89336; AAW89336; NGO_0608. DR GeneID; 3281605; -. DR KEGG; ngo:NGO0608; -. DR PATRIC; 20334296; VBINeiGon24812_0720. DR HOGENOM; HOG000258639; -. DR KO; K08307; -. DR OMA; IVPQNDM; -. DR OrthoDB; EOG6038ZC; -. DR BioCyc; NGON242231:GI2G-576-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004255552. 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; 72089 MW; B706B5173E181FDD CRC64; MSKLKTIALT ASGLSVCPGF LYAQNTSSHQ VGLAIMRLNS SILDLPPTKQ YFQSGSLWDE LRQGFRMGEV NPELVRRHES KFIASRSYFD RVVNRSRPYM YHIANEVKKR NMPAEAALLP FIESAFVTKA KSHVGASGLW QFMPATGRHY GLEKTPVYDG RHDVYAATDA ALNYLQYLYG LFGDWPLAFA AYNWGEGNVG RAVNRARDQG LEPTYENLRM PNETRNYVPK LLAVRNIIAT PQSFGMNISD IDNKPYFQAV EPGRPLDNEA IARLAGITQS ELLALNPAFN VPAFIPKNKR KLLLPVASVQ TFQSNYLNAA PDSLFSWEVY TPAAKTSLSD ISTATGMSIA DIKRLNNLNG NLVNAGRSIL VAKNGKTLHT ASESVVSIDI DNTPDTYRSN MPAGTVNVSI ARIQPAAAQT ADITVAPLPQ ETVRTEPDPL VRITEPALAT AAAQPQTEKQ TAMPSETQTA TLAQVIPPND MQAADELMQL VARNNLRRQA EETISAVIGT PDTVAEHNIS SSPQHTVAAD GKRRARLETR VAKAADGEAE TSPLHASIHR VVEGDTLFNI AKRYNVSVAD LIVANNIKGN TIQKGQVLRL AQAAPAQTRI EKVSYTARKG DTFKSIAARF NIHIDDIRRL NPNLNTINPG QRVKLIGS // ID Q5F627_NEIG1 Unreviewed; 387 AA. AC Q5F627; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90360.1}; GN ORFNames=NGO_1739 {ECO:0000313|EMBL:AAW90360.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90360.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90360.1; -; Genomic_DNA. DR RefSeq; WP_003691920.1; NC_002946.2. DR RefSeq; YP_208772.1; NC_002946.2. DR DNASU; 3281176; -. DR EnsemblBacteria; AAW90360; AAW90360; NGO_1739. DR GeneID; 3281176; -. DR KEGG; ngo:NGO1739; -. DR PATRIC; 20337076; VBINeiGon24812_2078. DR HOGENOM; HOG000137687; -. DR OMA; WADEIAM; -. DR OrthoDB; EOG6M9DSH; -. DR BioCyc; NGON242231:GI2G-1635-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025202; PLD-like_dom. DR Pfam; PF13091; PLDc_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 53 134 PLDc_2. {ECO:0000259|Pfam:PF13091}. SQ SEQUENCE 387 AA; 44971 MW; 2DF877F15805F375 CRC64; MTQLFLHSDT PNEKELISIY EKAVSEAVEL YIFSAYLTHW DVKNKLNSKL QEFKFIFGQD FGLSKKEAIR KVLKWLPSHL KFTLMVAQGI QGFHPKAVFW KNDKNEYYAL IGSSNLTHAA FNSNYEANIL TKISEQDFIK VKSWADEIAM KSIPVSEDWL EEYQEAEINY KKSTVRQSVM DKLFMEMPNY NQELIAARRK QMRNHQTVCN QLKNLIKQCA AGKIDNNDFY GEFNKLWSWK SENKGEGVGN RFQDKTWKRT GKSSDFRKLC IAIQSVFDAP LTERDNVVAK QIDWLKECGV STRGSVFSEM LCQEYPDRYP VLNAPIKKFL EENKFKSAKG ASEGSKYIDL SMKLRALLAM QSEIKDLAEL DVLVQAEYRN RTDIDWE // ID Q5F7L0_NEIG1 Unreviewed; 289 AA. AC Q5F7L0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Hemagglutinin {ECO:0000313|EMBL:AAW89827.1}; GN ORFNames=NGO_1161 {ECO:0000313|EMBL:AAW89827.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89827.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89827.1; -; Genomic_DNA. DR RefSeq; WP_003705511.1; NC_002946.2. DR RefSeq; YP_208239.1; NC_002946.2. DR ProteinModelPortal; Q5F7L0; -. DR EnsemblBacteria; AAW89827; AAW89827; NGO_1161. DR GeneID; 3281908; -. DR KEGG; ngo:NGO1161; -. DR PATRIC; 20335593; VBINeiGon24812_1360. DR HOGENOM; HOG000120596; -. DR KO; K16868; -. DR OMA; LHKTDEN; -. DR OrthoDB; EOG6C2WG4; -. DR BioCyc; NGON242231:GI2G-1074-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 91 DUF1971. {ECO:0000259|Pfam:PF09313}. FT DOMAIN 93 284 TehB. {ECO:0000259|Pfam:PF03848}. SQ SEQUENCE 289 AA; 31547 MW; E1E8F99F5B612BB6 CRC64; MKERIVGQSG ELFCFGQMPV WKVENLPEVL LSGYSSEEGE WVCLNVLQGD VEVRAPDGAA EVWSAESGDC VFAPQQVFSV KPKTDDAEIR LSLYCAAADY FHKKYGMSAT HSAVAAAQDT VPAGRALDMG CGQGRNALFL GLKGFDVTAA DCNPAALANV AELAEAEGLN VRTLEYDLNA AALQGEFDYI VATVVLMFLM PQRVPDVIAD MQAHTAAGGY NLIVSAMDTA DFPCPMPFPF KFKEGELKDY YRDWELVEYK EELGAMHAKD ENGNPIRFKF VTMLAKKPG // ID Q5F6Z4_NEIG1 Unreviewed; 215 AA. AC Q5F6Z4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 52. DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:AAW90043.2}; GN ORFNames=NGO_1395 {ECO:0000313|EMBL:AAW90043.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90043.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90043.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6Z4; -. DR EnsemblBacteria; AAW90043; AAW90043; NGO_1395. DR PATRIC; 20336183; VBINeiGon24812_1640. DR HOGENOM; HOG000218674; -. DR OMA; DMEHFSV; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NGON242231:GI2G-1308-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 50 173 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 215 AA; 24753 MW; 71817DFE9461CBE8 CRC64; MSRVTYLLIW YRPLSYRLNA APMFNDNPVV YGKIKLQSWK ARRDFNIVKQ DLDFSCGAAS VATLLNNFYG QKLTEEEVLE KLGKEQMRAS FEDMRRIMPD LGFEAKGYAL SFEQLAQLKI PVIVYLKYRK DDHFSVLRGV DGNTVLLADP SPGHVSMSRA QFLEAWQTRE GNLAGKILAV VPKKAEAISN KLFFTHHPKR QTEFAVGQVK WWRAY // ID Q5F7Y9_NEIG1 Unreviewed; 94 AA. AC Q5F7Y9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 57. DE SubName: Full=DNA-binding phage protein {ECO:0000313|EMBL:AAW89698.2}; GN ORFNames=NGO_1015 {ECO:0000313|EMBL:AAW89698.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89698.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89698.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7Y9; -. DR DNASU; 3282563; -. DR EnsemblBacteria; AAW89698; AAW89698; NGO_1015. DR PATRIC; 20335238; VBINeiGon24812_1187. DR HOGENOM; HOG000218922; -. DR OMA; PANINRA; -. DR OrthoDB; EOG62RSH8; -. DR BioCyc; NGON242231:GI2G-941-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005090; Rep_C. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03428; RP-C; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000313|EMBL:AAW89698.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 72 94 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 94 AA; 10599 MW; 452AF81D6838240A CRC64; MATSKKAQRL LRVFLAMDAH PVIGISNKEL SDGLGLTPSQ VSRDIDDLVA SGLVIKLENG NYAYGIKTLQ IAERFRKQQE RLNARLQELE NRIY // ID Q5F710_NEIG1 Unreviewed; 283 AA. AC Q5F710; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 58. DE RecName: Full=Protein TonB {ECO:0000256|RuleBase:RU362123}; GN ORFNames=NGO_1379 {ECO:0000313|EMBL:AAW90027.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90027.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|RuleBase:RU362123}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU362123}; Single-pass membrane protein CC {ECO:0000256|RuleBase:RU362123}; Periplasmic side CC {ECO:0000256|RuleBase:RU362123}. CC -!- SIMILARITY: Belongs to the TonB family. CC {ECO:0000256|RuleBase:RU362123}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90027.1; -; Genomic_DNA. DR RefSeq; WP_003693736.1; NC_002946.2. DR RefSeq; YP_208439.1; NC_002946.2. DR ProteinModelPortal; Q5F710; -. DR EnsemblBacteria; AAW90027; AAW90027; NGO_1379. DR GeneID; 3281642; -. DR KEGG; ngo:NGO1379; -. DR PATRIC; 20336147; VBINeiGon24812_1622. DR HOGENOM; HOG000220758; -. DR OMA; PNYPAIS; -. DR OrthoDB; EOG6R2H0M; -. DR BioCyc; NGON242231:GI2G-1292-MONOMER; -. DR Proteomes; UP000000535; 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: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 {ECO:0000256|RuleBase:RU362123}; KW Cell membrane {ECO:0000256|RuleBase:RU362123}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU362123}; KW Protein transport {ECO:0000256|RuleBase:RU362123}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal-anchor {ECO:0000256|RuleBase:RU362123}; KW Transmembrane {ECO:0000256|RuleBase:RU362123}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362123}; KW Transport {ECO:0000256|RuleBase:RU362123}. FT TRANSMEM 6 27 Helical. {ECO:0000256|RuleBase:RU362123}. FT DOMAIN 210 282 TonB_C. {ECO:0000259|Pfam:PF03544}. SQ SEQUENCE 283 AA; 28749 MW; 3CD3F8353B445748 CRC64; MDKERILTPA VVFSVALLHL AIVALLWQAH KLPVIESGNV IEFVDLGDFG GGGGAPEGAG APAAPEPQPA PDPPKPVEPP KPVLKPAVTK KADADIQQPK EKPKPEEKPK PEPEPEAKPA PKPAEKPAEK PSEKPAEHSG NASAKAGSEQ GNGEGKGTGT KGDGTGRGEG SGKGSGGAKG EHGEGAGGSG GGTGVGSSKG NPLRANGSIP RPAYPALSME NDEQGMVVLS VLVSPGGHVE SVKVVKSSGF SRLDNAARKA AQNGHFQANA WTEFKVPVKF ELN // ID Q5F5G3_NEIG1 Unreviewed; 328 AA. AC Q5F5G3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Protease {ECO:0000313|EMBL:AAW90574.1}; GN ORFNames=NGO_1963 {ECO:0000313|EMBL:AAW90574.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90574.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90574.1; -; Genomic_DNA. DR RefSeq; WP_003688139.1; NC_002946.2. DR RefSeq; YP_208986.1; NC_002946.2. DR ProteinModelPortal; Q5F5G3; -. DR DNASU; 3282658; -. DR EnsemblBacteria; AAW90574; AAW90574; NGO_1963. DR GeneID; 3282658; -. DR KEGG; ngo:NGO1963; -. DR PATRIC; 20337681; VBINeiGon24812_2367. DR HOGENOM; HOG000022574; -. DR KO; K04773; -. DR OMA; QIFVDKA; -. DR OrthoDB; EOG6GFGG4; -. DR BioCyc; NGON242231:GI2G-1864-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90574.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000313|EMBL:AAW90574.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 64 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 143 287 Peptidase_S49. FT {ECO:0000259|Pfam:PF01343}. SQ SEQUENCE 328 AA; 35963 MW; 03FD5185E9F3DFB5 CRC64; MQYRIRRENE APEAKNAGET LWERDIMREV LLSAYRDRRR ERMWKNIWRA VSTLILVALI AGIFRKDEAA LQLAGNTPHT AVVNLYGKIG NGVEDQVKKL KDGMEAAYKN PQAKAIVIRA NSPGGSPVVS NTAFEEIRRL KAQHPGIPVY LVAEDMCASG CYYIAAAADK IYADPSSIVG SIGVIGSSFD ATGLMEKIGV KRRVKIAGSN KGMGDPFSPE TPEQSKIWEE MLTGIHGEFI KAVKTGRGGR LKFRQYPDVF SGRVYTGADA LKVGLVDGLG NIYSVARDVV KAPDVVDYTP KDDFGRILGR RFGAELKASV SEALQAVR // ID Q5F4Z7_NEIG1 Unreviewed; 117 AA. AC Q5F4Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=ATP synthase subunit I {ECO:0000313|EMBL:AAW90740.1}; GN ORFNames=NGO_2143 {ECO:0000313|EMBL:AAW90740.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90740.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90740.1; -; Genomic_DNA. DR RefSeq; WP_003687149.1; NC_002946.2. DR RefSeq; YP_209152.1; NC_002946.2. DR EnsemblBacteria; AAW90740; AAW90740; NGO_2143. DR GeneID; 3282778; -. DR KEGG; ngo:NGO2143; -. DR PATRIC; 20338139; VBINeiGon24812_2592. DR HOGENOM; HOG000218748; -. DR KO; K02116; -. DR OrthoDB; EOG6V1M7M; -. DR BioCyc; NGON242231:GI2G-2034-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 12864 MW; DACB33EC87DC4EE1 CRC64; MKQIIILQSA VLSICAAVAF AVWGFAGFLS AVGGGLSYLL PTFVAVLLLK LFRGNPFLQS RMFVFGEILK VMLSLLSMLA VFAIWHQSLV FVPFLMGLLG VSHLVFLVLL RVKDYGR // ID Q5F841_NEIG1 Unreviewed; 54 AA. AC Q5F841; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89646.1}; GN ORFNames=NGO_0957 {ECO:0000313|EMBL:AAW89646.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89646.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89646.1; -; Genomic_DNA. DR RefSeq; WP_003688343.1; NC_002946.2. DR RefSeq; YP_208058.1; NC_002946.2. DR EnsemblBacteria; AAW89646; AAW89646; NGO_0957. DR GeneID; 3282179; -. DR KEGG; ngo:NGO0957; -. DR PATRIC; 20335100; VBINeiGon24812_1119. DR HOGENOM; HOG000071275; -. DR OMA; FLHEVQE; -. DR OrthoDB; EOG62G5XM; -. DR BioCyc; NGON242231:GI2G-888-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 54 AA; 6483 MW; 3C28AF3BEE4B84BB CRC64; MVCWKSGYYY YFLHEVQERT ALSRLPFDSG QRKTCSFRFL TKCRLNGFQT AYGQ // ID Q5F8J4_NEIG1 Unreviewed; 435 AA. AC Q5F8J4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579}; DE EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579}; GN ORFNames=NGO_0779 {ECO:0000313|EMBL:AAW89493.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89493.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89493.1; -; Genomic_DNA. DR RefSeq; WP_003695291.1; NC_002946.2. DR RefSeq; YP_207905.1; NC_002946.2. DR ProteinModelPortal; Q5F8J4; -. DR EnsemblBacteria; AAW89493; AAW89493; NGO_0779. DR GeneID; 3281861; -. DR KEGG; ngo:NGO0779; -. DR PATRIC; 20334704; VBINeiGon24812_0924. DR HOGENOM; HOG000076615; -. DR KO; K00003; -. DR OMA; EWIAGII; -. DR OrthoDB; EOG6XM7CQ; -. DR BioCyc; NGON242231:GI2G-733-MONOMER; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW89493.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 46560 MW; 82BB3C0E6F9B16C2 CRC64; MKPVNIGLLG LGTVGGGAAA VLRDNAEEIS RRLGREIRIS AMCDLSEEKA RQICPSAAFV KDPFELVARK DVDVVVELFG GTGIAKEAVL KAIENGKHIV TANKKLLAEY GNEIFPLAEK QNVIVQFEAA VAGGIPIIKA LREGLAANRI KSIAGIINGT SNFILSEMRE KGSAFADVLK EAQALGYAEA DPTFDIEGND AGHKITIMSA LAFGTPMNFS ACYLEGISKL DSRDIKYAEE LGYRIKLLGV TRKTGKGIEL RVHPTLIPES RLLANVDGVM NAVRVNADMV GETLYYGAGA GALPTASAVV ADIIDIARLV EADTAHRVPH LAFQPAQVQA QTILPMDEIT SSYYLRVQAK DEPGTLGQIA ALLAQENVSI EALIQKGVID QTTAEIVILT HSTVEKHIKS AIAAIEALDC VEKPITMIRM ESLHD // ID Q5F653_NEIG1 Unreviewed; 626 AA. AC Q5F653; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Ribonuclease II {ECO:0000313|EMBL:AAW90334.2}; GN ORFNames=NGO_1713 {ECO:0000313|EMBL:AAW90334.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90334.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90334.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F653; -. DR EnsemblBacteria; AAW90334; AAW90334; NGO_1713. DR PATRIC; 20337018; VBINeiGon24812_2049. DR HOGENOM; HOG000256055; -. DR OMA; QGDKMEK; -. DR OrthoDB; EOG6DRPCH; -. DR BioCyc; NGON242231:GI2G-1609-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR012340; NA-bd_OB-fold. DR SUPFAM; SSF50249; SSF50249; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 626 AA; 69181 MW; 968EA06F5C1D196D CRC64; MNIFYEESGQ FKVAVVVQKN DATYQVDTQH GKRTKVKANN VFAEFDGDMA AFLENAQAQA ADIDTDLLWE VCGEEEFTAE AIAEEYYGHA PTKTELAATL IALYAAPVYF YKKAKGVFKA APEETLKQAL AAIERKKQQD AQIDAWAEAL KRGEMPSEIA ADLRTILHAP DKQSLTYKAF TKAADALKTS AYELAKKTGG ITSIPQYLQD GFEIKYFPKG TGFPDLSLPE MPDLPKADVT AFSIDDESTT EVDDALSLTD LGNGTKRVGI HIAAPSLAVR QGGGMEQIIM QRLSTVYFPG GKITMLPENW ITAFSLDAGA YRPAVSIYFD VDGEFNVGEP TCKIEAVNIA ANLRIQAIEP HFNAETGLDQ AGEMMFAHHQ DLIWFYQFAT ALQKARGKYE PDRAPQYDYS IELDEEGNVS VVRRERGSPI DTLVSEMMIL ANSTWAQMLD ENGLPGLFRV QPAGKVRMST QSEPHIGMGV QHYGWFTSPL RRAADYINQK QLLSLIDDTA EPLFQQSDAE LFAALRDFDT AYAAYADFQR QMEAYWSLVY LQQQGISELT ATILKEDLVR IEGLPLTTRA TGIPFDALPK SQALFKITEL DAEKQFVSLN YIKAAAPGGK TAGNAV // ID Q5F8A3_NEIG1 Unreviewed; 56 AA. AC Q5F8A3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 74. DE RecName: Full=Rubredoxin {ECO:0000256|PIRNR:PIRNR000071}; GN ORFNames=NGO_0885 {ECO:0000313|EMBL:AAW89584.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89584.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89584.1; -; Genomic_DNA. DR RefSeq; WP_003688501.1; NC_002946.2. DR RefSeq; YP_207996.1; NC_002946.2. DR ProteinModelPortal; Q5F8A3; -. DR SMR; Q5F8A3; 1-53. DR EnsemblBacteria; AAW89584; AAW89584; NGO_0885. DR GeneID; 3281432; -. DR KEGG; ngo:NGO0885; -. DR PATRIC; 20334945; VBINeiGon24812_1042. DR HOGENOM; HOG000223371; -. DR OMA; SKDMFEP; -. DR OrthoDB; EOG69SKK0; -. DR BioCyc; NGON242231:GI2G-826-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 6345 MW; 17DACAA86E7DB8CF CRC64; MAQYMCGPCG WIYDEELGDP EHGIAPGTKF EDIPDDWKCP ECGVGKEDFY LLDFVI // ID Q5F720_NEIG1 Unreviewed; 1068 AA. AC Q5F720; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 68. 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 ORFNames=NGO_1369 {ECO:0000313|EMBL:AAW90017.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90017.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90017.1; -; Genomic_DNA. DR RefSeq; WP_010951252.1; NC_002946.2. DR RefSeq; YP_208429.1; NC_002946.2. DR ProteinModelPortal; Q5F720; -. DR EnsemblBacteria; AAW90017; AAW90017; NGO_1369. DR GeneID; 3282239; -. DR KEGG; ngo:NGO1369; -. DR PATRIC; 20336123; VBINeiGon24812_1610. DR HOGENOM; HOG000258319; -. DR KO; K03583; -. DR OMA; SWMRRYP; -. DR OrthoDB; EOG61P6M4; -. DR BioCyc; NGON242231:GI2G-1282-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. SQ SEQUENCE 1068 AA; 120004 MW; 1783FA74F8585F7C CRC64; MFYLYQSNRL ESLAALFARI QKVKPLKCAL QPEQIVVQSQ GMRRYLNTCL ARDLGVAANL AFSLPAGLTW KLMKKLIPGI PELSPFAPEV MRWRLLDLFR SAEFQNGAEF EDVRNVLQDY LGSGESADYQ LAGQLADIFD QYLVYRPQWI DAWQQGRILG LGDDEIWQSK LWRYLDDGRQ SAPHRVALWE KLLAALDKDK LPERYFVFGI STMAPMYLQL LHKLSEHCDV FVFALNPSGM HWGNVIEAAQ ILKGGGDPDL TQAGHPLLAS LGKQGRDFFD FLNEMEIEEE TPVFEEGGRD TLLHALQTDI QNLKMPSENV GSVGTDDGSI CIVSAHSPLR ELQILKDKLL KILHEHPDWQ PHDIAVLTPN IEPYTPFIEA VFGQAQPGAQ ALPYSVSDVK ISRRQPFFYA LECVSDLLES RFEVGKVLAL LETAPVLRRF GLTGDDLPLL HDMVADLNVH WGLDGEMRGG TDQLFTWKQA ADRMILGWML PEGGNPMWQD VSAWYADVNQ TAMFGRFAAF LETLSDIARI WRQPATVGEW VARCRDLLET LFQAGPDDQK AVQNLENEWV KWQEESTLAG FFGQLPQQTV IRHIRRFLDS ESEAGFLRGG ITFCSMVPMR SLPFKVICLL GLNDGDFPRN TKAAVFDLVA KHPAKGDRAR RDDDRYLFLE ALISAREILY LSYIGRDIRK DEELASSSLL GELIDTVAAM TGTNSRQLAQ NWIEQHPLQA FSRRYFQEGG RSDGIFGTRT DYAAALGQTP EPPQPFFDQP VENAEPVAEI GQDEFIRFWR NPVKVWLQQL AWSEPHIGEA WEPAEPFEPQ HAEQIAETYI GARREGQDFS QTAARIAAES LLPSGELGKL WQQSFQTAAK QIDTAVLNSP KLPPFPYAIP SDGQILKGSL GNLYRCGQVF YAYGKPNAPQ RVAFLLEHLI FCAVMPSEAE TRQTFIVQSG ETEVLAEIAQ DRALQLLSEW MAFFNIGQNR PLPFFAKTSL AAAEAFAQKQ DWEAALKKAQ TAYYGSKVSK GQKDYTEVAL VFGNASQNPL EQPLFENLAR LLADTLAAAE KREGTGAA // ID Q5F5N2_NEIG1 Unreviewed; 65 AA. AC Q5F5N2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90505.1}; GN ORFNames=NGO_1888 {ECO:0000313|EMBL:AAW90505.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90505.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90505.1; -; Genomic_DNA. DR RefSeq; WP_003690155.1; NC_002946.2. DR RefSeq; YP_208917.1; NC_002946.2. DR EnsemblBacteria; AAW90505; AAW90505; NGO_1888. DR GeneID; 3282325; -. DR KEGG; ngo:NGO1888; -. DR PATRIC; 20337476; VBINeiGon24812_2269. DR HOGENOM; HOG000218676; -. DR OMA; WVVAARL; -. DR OrthoDB; EOG61S34B; -. DR BioCyc; NGON242231:GI2G-1789-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7206 MW; 58CDE2B47F80E022 CRC64; MNTVPKSRIP VKPLPEKTTA EAKVEKWRQL GADHGLSGEW AVAARLGENG FTEEQMENIA NLFGR // ID Q5F887_NEIG1 Unreviewed; 525 AA. AC Q5F887; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89600.1}; GN ORFNames=NGO_0902 {ECO:0000313|EMBL:AAW89600.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89600.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89600.1; -; Genomic_DNA. DR RefSeq; WP_003702612.1; NC_002946.2. DR RefSeq; YP_208012.1; NC_002946.2. DR ProteinModelPortal; Q5F887; -. DR DNASU; 3281106; -. DR EnsemblBacteria; AAW89600; AAW89600; NGO_0902. DR GeneID; 3281106; -. DR KEGG; ngo:NGO0902; -. DR PATRIC; 20334985; VBINeiGon24812_1062. DR HOGENOM; HOG000157571; -. DR KO; K06132; -. DR OMA; YIFKTDA; -. DR OrthoDB; EOG6VF309; -. DR BioCyc; NGON242231:GI2G-842-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 180 207 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. FT DOMAIN 418 445 PLD phosphodiesterase. FT {ECO:0000259|PROSITE:PS50035}. SQ SEQUENCE 525 AA; 59245 MW; 67C126AFCDA0A360 CRC64; MHTDPKIQAM PSETISPMKT RSLISLLCLL LCSCSSWLPP LEERTESRHF NTSKPVLLDN ILQIRHTPHN NGLSDIYLLD DPHEAFAARA ALIESAEHSL DLQYYIWRND ISGRLLFNLM YLAAERGVRV RLLLDDNNTR GLDDLLLALD SHPNIEVRLF NPFVLRKWRA LGYLTDFPRL NRRMHNKSFT ADNRATILGG RNIGDEYFKV GEDTVFADLD ILATGSVVGE VSHDFDRYWA SHSAHNATRI IRSGNIGKGL QALGYNDETS RHALLRYRET VEQSPLYQKI QTGRIDWQSV QTRLISDSPA KGLDRDRRKP PIAGRLQDAL KQPEKSVYLV SPYFVPTKSG TDALAKLVQD GIDVTVLTNS LQATDVAAVH SGYVKYRKPL LKAGIKLYEL QPNHAVPATK DKGLTGSSVT SLHAKTFIVD GKRIFIGSFN LDPRSARLNT EMGVVIESPK IAEQMERTLA DTTPEYAYRV TLDKHNRLQW HDPATRKTYP NEPEAKLWKR IAAKILSLLP IEGLL // ID Q5F9X4_NEIG1 Unreviewed; 163 AA. AC Q5F9X4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=Transcription elongation factor GreB {ECO:0000256|HAMAP-Rule:MF_00930}; DE AltName: Full=Transcript cleavage factor GreB {ECO:0000256|HAMAP-Rule:MF_00930}; GN Name=greB {ECO:0000256|HAMAP-Rule:MF_00930}; GN ORFNames=NGO_0262 {ECO:0000313|EMBL:AAW89013.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89013.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00930}. CC -!- SIMILARITY: Belongs to the GreA/GreB family. GreB subfamily. CC {ECO:0000256|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; AE004969; AAW89013.1; -; Genomic_DNA. DR RefSeq; WP_003687613.1; NC_002946.2. DR RefSeq; YP_207425.1; NC_002946.2. DR ProteinModelPortal; Q5F9X4; -. DR EnsemblBacteria; AAW89013; AAW89013; NGO_0262. DR GeneID; 3281575; -. DR KEGG; ngo:NGO0262; -. DR PATRIC; 20333491; VBINeiGon24812_0326. DR HOGENOM; HOG000241145; -. DR KO; K04760; -. DR OMA; DQIFFGA; -. DR OrthoDB; EOG686NQ9; -. DR BioCyc; NGON242231:GI2G-245-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 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 {ECO:0000256|HAMAP-Rule:MF_00930}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00105, ECO:0000256|HAMAP- KW Rule:MF_00930, ECO:0000256|SAAS:SAAS00416876}; KW Elongation factor {ECO:0000313|EMBL:AAW89013.1}; KW Protein biosynthesis {ECO:0000313|EMBL:AAW89013.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00105, ECO:0000256|HAMAP- KW Rule:MF_00930, ECO:0000256|SAAS:SAAS00425054}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00105, KW ECO:0000256|HAMAP-Rule:MF_00930, ECO:0000256|SAAS:SAAS00425054}. FT DOMAIN 7 77 GreA_GreB_N. {ECO:0000259|Pfam:PF03449}. FT DOMAIN 86 159 GreA_GreB. {ECO:0000259|Pfam:PF01272}. FT COILED 54 76 {ECO:0000256|HAMAP-Rule:MF_00930}. SQ SEQUENCE 163 AA; 18594 MW; E3D0715146A18EB6 CRC64; MSTETKNYIT PAGWQALKDE LYQLVNKERP EIVQIVNWAA GNGDRSENGD YLYGKRRMRE IDRRIRFLTK RLEAAVVVDP ELREATDQVF FGATVGLLRG DGREQTVKIV GVDEIDTAQN KISWISPLAR CLIKAREGDE VVLNTPEGRE EIEILSVEYI KID // ID Q5F5I7_NEIG1 Unreviewed; 67 AA. AC Q5F5I7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90550.1}; GN ORFNames=NGO_1938 {ECO:0000313|EMBL:AAW90550.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90550.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90550.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90550; AAW90550; NGO_1938. DR PATRIC; 20337619; VBINeiGon24812_2336. DR OrthoDB; EOG6Z0QCR; -. DR BioCyc; NGON242231:GI2G-1840-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025384; DUF4298. DR Pfam; PF14131; DUF4298; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7947 MW; 34FDAD8F31228EC1 CRC64; MDNFYTHEYQ VRHQTIEDGV ELNLQTEGEY SIMSEDALWN APGEFHQLAW LYLCSSVDTL DRYTQEN // ID Q5F7V3_NEIG1 Unreviewed; 693 AA. AC Q5F7V3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Carbon starvation protein A {ECO:0000313|EMBL:AAW89734.1}; GN ORFNames=NGO_1064 {ECO:0000313|EMBL:AAW89734.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89734.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89734.1; -; Genomic_DNA. DR RefSeq; WP_010951168.1; NC_002946.2. DR RefSeq; YP_208146.1; NC_002946.2. DR EnsemblBacteria; AAW89734; AAW89734; NGO_1064. DR GeneID; 3281225; -. DR KEGG; ngo:NGO1064; -. DR PATRIC; 20335362; VBINeiGon24812_1247. DR HOGENOM; HOG000220271; -. DR KO; K06200; -. DR OMA; WGFSISA; -. DR OrthoDB; EOG6H1PW0; -. DR BioCyc; NGON242231:GI2G-979-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 74492 MW; AB94F3CEC3C417EB CRC64; MKSLKTFLIW GIVVLVGLAS FTTLALSRGE QVSAVWMVTA AISVYCIAYR FYSLYIANRV MRLDPNRLTP AERHNDGLDY VPTHKGVLFG HHFAAIAGAG PLVGPVLAAQ MGYLPGTLWI IFGVVFAGAV QDMTVLFVSM RRDGKSLGDI VKQELGTVPG VIASIGILMI MVIIMAVLAL IVVKALVHSP WGTFTIAATM PIALFMGIYT RHIRPGKIGE ISIVGFILLM LAVIYGEDVA KSSIGHWFDL DGIQLTWAIM IYGFVASVLP VWLLLTPRDY LSTFLKIGTI AALALGIVIV NPALQMPAVT HFIDGSGPVF SGTLFPFLFI TIACGAVSGF HALISSGTTP KMLENETHVR MIGYGGMLME SFVAIMALAA AASLDPGVYF AMNSPAALIG TDANTAAEVI TTKLNFPVDA ATLLHTAKEV GENTILSRTG GAPTLAVGMA HIMSRLIPGE AMMAFWYHFA LLFEALFILT AVDAGTRVAR FMIQDLGSIF YKPFGNTDSI PANLIATFFA VALWGYFLYT GVTDPLGGIN SLWPLFGIAN QMLAGVALIM CAVVLIKMKR DRYVWVALVP AVGVLLVTCY AGLQKLFHND PRASFLAHAG KYSDTLAKNE VLAPAKDIGE MAQIIFNDKI NAGLTILFLS VVVTVAAYGL RTALKARKVG WPTAKEIPAV YRDGKQPEEQ SEA // ID Q5F5G4_NEIG1 Unreviewed; 266 AA. AC Q5F5G4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Damage-inducible protein CinA {ECO:0000313|EMBL:AAW90573.1}; GN ORFNames=NGO_1962 {ECO:0000313|EMBL:AAW90573.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90573.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90573.1; -; Genomic_DNA. DR RefSeq; WP_003697756.1; NC_002946.2. DR RefSeq; YP_208985.1; NC_002946.2. DR ProteinModelPortal; Q5F5G4; -. DR EnsemblBacteria; AAW90573; AAW90573; NGO_1962. DR GeneID; 3282659; -. DR KEGG; ngo:NGO1962; -. DR PATRIC; 20337679; VBINeiGon24812_2366. DR HOGENOM; HOG000262180; -. DR OMA; RHFQTAS; -. DR OrthoDB; EOG6130BR; -. DR BioCyc; NGON242231:GI2G-1863-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 172 MoCF_biosynth. FT {ECO:0000259|SMART:SM00852}. SQ SEQUENCE 266 AA; 29791 MW; FF7A82094B2D0325 CRC64; MNAFNLIIIG DEILHGSRQD KHFAFFKSLL ESKGLKLNQV QYLPDEPDLL VRQLRRSFSD GIPTFVTGGI GATPDDRTRQ TAAAALDLPV VRHPEAAKFI EGITRKRGKP LDSPEHAQRL KMADFPEGAE LVPNPFNNIA GFSIREHYFF PGFPVMAHPM AEWVLETYYA GRFNQTERGS RSVYVFEQPE SRITPIIEHI EQTYPGVRSY SLPSVGWTHS DGTQVKPHIE FGIKAEGEAV NLLDAAWAEV LHSLDGLGAE LKNRVN // ID Q5F9H7_NEIG1 Unreviewed; 317 AA. AC Q5F9H7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Phosphate starvation protein PhoH {ECO:0000313|EMBL:AAW89160.1}; GN ORFNames=NGO_0417 {ECO:0000313|EMBL:AAW89160.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89160.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89160.1; -; Genomic_DNA. DR RefSeq; WP_003687857.1; NC_002946.2. DR RefSeq; YP_207572.1; NC_002946.2. DR ProteinModelPortal; Q5F9H7; -. DR SMR; Q5F9H7; 109-312. DR EnsemblBacteria; AAW89160; AAW89160; NGO_0417. DR GeneID; 3282999; -. DR KEGG; ngo:NGO0417; -. DR PATRIC; 20333845; VBINeiGon24812_0500. DR HOGENOM; HOG000015043; -. DR KO; K06217; -. DR OMA; FDITFGI; -. DR OrthoDB; EOG6F81S0; -. DR BioCyc; NGON242231:GI2G-395-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 109 312 PhoH. {ECO:0000259|Pfam:PF02562}. SQ SEQUENCE 317 AA; 35343 MW; F12D1B35605FEAE1 CRC64; MTHTVHLHLE ETDNPTLQRL CGSFDSNLDS LAKALDIHIS RRFEHFTFNG AFAHAGKRAL LKLLETAQTR DLNDSIIRLA AVETQTEDAG HQEKNHEHAY YFRTKRGSIG GRTPRQNGYI RALLDHDIVF GLGPAGTGKT YLAVAAAVDA MEKHQVERII LVRPAVEAGE KLGFLPGDLT QKVDPYLRPL YDALYDLMGF DRVTKLIEKG LIEIAPLAYM RGRTLNGAYI ILDEAQNTTP EQMKMFLTRI GFGAKAVITG DTSQIDLPKN IKSGLKDARE KLHGVAGLYF HTFTGEDVVR HPLVQKIVEA YESAEHD // ID Q5F6I6_NEIG1 Unreviewed; 502 AA. AC Q5F6I6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 62. DE RecName: Full=L-aspartate oxidase {ECO:0000256|RuleBase:RU362049}; DE EC=1.4.3.16 {ECO:0000256|RuleBase:RU362049}; GN ORFNames=NGO_1568 {ECO:0000313|EMBL:AAW90201.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90201.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to CC iminoaspartate. {ECO:0000256|RuleBase:RU362049}. CC -!- CATALYTIC ACTIVITY: L-aspartate + O(2) = iminosuccinate + CC H(2)O(2). {ECO:0000256|RuleBase:RU362049}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU362049}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; CC iminoaspartate from L-aspartate (oxidase route): step 1/1. CC {ECO:0000256|RuleBase:RU362049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC NadB subfamily. {ECO:0000256|RuleBase:RU362049}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90201.1; -; Genomic_DNA. DR RefSeq; WP_003689488.1; NC_002946.2. DR RefSeq; YP_208613.1; NC_002946.2. DR ProteinModelPortal; Q5F6I6; -. DR EnsemblBacteria; AAW90201; AAW90201; NGO_1568. DR GeneID; 3281440; -. DR KEGG; ngo:NGO1568; -. DR PATRIC; 20336646; VBINeiGon24812_1869. DR HOGENOM; HOG000160476; -. DR KO; K00278; -. DR OMA; HCVQWLI; -. DR OrthoDB; EOG696BWH; -. DR BioCyc; NGON242231:GI2G-1469-MONOMER; -. DR UniPathway; UPA00253; UER00326. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW FAD {ECO:0000256|RuleBase:RU362049}; KW Flavoprotein {ECO:0000256|RuleBase:RU362049}; KW Oxidoreductase {ECO:0000256|RuleBase:RU362049}; KW Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362049}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 379 FAD_binding_2. FT {ECO:0000259|Pfam:PF00890}. SQ SEQUENCE 502 AA; 54938 MW; 97D647631854BC24 CRC64; MQTDCDVLIA GNGLAALTLA LSLPESFRIV ILCKNRLDDT ASRHAQGGIA AAWSGEDDIG KHVADTLEAG AGLCDEAAVR TILSQGKPAI EWLLAQGVAF DRNHNDLHLT REGGHTCRRI AHVADYTGEA VMQSLIIQIR RRPNIRVYER QMALDVQTES GAACGLTVLD CRTQETYRIR ARHTVLAGGG LGQIYAATTT PPECTGDAIA MAIRAGCAIE NLEFIQFHPT GLARPSENGR TFLISEAVRG EGGILTNQSG ERFMPHYDRR AELAPRDIVA RAIAAETAKQ TQDFVSLDIS RQPAAFVRRH FPSIHRHCLS QCGLDITRQA IPVRPVQHYT CGGIQTDPSG RTSLPQLYAL GETACTGLHG ANRLASNSLL ECVVTARLAA QGIADGQAFQ IEPFQRPSES PSAETDIFSN DLQNTFSRPV LQTFNQRHLG ILRNDTDLHR AIDQLRLWKQ NQAEPHTASE YENRNLLECS LAVAQAAYRR RQNIGAHFNS DC // ID Q5F9N9_NEIG1 Unreviewed; 106 AA. AC Q5F9N9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=RNA polymerase subunit sigma-32 {ECO:0000313|EMBL:AAW89098.1}; GN ORFNames=NGO_0354 {ECO:0000313|EMBL:AAW89098.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89098.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89098.1; -; Genomic_DNA. DR RefSeq; WP_003690805.1; NC_002946.2. DR RefSeq; YP_207510.1; NC_002946.2. DR EnsemblBacteria; AAW89098; AAW89098; NGO_0354. DR GeneID; 3281257; -. DR KEGG; ngo:NGO0354; -. DR PATRIC; 20333705; VBINeiGon24812_0430. DR HOGENOM; HOG000123173; -. DR OMA; FAEHVED; -. DR OrthoDB; EOG6D8BG7; -. DR BioCyc; NGON242231:GI2G-333-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR016755; UCP019302. DR Pfam; PF10084; DUF2322; 1. DR PIRSF; PIRSF019302; UCP019302; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 106 AA; 11507 MW; CF5C9E425DC66C0A CRC64; MNFQDYLATF PSIDHLGGLD VQDAEGKTVH HIPAVQGKLG SLKLYNALAE RFDGKLGKEA AEQGLIWFAE HVADARAHPG KHPNIDLLEN VVQSGETLLL KPLAAQ // ID Q5F9W6_NEIG1 Unreviewed; 151 AA. AC Q5F9W6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89021.1}; GN ORFNames=NGO_0270 {ECO:0000313|EMBL:AAW89021.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89021.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89021.1; -; Genomic_DNA. DR RefSeq; WP_003690747.1; NC_002946.2. DR RefSeq; YP_207433.1; NC_002946.2. DR EnsemblBacteria; AAW89021; AAW89021; NGO_0270. DR GeneID; 3281616; -. DR KEGG; ngo:NGO0270; -. DR PATRIC; 20333509; VBINeiGon24812_0335. DR HOGENOM; HOG000071237; -. DR OMA; RDWIAKE; -. DR OrthoDB; EOG600DXG; -. DR BioCyc; NGON242231:GI2G-253-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 151 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256088. SQ SEQUENCE 151 AA; 17411 MW; 8E667BF32819EB61 CRC64; MKYTAALLTF LLTACMNPND AFFQNRRYQM PEAQLNGSNA VFHYGYSQNP DHDLLVDQVR VPDAYRASFA RDWIAKEQGY RKNDCVLEKA ESGGVTYYTC DAEKGFNGTR FVIYVVNMKN DKGYVKVYRG MNKPNQEELT KLVADLNKFY P // ID Q5F5P2_NEIG1 Unreviewed; 216 AA. AC Q5F5P2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90495.1}; GN ORFNames=NGO_1875 {ECO:0000313|EMBL:AAW90495.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90495.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90495.1; -; Genomic_DNA. DR RefSeq; WP_010951363.1; NC_002946.2. DR RefSeq; YP_208907.1; NC_002946.2. DR EnsemblBacteria; AAW90495; AAW90495; NGO_1875. DR GeneID; 3282260; -. DR KEGG; ngo:NGO1875; -. DR PATRIC; 20337444; VBINeiGon24812_2253. DR HOGENOM; HOG000218667; -. DR OMA; IFGDACS; -. DR OrthoDB; EOG63C0S9; -. DR BioCyc; NGON242231:GI2G-1779-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 62 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 216 AA; 23972 MW; 2391CB79643DF531 CRC64; MMMHASVQSR FAPILYVLIF FAGFLTAQIW FNQKAYTEEL PPLLSALSAV ALVWLAWAFV SVRSKAKAEK FYREKMIQNE SIHPVLHASL QHLEHKPQML ALLVKNHGKG MAEQVRFKAE VLPDDEDART IAAELAKMDM FALGTDAVAS GETYGRVFAD IFELSAALEG RAFKGILKLT AEYKKHLRRC LPFGNGVGFG RAQSGVEGNL ENTGKA // ID Q5F512_NEIG1 Unreviewed; 209 AA. AC Q5F512; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 56. DE SubName: Full=Cadmium transporter {ECO:0000313|EMBL:AAW90725.2}; GN ORFNames=NGO_2127 {ECO:0000313|EMBL:AAW90725.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90725.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90725.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90725; AAW90725; NGO_2127. DR PATRIC; 20338103; VBINeiGon24812_2574. DR HOGENOM; HOG000099674; -. DR OMA; SRENEDY; -. DR OrthoDB; EOG6RG02S; -. DR BioCyc; NGON242231:GI2G-2019-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 86 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 191 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 209 AA; 23129 MW; A216125CEBE4A56C CRC64; MIQNVVTSII LYSGTAVDLL TYPNVIFCQK KSRKDIINIY LGQFLGSVSL ILLSLLFAFV LDYIPSKEIL GLLGLIPIFL GLKVLLLGDS DGESIAKEGL RKDNKNLIFL VAMITFASCG ADNIGVFVPY FTTLNLANLI VALLTFLVMI YLLVFSAQKL AQVPSVGETL EKYSRWFVAV VYLGLGIYIL IENNSFDMLW TVSGQEKIL // ID Q5F669_NEIG1 Unreviewed; 162 AA. AC Q5F669; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 70. DE RecName: Full=Dihydrofolate reductase {ECO:0000256|PIRNR:PIRNR000194}; DE EC=1.5.1.3 {ECO:0000256|PIRNR:PIRNR000194}; GN ORFNames=NGO_1694 {ECO:0000313|EMBL:AAW90318.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90318.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|PIRNR:PIRNR000194}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- CC dihydrofolate + NADPH. {ECO:0000256|PIRNR:PIRNR000194}. CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; CC 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. CC {ECO:0000256|PIRNR:PIRNR000194}. CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family. CC {ECO:0000256|PIRNR:PIRNR000194}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90318.1; -; Genomic_DNA. DR RefSeq; WP_003689852.1; NC_002946.2. DR RefSeq; YP_208730.1; NC_002946.2. DR ProteinModelPortal; Q5F669; -. DR EnsemblBacteria; AAW90318; AAW90318; NGO_1694. DR GeneID; 3281193; -. DR KEGG; ngo:NGO1694; -. DR PATRIC; 20336952; VBINeiGon24812_2020. DR HOGENOM; HOG000040234; -. DR KO; K00287; -. DR OMA; MCITHVE; -. DR OrthoDB; EOG6KT2V2; -. DR BioCyc; NGON242231:GI2G-1588-MONOMER; -. DR UniPathway; UPA00077; UER00158. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 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 {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000313|EMBL:AAW90318.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000194}; KW One-carbon metabolism {ECO:0000256|PIRNR:PIRNR000194}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000194}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90318.1}. FT DOMAIN 3 161 DHFR (dihydrofolate reductase). FT {ECO:0000259|PROSITE:PS51330}. SQ SEQUENCE 162 AA; 17702 MW; B26FF94E677BF56C CRC64; MLKITIIAAC AENLCIGAGN AMPWHIPEDF AFFKAYTLGK PVIMGRKTWE SLPVKPLPGR RNIVISRQAD YCAAGAETVA SLEVALALCA GAEEAVIMGG AQIYGQAMPL ATDLRITEVD LSVEGDAFFP EIDRTHWREA ERTERRVSSK GVAYTFVHYL KG // ID Q5F665_NEIG1 Unreviewed; 151 AA. AC Q5F665; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90322.1}; GN ORFNames=NGO_1701 {ECO:0000313|EMBL:AAW90322.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90322.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90322.1; -; Genomic_DNA. DR RefSeq; WP_003689877.1; NC_002946.2. DR RefSeq; YP_208734.1; NC_002946.2. DR ProteinModelPortal; Q5F665; -. DR DNASU; 3281188; -. DR EnsemblBacteria; AAW90322; AAW90322; NGO_1701. DR GeneID; 3281188; -. DR KEGG; ngo:NGO1701; -. DR PATRIC; 20336994; VBINeiGon24812_2037. DR HOGENOM; HOG000040998; -. DR OMA; EACLECA; -. DR OrthoDB; EOG6GN73M; -. DR BioCyc; NGON242231:GI2G-1597-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR030913; TAT_Cys_rich. DR InterPro; IPR006311; TAT_signal. DR TIGRFAMs; TIGR04401; TAT_Cys_rich; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 151 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255481. SQ SEQUENCE 151 AA; 15980 MW; FCCE4B6D7CE09E76 CRC64; MNRRQFLGSA AAVSLASAAS FARAHGHADY HHHHDMQPAA ASAYTAVRQT AAHCLDAGQV CLTHCLSLLT QGDTSMSDCA VAVRQMLALC GAVHDLAAQN SPLTRDAAKV CLEACKQCAK ACKEHSAHHA ECKACYESCL DCIKECEKLA A // ID Q5F6S5_NEIG1 Unreviewed; 461 AA. AC Q5F6S5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 73. 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:AAW90112.1}; GN ORFNames=NGO_1472 {ECO:0000313|EMBL:AAW90112.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90112.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90112.1; -; Genomic_DNA. DR RefSeq; WP_003689349.1; NC_002946.2. DR RefSeq; YP_208524.1; NC_002946.2. DR ProteinModelPortal; Q5F6S5; -. DR SMR; Q5F6S5; 293-459. DR EnsemblBacteria; AAW90112; AAW90112; NGO_1472. DR GeneID; 3281598; -. DR KEGG; ngo:NGO1472; -. DR PATRIC; 20336377; VBINeiGon24812_1737. DR HOGENOM; HOG000243958; -. DR KO; K00325; -. DR OMA; HHAEVFI; -. DR OrthoDB; EOG6WDSHK; -. DR BioCyc; NGON242231:GI2G-1377-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW90112.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 48493 MW; F823CB92BD4CF50E CRC64; MSSGLVTAAY IVAAILFIFS LAGLSKQETA KRGCYSGIAG MAVALFVTVF SDNTHGLGWI IIAMLIGAAI GIHKAKKVEM TEMPELIALL HSFVGLAAVL VGFNSYIEPG NVSHDMHTIH LVEVYLGIFI GAVTFTGSLA AFGKLNGKIS SSPLQLPAKH KLNALALAVS FVLLLVFVGI DGSGFILLIM TLIALAFGWH LVASIGGADM PVVVSMLNSY SGWAAAAAGF MLSNDLLIVT GALVGSSGAI LSYIMCKAMN RSFVSVIAGG FGSDSGISSS GSQEIEEYRE VKAADVAEML KGASSVIITP GYGMAVAQAQ YPVAEITELL RKNGIEVRFG IHPVAGRLPG HMNVLLAEAK VPYDIVLEMD EINDDFPETD VVLVIGANDT VNPAAQTDPN SPIAGMPVLE VWKAKEVVVF KRSMNTGYAG VQNPLFFNEN SVMCFGDAKK TVDGILAELK K // ID Q5F8I6_NEIG1 Unreviewed; 135 AA. AC Q5F8I6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89501.1}; GN ORFNames=NGO_0787 {ECO:0000313|EMBL:AAW89501.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89501.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89501.1; -; Genomic_DNA. DR RefSeq; WP_003704054.1; NC_002946.2. DR RefSeq; YP_207913.1; NC_002946.2. DR EnsemblBacteria; AAW89501; AAW89501; NGO_0787. DR GeneID; 3281995; -. DR KEGG; ngo:NGO0787; -. DR PATRIC; 20334722; VBINeiGon24812_0933. DR HOGENOM; HOG000261744; -. DR OMA; GHARIHY; -. DR OrthoDB; EOG6W7227; -. DR BioCyc; NGON242231:GI2G-741-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 14448 MW; 5D987DD97B8A3433 CRC64; MTVWFVAAVA VLIIELLTGT VYLLVVSAAL AGSGIAYGLT GSTPAAVLTA ALLSALGIWF VHAKTAVGKV ETDSYQDLDT GKYAEILRYT GGNRYEVFYR GTHWQAQNTG QEVFEPGTRA LIVRKEGNLL IIANP // ID Q5F8R3_NEIG1 Unreviewed; 186 AA. AC Q5F8R3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89424.1}; GN ORFNames=NGO_0700 {ECO:0000313|EMBL:AAW89424.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89424.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89424.1; -; Genomic_DNA. DR RefSeq; WP_002239757.1; NC_002946.2. DR RefSeq; YP_207836.1; NC_002946.2. DR EnsemblBacteria; AAW89424; AAW89424; NGO_0700. DR GeneID; 3281811; -. DR KEGG; ngo:NGO0700; -. DR HOGENOM; HOG000270328; -. DR OMA; HANNSFL; -. DR OrthoDB; EOG60PHBW; -. DR BioCyc; NGON242231:GI2G-664-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 50 69 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 134 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 186 AA; 21979 MW; CC78ED1D3C79C4A6 CRC64; MDKLFKILLN ISSTSLLLSI YFIKSQYYIL DLTWFYRVIS NHWIEPISKL SLLFYFLIPF IATATVLWLS KYLGKDEFKQ GEVKELEYVN DNFLPSYLGY FFVALSIPDN NLFLLFVMYG IIFLLVSCSK SFYFNPVFFL FGYRFYQAKT ESGLLLVLIS KQEFRTPQSV SSIAVYRINN FTFLEK // ID Q5F9Y8_NEIG1 Unreviewed; 98 AA. AC Q5F9Y8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=3-deoxy-manno-octulosonate cytidylyltransferase {ECO:0000313|EMBL:AAW88999.1}; GN ORFNames=NGO_0246 {ECO:0000313|EMBL:AAW88999.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88999.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88999.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88999; AAW88999; NGO_0246. DR PATRIC; 20333443; VBINeiGon24812_0303. DR HOGENOM; HOG000218834; -. DR OrthoDB; EOG6VF34J; -. DR BioCyc; NGON242231:GI2G-230-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW88999.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88999.1}. SQ SEQUENCE 98 AA; 11403 MW; 7ADBBAF217F0B2AA CRC64; MQQHIEKWQH LSREEQKILA EVWGLVQNDD QEVHYEMLKL NAPDEVSGEF WFRMAETLST LPPNRSLDLR MNGGRLSTAV SILSVMIEDN PDIPQLWA // ID Q5F589_NEIG1 Unreviewed; 291 AA. AC Q5F589; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 65. DE SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:AAW90648.1}; GN ORFNames=NGO_2040 {ECO:0000313|EMBL:AAW90648.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90648.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90648.1; -; Genomic_DNA. DR RefSeq; WP_003686971.1; NC_002946.2. DR RefSeq; YP_209060.1; NC_002946.2. DR ProteinModelPortal; Q5F589; -. DR EnsemblBacteria; AAW90648; AAW90648; NGO_2040. DR GeneID; 3282707; -. DR KEGG; ngo:NGO2040; -. DR PATRIC; 20337863; VBINeiGon24812_2455. DR HOGENOM; HOG000218721; -. DR OMA; VIVEFLI; -. DR OrthoDB; EOG6K9QF5; -. DR BioCyc; NGON242231:GI2G-1941-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90648.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 126 267 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 291 AA; 32350 MW; 364D7BFD622C0838 CRC64; MPTVRFTESV SKQDLDALFE RAKASYGAES CWKTLYLNRL PLGNLSPEWA ERIKKDWEAG CSESSDGIFL NADGWPDMGG RLQHLARTWN KAGLLHGWRN ECFDLTDGGG NPLFTLERAA FRPFGLLSRA VHLNGLVESN GRWHFWIGRR SPHKAVDPGK LDNIAGGGVS GGEMPSEAVC RESSEEAGLD KTLFPLIRPV SRLHSLRPVS RGVHNEILYV FDAVLPETFL PENQDGEVAG FEKMDIGGLL DAMLSKNMMH DAQLVTLDAF YRYGLIDAAH PLSEWLDGIR L // ID Q5F8K8_NEIG1 Unreviewed; 542 AA. AC Q5F8K8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW89479.1}; GN ORFNames=NGO_0764 {ECO:0000313|EMBL:AAW89479.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89479.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89479.1; -; Genomic_DNA. DR RefSeq; WP_010951119.1; NC_002946.2. DR RefSeq; YP_207891.1; NC_002946.2. DR ProteinModelPortal; Q5F8K8; -. DR EnsemblBacteria; AAW89479; AAW89479; NGO_0764. DR GeneID; 3282480; -. DR KEGG; ngo:NGO0764; -. DR PATRIC; 20334676; VBINeiGon24812_0910. DR HOGENOM; HOG000271629; -. DR OMA; WSENAKI; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NGON242231:GI2G-719-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89479.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW89479.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 60807 MW; 067241EF1F86D1C0 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 KRFETQLFRN LNFILEAGQR LAIIGPNGAG KSTLLKLLAG AYNPEYSDGL LPDEGSIKWA EKASVGYYPQ DHENDFDVDM DLSEWMRQWG REGDDEQVIR GTLGRLLFGS NDVVKKVKVL SGGEKGRMLY GKLLLLKPNV LVMDEPTNHM DMESIESLNM ALDKYNGTLI FVSHDRQFVS SLATQIIELD GKGGYEHYLG DYESYLEKKG VA // ID Q5F6Q2_NEIG1 Unreviewed; 47 AA. AC Q5F6Q2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90135.1}; GN ORFNames=NGO_1497 {ECO:0000313|EMBL:AAW90135.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90135.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90135.1; -; Genomic_DNA. DR RefSeq; WP_010951285.1; NC_002946.2. DR RefSeq; YP_208547.1; NC_002946.2. DR EnsemblBacteria; AAW90135; AAW90135; NGO_1497. DR GeneID; 3281590; -. DR KEGG; ngo:NGO1497; -. DR PATRIC; 20336460; VBINeiGon24812_1777. DR HOGENOM; HOG000071355; -. DR OrthoDB; EOG69WFVS; -. DR BioCyc; NGON242231:GI2G-1401-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 46 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 47 AA; 4914 MW; 643FB9620A82B5BE CRC64; MGKIAATWKV PSPQPSAAQG RERIAAGLAV AGGFKSSAGM TVFWFIY // ID Q5F817_NEIG1 Unreviewed; 455 AA. AC Q5F817; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW89670.1}; GN ORFNames=NGO_0984 {ECO:0000313|EMBL:AAW89670.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89670.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89670.1; -; Genomic_DNA. DR RefSeq; WP_003702575.1; NC_002946.2. DR RefSeq; YP_208082.1; NC_002946.2. DR ProteinModelPortal; Q5F817; -. DR EnsemblBacteria; AAW89670; AAW89670; NGO_0984. DR GeneID; 3282864; -. DR KEGG; ngo:NGO0984; -. DR PATRIC; 20335168; VBINeiGon24812_1153. DR HOGENOM; HOG000230997; -. DR OMA; NEDWMRK; -. DR OrthoDB; EOG6CK7K6; -. DR BioCyc; NGON242231:GI2G-912-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 32 210 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. SQ SEQUENCE 455 AA; 50270 MW; B848755699B2B471 CRC64; MPDLHTEFSR LLPADEIAEP SPTLLKDQRN RFTSAPDIIL QPRSVESVQT IMRFCYEHRI PVTPQGGNTG LCGAAVSENG VLLNLSKLNR IRSINLSDNC ITVEAGSVLQ TVQQAAEASN RLFPLSLASE GSCQIGGNIA CNAGGLNVLR YGTMRDLVIG LEVVLPNGEL VSHLHPLHKN TTGYDLRHLF IGSEGTLGII TAATLKLFAR PSDKATAWVG IPDIESAVRL LTETQAHFAE RLCSFELIGR FAAKLSSEFS KLPLPTHSEW HILLELTDSL PDSNLDDRLV EFLYKKGFTD SVLAQSEQER IHMWALRENI SASQRKLGTS IKHDIAVPIG RVADFVRQCA KDLEQNFKGI QIVCFGHLGD GSLHYNTFPP EILSNEVYRY ENDINSTVYR NVLARNGTIA AEHGIGIIKK QWLPAVRTPS EIALMKSIKQ HLDPYNIMNP GKLLP // ID Q5F6G3_NEIG1 Unreviewed; 133 AA. AC Q5F6G3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90224.1}; GN ORFNames=NGO_1596 {ECO:0000313|EMBL:AAW90224.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90224.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90224.1; -; Genomic_DNA. DR RefSeq; WP_003693500.1; NC_002946.2. DR RefSeq; YP_208636.1; NC_002946.2. DR EnsemblBacteria; AAW90224; AAW90224; NGO_1596. DR GeneID; 3281735; -. DR KEGG; ngo:NGO1596; -. DR PATRIC; 20336722; VBINeiGon24812_1907. DR HOGENOM; HOG000219106; -. DR OMA; TANYFFE; -. DR OrthoDB; EOG683S9H; -. DR BioCyc; NGON242231:GI2G-1492-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 133 AA; 16002 MW; CE4D97FFF00EEC47 CRC64; MKIKPLQFSN NNHRFYVDKI CVTEQDVNIL ASDRNYELNI EIFIDNIIHF QITDESYKVK FSEYLFENKT ENNSDGNPTA NYFFEIIDDS YMDWLKEESF GFFEKKYYKA YIFFFSDSVI EVISSTEPVF YSK // ID Q5F8H3_NEIG1 Unreviewed; 82 AA. AC Q5F8H3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89514.1}; GN ORFNames=NGO_0800 {ECO:0000313|EMBL:AAW89514.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89514.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89514.1; -; Genomic_DNA. DR RefSeq; WP_003688613.1; NC_002946.2. DR RefSeq; YP_207926.1; NC_002946.2. DR EnsemblBacteria; AAW89514; AAW89514; NGO_0800. DR GeneID; 3282030; -. DR KEGG; ngo:NGO0800; -. DR PATRIC; 20334748; VBINeiGon24812_0946. DR HOGENOM; HOG000027812; -. DR OMA; SADWAQT; -. DR OrthoDB; EOG6CCH8F; -. DR BioCyc; NGON242231:GI2G-754-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 9483 MW; 87EBD62D9629AB78 CRC64; MGRAGHTFPK PPPDFLIWRP AHHFRPIETP VLKDCVYFHR RFKGRRYSAD GVQTAFRRHF HSFGVSVRMA LPVRAISPCG LP // ID Q5FA08_NEIG1 Unreviewed; 140 AA. AC Q5FA08; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88979.1}; GN ORFNames=NGO_0226 {ECO:0000313|EMBL:AAW88979.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88979.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88979.1; -; Genomic_DNA. DR RefSeq; WP_002261379.1; NC_002946.2. DR RefSeq; YP_207391.1; NC_002946.2. DR EnsemblBacteria; AAW88979; AAW88979; NGO_0226. DR GeneID; 3281476; -. DR KEGG; ngo:NGO0226; -. DR PATRIC; 20333393; VBINeiGon24812_0278. DR HOGENOM; HOG000220702; -. DR OrthoDB; EOG67MF3J; -. DR BioCyc; NGON242231:GI2G-210-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 16552 MW; FF9CCF76ACA4B614 CRC64; MMKRIKCFCD KFPSGDTFRM CIILDDYDNR VDYYVGIYDY ITSTLMSDIY YRSTIDEHFK IIELIENNPN EIYDDGGGQQ FCLEFHHDKV IFYHNEFDEE DGYPVLSCSL HTFKTALIAW NAFLQLPKSI HSVVETVIEE // ID Q5F6W0_NEIG1 Unreviewed; 231 AA. AC Q5F6W0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 84. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90077.2}; GN ORFNames=NGO_1434 {ECO:0000313|EMBL:AAW90077.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90077.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90077.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6W0; -. DR EnsemblBacteria; AAW90077; AAW90077; NGO_1434. DR PATRIC; 20336287; VBINeiGon24812_1692. DR OMA; NIAIFMD; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1342-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90077.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90077.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 218 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 231 AA; 25712 MW; FBF778EA719AA08A CRC64; MMICLENVRF EILRDPIVRD FSLNLQQGEV KALFGPSGCG KTTVLRLIAG LETPKSGTIR NTFHKTGFLF QENRLPENLT AMQNIAIFMD NPDEGEIVAL AAKVGLTAGD LNKYPTELSG GMAKRVAFLR LLLCGCDLAL LDEPFVGLDR DLRDILVAML VEKIERQGMA CILVTHDRFE AARLSHEIML LSAKGMNVQN VITLPTPLSE RDSAFEEVVV AREFQGIHYY E // ID Q5F8P2_NEIG1 Unreviewed; 102 AA. AC Q5F8P2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89445.1}; GN ORFNames=NGO_0725 {ECO:0000313|EMBL:AAW89445.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89445.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89445.1; -; Genomic_DNA. DR RefSeq; WP_003688714.1; NC_002946.2. DR RefSeq; YP_207857.1; NC_002946.2. DR EnsemblBacteria; AAW89445; AAW89445; NGO_0725. DR GeneID; 3282090; -. DR KEGG; ngo:NGO0725; -. DR PATRIC; 20334578; VBINeiGon24812_0861. DR HOGENOM; HOG000071295; -. DR OMA; DERREQP; -. DR OrthoDB; EOG6ZPT33; -. DR BioCyc; NGON242231:GI2G-685-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 102 AA; 11429 MW; A7CDAD3A6EEF33B6 CRC64; MPRQSCHSSP FPRKRESGTQ TRQESIGKNN PTAVIPAQAG IQTHNVKAVY QKKPKPNALD FRLRGNDEEL GSDERREQPR KKPPTPSDGI GNKKARKNRA ES // ID Q5F6Z1_NEIG1 Unreviewed; 276 AA. AC Q5F6Z1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90046.1}; GN ORFNames=NGO_1398 {ECO:0000313|EMBL:AAW90046.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90046.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90046.1; -; Genomic_DNA. DR RefSeq; WP_003695633.1; NC_002946.2. DR RefSeq; YP_208458.1; NC_002946.2. DR EnsemblBacteria; AAW90046; AAW90046; NGO_1398. DR GeneID; 3281237; -. DR KEGG; ngo:NGO1398; -. DR PATRIC; 20336191; VBINeiGon24812_1644. DR HOGENOM; HOG000286736; -. DR KO; K19341; -. DR OMA; EYMLSFP; -. DR OrthoDB; EOG6PGK5S; -. DR BioCyc; NGON242231:GI2G-1311-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR032688; ABC2_membrane_2. DR Pfam; PF12679; ABC2_membrane_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 105 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 198 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 271 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 276 AA; 29337 MW; 189E1C38026506A9 CRC64; MNPVWIITGK EARDSLRNRW VLAAVLLLAA LALSLGFLGS SPTGSVKVDP LTVTVVSLSS LSIFLIPLIA MLLSYDALIG EIERGTMALL LSYPIWRNQI LAGKFVGHLI ILALATTAGY GLAGITLQLA NGGFDIAAWK PFALLIAASV ILGAAFLSMG YLISAKVKER GTAAGISIGV WLFFVVIFDM ALLGILVADS KQVITAPVVE TVLLFNPTDI YRLLNLTGYE NTAMYAGMAG LSGQIGLTVP VLLTAQVLWV IIPLVLAAGI FRKRRI // ID Q5F9Q1_NEIG1 Unreviewed; 78 AA. AC Q5F9Q1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89086.1}; GN ORFNames=NGO_0342 {ECO:0000313|EMBL:AAW89086.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89086.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89086.1; -; Genomic_DNA. DR RefSeq; WP_003687749.1; NC_002946.2. DR RefSeq; YP_207498.1; NC_002946.2. DR EnsemblBacteria; AAW89086; AAW89086; NGO_0342. DR GeneID; 3281770; -. DR KEGG; ngo:NGO0342; -. DR PATRIC; 20333681; VBINeiGon24812_0418. DR HOGENOM; HOG000071240; -. DR OMA; SYAARTH; -. DR OrthoDB; EOG6W4621; -. DR BioCyc; NGON242231:GI2G-321-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 78 AA; 8665 MW; B4AD253CFEA5D716 CRC64; MSVFPYAAHT VSRTKCPLFN GMGFHTNGNN RLFTCRRIKS TDDLNTGKSY AARTHHFSRQ SICAAHIDNA GKAVHIVD // ID Q5F7F7_NEIG1 Unreviewed; 238 AA. AC Q5F7F7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 63. DE SubName: Full=GntR family transcriptional regulator {ECO:0000313|EMBL:AAW89880.1}; GN ORFNames=NGO_1221 {ECO:0000313|EMBL:AAW89880.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89880.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89880.1; -; Genomic_DNA. DR RefSeq; WP_003689664.1; NC_002946.2. DR RefSeq; YP_208292.1; NC_002946.2. DR ProteinModelPortal; Q5F7F7; -. DR EnsemblBacteria; AAW89880; AAW89880; NGO_1221. DR GeneID; 3281966; -. DR KEGG; ngo:NGO1221; -. DR PATRIC; 20335755; VBINeiGon24812_1436. DR HOGENOM; HOG000219030; -. DR OMA; YAHIFEA; -. DR OrthoDB; EOG6FJNCS; -. DR BioCyc; NGON242231:GI2G-1132-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00452277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 27086 MW; 4D1AB685F60654B1 CRC64; MNFENDDIIH APTTSSLILE ERHDSELFRV YALILDGITD QVLLPGKKLT ESELCRQMVC SRNTVRGALS LLAHDKIVDL QPNRGAFVHV PDLKEMQDVF NARIEMETMI LNILAGLPDL ETRLKPLYAM IRCEEEASGR GDRVGWNRLS NAFHVELARL VGNDVLFDIM NTLCARSSLI VAVAGVHREK KHAINTHTHS EHREILDLLL AGRRNRVVKI LRRHLGNCME RLEKTLED // ID Q5F8N4_NEIG1 Unreviewed; 52 AA. AC Q5F8N4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89453.1}; GN ORFNames=NGO_0735 {ECO:0000313|EMBL:AAW89453.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89453.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89453.1; -; Genomic_DNA. DR RefSeq; WP_003688702.1; NC_002946.2. DR RefSeq; YP_207865.1; NC_002946.2. DR EnsemblBacteria; AAW89453; AAW89453; NGO_0735. DR GeneID; 3282176; -. DR KEGG; ngo:NGO0735; -. DR BioCyc; NGON242231:GI2G-693-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 48 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 52 AA; 5869 MW; AE604A255B9BA690 CRC64; MLLSLSVFVG IIANLGVFFC LTLLDFMKKL GLTVFIIILF QILLKNALPT RR // ID Q5F558_NEIG1 Unreviewed; 513 AA. AC Q5F558; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 74. DE SubName: Full=ABC transporter permease {ECO:0000313|EMBL:AAW90679.2}; GN ORFNames=NGO_2078 {ECO:0000313|EMBL:AAW90679.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90679.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90679.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F558; -. DR EnsemblBacteria; AAW90679; AAW90679; NGO_2078. DR PATRIC; 20337989; VBINeiGon24812_2517. DR HOGENOM; HOG000218723; -. DR OMA; RWAVWGA; -. DR OrthoDB; EOG6TN430; -. DR BioCyc; NGON242231:GI2G-1973-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 32 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 52 77 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 89 113 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 125 145 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 181 205 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 225 249 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 270 296 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 316 339 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 351 371 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 377 394 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 480 501 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 52 244 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. FT DOMAIN 317 501 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 513 AA; 55353 MW; 15AB1D6F582C040B CRC64; MDGRCWAVRG AFSLLPSAFL AVMVVAPLWA VAAYDGLAWR AVLSDAYMLK RLAWTVFQAA ATCVLVLPLG VPVAWVLARL AFPGRALVLR LLMLPFVMPT LVAGVGVLAL FGADGLLWRG RQDTPYLLLY GNVFFNLPVL VRAAYQGFAQ VPAARLQTAR TLGAGAWRRF WDIEMPVLRP WLAGGVCLVF LYCFSGFGLA LLLGGSRYAT VEVEIYQLVM FELDMAGASA LVWLVLGVTA AAGLLYAWFG RRAVSDKAVS PVMPSPPQSV GEYVLLAFSV AVLSVCCLFP LSAIVVKAWS AGESRRVLME SETWQAVWNT LRFSAAAVFA AAVLGVVYAA AARRLVWMRG LVFLPFMVSP VCVSAGVLLL YPGWTASLPL LLAMYALLAY PFVAKDVLSA WDALPPDYGR AAAGLGANGF QTACRITFPL LKPALRRGLT LAAATCVGEF AATLFLSRPE WQTLTTLIYA YLGRAGEDNY ARAMVLTLLL SAFAVCIFLL LDNGEGGKRT ETL // ID Q5F5V7_NEIG1 Unreviewed; 348 AA. AC Q5F5V7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90430.1}; GN ORFNames=NGO_1812 {ECO:0000313|EMBL:AAW90430.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90430.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU000469}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane CC {ECO:0000256|RuleBase:RU000469}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000469}. CC -!- SIMILARITY: Belongs to the Gram-negative porin family. CC {ECO:0000256|RuleBase:RU000469}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90430.1; -; Genomic_DNA. DR RefSeq; WP_010951356.1; NC_002946.2. DR RefSeq; YP_208842.1; NC_002946.2. DR ProteinModelPortal; Q5F5V7; -. DR EnsemblBacteria; AAW90430; AAW90430; NGO_1812. DR GeneID; 3282133; -. DR KEGG; ngo:NGO1812; -. DR PATRIC; 20337282; VBINeiGon24812_2176. DR HOGENOM; HOG000114654; -. DR KO; K18133; -. DR OMA; FSAMYSF; -. DR OrthoDB; EOG6358DM; -. DR BioCyc; NGON242231:GI2G-1710-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|RuleBase:RU000469}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ion transport {ECO:0000256|RuleBase:RU000469}; KW Membrane {ECO:0000256|RuleBase:RU000469}; KW Porin {ECO:0000256|RuleBase:RU000469}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000469}; KW Transport {ECO:0000256|RuleBase:RU000469}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 348 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255473. SQ SEQUENCE 348 AA; 37187 MW; 5D17BCBC72822BB0 CRC64; MKKSLIALTL AALPVAAMAD VTLYGAIKAG VQTYRSVEHT DGKVSKVETG SEIADFGSKI GFKGQEDLGN GLKAVWQLEQ GASVAGTNTG WGNKQSFVGL KGGFGTIRAG SLNSPLKNTG ANVNAWESGK FTGNVLEISG MAQREHRYLS VRYDSPEFAG FSGSVQYAPK DNSGSNGESY HVGLNYQNSG FFAQYAGLFQ RYGEGTKKIE YDGQTYSIPS LFVEKLQVHR LVGGYDNNAL YVSVAAQQQD AKLYGAMSGN SHNSQTEVAA TAAYRFGNVT PRVSYAHGFK GTVDSANHDN TYDQVVVGAE YDFSKRTSAL VSAGWLQEGK GADKIVSTAS AVVLRHKF // ID Q5F6F3_NEIG1 Unreviewed; 176 AA. AC Q5F6F3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 57. 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 ORFNames=NGO_1606 {ECO:0000313|EMBL:AAW90234.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90234.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90234.1; -; Genomic_DNA. DR RefSeq; WP_003689542.1; NC_002946.2. DR RefSeq; YP_208646.1; NC_002946.2. DR ProteinModelPortal; Q5F6F3; -. DR EnsemblBacteria; AAW90234; AAW90234; NGO_1606. DR GeneID; 3281550; -. DR KEGG; ngo:NGO1606; -. DR PATRIC; 20336750; VBINeiGon24812_1920. DR HOGENOM; HOG000264762; -. DR KO; K09774; -. DR OMA; RADRDKP; -. DR OrthoDB; EOG6KQ6FT; -. DR BioCyc; NGON242231:GI2G-1503-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Periplasm {ECO:0000256|HAMAP-Rule:MF_01914}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5005078505. FT DOMAIN 32 142 OstA-like_N. {ECO:0000259|Pfam:PF03968}. SQ SEQUENCE 176 AA; 18344 MW; CADF44C9104214D4 CRC64; MIQKICKLFV LIVIFATSPA FALQSDSRRP IQIEADQGSL DQANQSTTFS GNVIIRQGTL NISASRVNVT RGGKGGESVR AEGSPVRFSQ TLDGGKGTVR GQANNVTYSS AGSTVVLTGN AKVQRGGDVA EGAVITYNTK TEVYTINGST KSGAKSASKT GRVSVVIQPS STQKTE // ID Q5F894_NEIG1 Unreviewed; 333 AA. AC Q5F894; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=tRNA-dihydrouridine(16) synthase {ECO:0000256|HAMAP-Rule:MF_02043}; DE EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02043}; DE AltName: Full=U16-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02043}; DE AltName: Full=tRNA-dihydrouridine synthase C {ECO:0000256|HAMAP-Rule:MF_02043}; GN Name=dusC {ECO:0000256|HAMAP-Rule:MF_02043}; GN ORFNames=NGO_0894 {ECO:0000313|EMBL:AAW89593.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89593.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_02043}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(16) in tRNA + NAD(P)(+) = CC uracil(16) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02043}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02043, CC ECO:0000256|PIRNR:PIRNR006621}; CC -!- SIMILARITY: Belongs to the Dus family. DusC subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02043}. 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; AE004969; AAW89593.1; -; Genomic_DNA. DR RefSeq; WP_003688483.1; NC_002946.2. DR RefSeq; YP_208005.1; NC_002946.2. DR ProteinModelPortal; Q5F894; -. DR EnsemblBacteria; AAW89593; AAW89593; NGO_0894. DR GeneID; 3281369; -. DR KEGG; ngo:NGO0894; -. DR PATRIC; 20334961; VBINeiGon24812_1050. DR HOGENOM; HOG000217854; -. DR KO; K05541; -. DR OMA; GYKPPAH; -. DR OrthoDB; EOG6VHZFQ; -. DR BioCyc; NGON242231:GI2G-835-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02043, KW ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02043, ECO:0000256|PIRNR:PIRNR006621}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02043}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02043, KW ECO:0000256|PIRNR:PIRNR006621}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_02043}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02043, KW ECO:0000256|PIRNR:PIRNR006621}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02043}. FT NP_BIND 211 213 FMN. {ECO:0000256|HAMAP-Rule:MF_02043}. FT NP_BIND 235 236 FMN. {ECO:0000256|HAMAP-Rule:MF_02043}. FT ACT_SITE 110 110 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_02043, FT ECO:0000256|PIRSR:PIRSR006621-1}. FT BINDING 80 80 FMN. {ECO:0000256|HAMAP-Rule:MF_02043}. FT BINDING 151 151 FMN. {ECO:0000256|HAMAP-Rule:MF_02043}. FT SITE 47 47 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02043}. FT SITE 107 107 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02043}. FT SITE 188 188 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02043}. FT SITE 289 289 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02043}. FT SITE 291 291 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02043}. FT SITE 312 312 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02043}. SQ SEQUENCE 333 AA; 36991 MW; 293C11D684E5B605 CRC64; MIDGQTTEPK QKTRIIPAPM RGLVDDVMRD LLTRIGGYDE CVSEFVRITH TVHSRSIWLK YVPEIANGNK TFSGTPCTVQ LLGSDADNMA ANALEAVRFG ADKIDLNFGC PAPTVNKHKG GAILLKEPEL IFHIVKTLRG RLPAHIPLTG KMRLGYEDKS PALECACAIA EGGACGLTVH ARTKAEGYEP PAHWEWIRKI HDTVNIPVTA NGDVFSLQDY IGIKTISGCN SVMLGRGAVI RPDLARQIKQ YENGGPVKDT DFAEVSTWIG QFFELCLTKE ANNKYPIARL KQWLGMMKKT FDPAQTLFDR VRTVKDADEV RRILNAFEHE MDV // ID Q5F642_NEIG1 Unreviewed; 262 AA. AC Q5F642; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AAW90345.1}; GN ORFNames=NGO_1724 {ECO:0000313|EMBL:AAW90345.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90345.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90345.1; -; Genomic_DNA. DR RefSeq; WP_004467096.1; NC_002946.2. DR RefSeq; YP_208757.1; NC_002946.2. DR ProteinModelPortal; Q5F642; -. DR EnsemblBacteria; AAW90345; AAW90345; NGO_1724. DR GeneID; 3281336; -. DR KEGG; ngo:NGO1724; -. DR PATRIC; 20337044; VBINeiGon24812_2062. DR HOGENOM; HOG000219127; -. DR KO; K02169; -. DR OMA; NAPGHIL; -. DR OrthoDB; EOG63VBXF; -. DR BioCyc; NGON242231:GI2G-1620-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW90345.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90345.1}. SQ SEQUENCE 262 AA; 29196 MW; 588F4CFB03278D66 CRC64; MNPQDKCWQV HRHLAEHTDQ RLTLVRNAPG HILLAGADAD ISRSLLAKRY PLAVFEEYDS RADFLAAAAA ARKGGFWQKL TGRGVVQHCQ SPTVPLPEAC ADMLWSNLGL LAAEQILPVL HNWARALKTD GLLFFTCFGR DTLAELKSRL KENGIESRSV MFPDMHDLGD MLAENGFYDP VTDTAKLVLD YKKAETFWAD MDTLGVWRAV AWDDENAARS CAGAIFEREG GLGITLETVY GHAVKKLVLP QGENVVRFFP KR // ID Q5F6W3_NEIG1 Unreviewed; 233 AA. AC Q5F6W3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90074.1}; GN ORFNames=NGO_1431 {ECO:0000313|EMBL:AAW90074.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90074.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90074.1; -; Genomic_DNA. DR RefSeq; WP_003705779.1; NC_002946.2. DR RefSeq; YP_208486.1; NC_002946.2. DR ProteinModelPortal; Q5F6W3; -. DR EnsemblBacteria; AAW90074; AAW90074; NGO_1431. DR GeneID; 3281754; -. DR KEGG; ngo:NGO1431; -. DR PATRIC; 20336281; VBINeiGon24812_1689. DR OrthoDB; EOG664CFG; -. DR BioCyc; NGON242231:GI2G-1339-MONOMER; -. DR Proteomes; UP000000535; 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; 2.40.170.20; -; 1. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. DR InterPro; IPR010917; TonB_rcpt_CS. DR Pfam; PF00593; TonB_dep_Rec; 1. DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT DOMAIN 5 230 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 233 AA; 25731 MW; 49C9857E07ACBBD6 CRC64; MQAIPLLKTE KHNRIRLTAD SRNDYYNGYM NSLAGAGWNV GGTLVADKVK DLIIFDRAHG QSGTASKDGG IITRNVDARL FTAQAYARYN FNPHWAAGIK AAYNYGHNET DGRPPYQIRP FEAAVQADYK NYFAHGSYNI GAATRFVAKQ TRGDFDMASG LGIDKREAAK GFTVADVYAG VNIKDKYGLR LGVNNVFNKK YVEYISGDHV LALSPSVVYA PGRTYWLSLH AAF // ID Q5F704_NEIG1 Unreviewed; 209 AA. AC Q5F704; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Pretoxin HINT domain protein {ECO:0000313|EMBL:AAW90033.1}; GN ORFNames=NGO_1385 {ECO:0000313|EMBL:AAW90033.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90033.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90033.1; -; Genomic_DNA. DR RefSeq; WP_003705819.1; NC_002946.2. DR RefSeq; YP_208445.1; NC_002946.2. DR ProteinModelPortal; Q5F704; -. DR EnsemblBacteria; AAW90033; AAW90033; NGO_1385. DR GeneID; 3281317; -. DR KEGG; ngo:NGO1385; -. DR PATRIC; 20336159; VBINeiGon24812_1628. DR HOGENOM; HOG000219103; -. DR OMA; DEASGKM; -. DR OrthoDB; EOG66F037; -. DR BioCyc; NGON242231:GI2G-1298-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 209 AA; 23236 MW; F8F8BB25B190277C CRC64; MVKTADGYKA IAHIQTGEHV FAKDETSGKT GYKPVTARYG NPYQETVYIK VSDGIGNSQT LISNRIHPFY SDGKWIKAED LKAGSRLLSE SGRTQTVRNT VVKPKPLKAY NLTVADWHTY FVKGNQAETE GVWVHNSCPP KRTGSSKNEK HGDGGRSQIS AESKIAELTN KIIPGMSKNE RLKIKQKIKN IAKNANRKTK GEEHGRRGR // ID Q5F854_NEIG1 Unreviewed; 92 AA. AC Q5F854; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89633.2}; GN ORFNames=NGO_0938 {ECO:0000313|EMBL:AAW89633.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89633.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89633.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89633; AAW89633; NGO_0938. DR PATRIC; 20335061; VBINeiGon24812_1100. DR HOGENOM; HOG000027911; -. DR OMA; QTMLLFV; -. DR OrthoDB; EOG683SBZ; -. DR BioCyc; NGON242231:GI2G-875-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 92 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364416. FT TRANSMEM 34 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 73 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 92 AA; 10634 MW; 0124BC006110B048 CRC64; MSRNLLVRWL AVCLIPLATL AVFAANPPED KPQHLINGII LACEATFLFK FVLFETIKHH LKQGFDLKRQ TMFLFIPIVL LVVYLFHYFG AF // ID Q5F6B9_NEIG1 Unreviewed; 177 AA. AC Q5F6B9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90268.2}; GN ORFNames=NGO_1640 {ECO:0000313|EMBL:AAW90268.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90268.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90268.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6B9; -. DR EnsemblBacteria; AAW90268; AAW90268; NGO_1640. DR PATRIC; 20336818; VBINeiGon24812_1954. DR HOGENOM; HOG000071252; -. DR OrthoDB; EOG61ZTH8; -. DR BioCyc; NGON242231:GI2G-1537-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1330.70; -; 1. DR InterPro; IPR008822; Endonuclease_RusA-like. DR Pfam; PF05866; RusA; 1. DR SUPFAM; SSF103084; SSF103084; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 177 AA; 19216 MW; FBFBCFC2E71246F1 CRC64; MQNLPQQGSP AKARGGGSRR DDGGKAARIH PRRARRLPDI GRRPVDATGR GMRVTRLILP YPVSANRYWR IWRNRAVRSA EAAAYKETVR RIAQGAGAMP SEGAVAVYVR LIPKANKDGG ANKTVIDLDN ALKVTLDALQ GVAYHNDRQV RRIAADYADE PVAGGGLAVE VGELDEK // ID Q5F726_NEIG1 Unreviewed; 467 AA. AC Q5F726; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Multidrug transporter {ECO:0000313|EMBL:AAW90011.1}; GN ORFNames=NGO_1363 {ECO:0000313|EMBL:AAW90011.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90011.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90011.1; -; Genomic_DNA. DR RefSeq; WP_010951247.1; NC_002946.2. DR RefSeq; YP_208423.1; NC_002946.2. DR ProteinModelPortal; Q5F726; -. DR EnsemblBacteria; AAW90011; AAW90011; NGO_1363. DR GeneID; 3282457; -. DR KEGG; ngo:NGO1363; -. DR PATRIC; 20336111; VBINeiGon24812_1604. DR HOGENOM; HOG000111955; -. DR KO; K18139; -. DR OMA; TITKARY; -. DR OrthoDB; EOG6MWN87; -. DR BioCyc; NGON242231:GI2G-1276-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lipoprotein {ECO:0000256|RuleBase:RU362097}; KW Membrane {ECO:0000256|RuleBase:RU362097}; KW Palmitate {ECO:0000256|RuleBase:RU362097}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|RuleBase:RU362097}; KW Transmembrane {ECO:0000256|RuleBase:RU362097}; KW Transmembrane beta strand {ECO:0000256|RuleBase:RU362097}. FT SIGNAL 1 22 {ECO:0000256|RuleBase:RU362097}. FT CHAIN 23 467 {ECO:0000256|RuleBase:RU362097}. FT /FTId=PRO_5001442367. SQ SEQUENCE 467 AA; 50413 MW; 7A92C95EE65581F1 CRC64; MNTTLKTTLT SVAAAFALSA CTMIPQYEQP KVEVAETFQN DTSVSSIRAV DLGWHDYFAD PRLQKLIDIA LERNTSLRTA VLNSEIYRKQ YMIERNNLLP TLAANANGSR QGSLSGGNVS SSYNVGLGAA SYELDLFGRV RSSSEAALQG YFASVANRDA AHLSLIATVA KAYFNERYAE KAMSLAQRVL KTREETYKLS ELRYKAGVIS AVALRQQEAL IESAKADYAH AARSREQARN ALATLINRPI PEDLPAGLPL DKQFFVEKLP AGLSSEVLLD RPDIRAAEHA LKQANANIGA ARAAFFPSIR LTGSVGTGSV ELGGLFKSGT GVWAFAPSIT LPIFTWGTNK ANLDVAKLRQ QAQIVAYESA VQSAFQDVAN ALAAREQLDK AYDALSKQSR ASKEALRLVG LRYKHGVSGA LDLLDAERIS YSAEGAALSA QLTRAENLAD LYKALGGGLK RDTQTGK // ID Q5FAF0_NEIG1 Unreviewed; 106 AA. AC Q5FAF0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88837.1}; GN ORFNames=NGO_0076 {ECO:0000313|EMBL:AAW88837.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88837.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88837.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88837; AAW88837; NGO_0076. DR PATRIC; 20333033; VBINeiGon24812_0100. DR OrthoDB; EOG6423DP; -. DR BioCyc; NGON242231:GI2G-66-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 106 AA; 11809 MW; 40121ACA55F6F823 CRC64; MRSQPEYGIA KENRPNRQAD RFAGSVLPLA ASLTHKPNIM KPIPTDTFQP AILPQAFETE IKSTCTGRIY RIQTATLGEM QSEGYPVLFV LDGEAFFPRC TTSCSR // ID Q5F8D1_NEIG1 Unreviewed; 226 AA. AC Q5F8D1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89556.1}; GN ORFNames=NGO_0852 {ECO:0000313|EMBL:AAW89556.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89556.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89556.1; -; Genomic_DNA. DR RefSeq; WP_010951134.1; NC_002946.2. DR RefSeq; YP_207968.1; NC_002946.2. DR EnsemblBacteria; AAW89556; AAW89556; NGO_0852. DR GeneID; 3282157; -. DR KEGG; ngo:NGO0852; -. DR PATRIC; 20334874; VBINeiGon24812_1007. DR HOGENOM; HOG000218930; -. DR OMA; SERGIWL; -. DR OrthoDB; EOG69D3CQ; -. DR BioCyc; NGON242231:GI2G-798-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 40 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 125 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 137 164 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 176 204 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 226 AA; 24551 MW; 35CEBAD423213A25 CRC64; MIFQTVWFSD VVLSVSWIVL ILILAASAPS AFRSLARYRS ALPLCTVIFS AAWCLNASVG GGQLAQMNYH LLAVNLVTLM VDTSAALWLA ALLMLPYCLL FAGSAGAYPP NALVLILPAL VVNRLSRMLV NRLPPNIFIF IFVNGFLASA AGILLTGLVL IGILDAANAF PSEILWTVAL PVFILLAWAE AFLSGISTAI FVALKPHWIN TFDDNRYLKS ERGIWL // ID Q5F8A8_NEIG1 Unreviewed; 63 AA. AC Q5F8A8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89579.1}; GN ORFNames=NGO_0879 {ECO:0000313|EMBL:AAW89579.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89579.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89579.1; -; Genomic_DNA. DR RefSeq; WP_003688505.1; NC_002946.2. DR RefSeq; YP_207991.1; NC_002946.2. DR EnsemblBacteria; AAW89579; AAW89579; NGO_0879. DR GeneID; 3282498; -. DR KEGG; ngo:NGO0879; -. DR PATRIC; 20334933; VBINeiGon24812_1036. DR OrthoDB; EOG6W4620; -. DR BioCyc; NGON242231:GI2G-821-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 7116 MW; E148807AA5C56986 CRC64; MFFESVIVYQ KEMRQPSAVL IAGNAGRSNR YARTPDKVLK TCLAKQVNGF ANLELPETRN TEI // ID Q5F507_NEIG1 Unreviewed; 148 AA. AC Q5F507; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 60. DE SubName: Full=Glutamyl-tRNA amidotransferase {ECO:0000313|EMBL:AAW90730.2}; GN ORFNames=NGO_2133 {ECO:0000313|EMBL:AAW90730.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90730.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90730.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F507; -. DR EnsemblBacteria; AAW90730; AAW90730; NGO_2133. DR PATRIC; 20338115; VBINeiGon24812_2580. DR HOGENOM; HOG000015154; -. DR OMA; RDSIAQY; -. DR OrthoDB; EOG69SKHS; -. DR BioCyc; NGON242231:GI2G-2024-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90730.2}. FT DOMAIN 4 146 YqeY. {ECO:0000259|Pfam:PF09424}. SQ SEQUENCE 148 AA; 16123 MW; 013E2E0DA7B55591 CRC64; MSLKTRLTED MKTAMRAKDQ VSLGTIRLIN AAVKQFEVDE RTEADDAKIT AILTKMVKQR KDGAKIYTEA GRQDLADKEN AEIDVLHRYL PQMLSAGEIR TAVEAAVAET GAAGMADMGK VMVVLKTRLA GKADMGEVNK ILKTVLTA // ID Q5F5L4_NEIG1 Unreviewed; 408 AA. AC Q5F5L4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AAW90523.1}; GN ORFNames=NGO_1909 {ECO:0000313|EMBL:AAW90523.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90523.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90523.1; -; Genomic_DNA. DR RefSeq; WP_003692100.1; NC_002946.2. DR RefSeq; YP_208935.1; NC_002946.2. DR ProteinModelPortal; Q5F5L4; -. DR EnsemblBacteria; AAW90523; AAW90523; NGO_1909. DR GeneID; 3282264; -. DR KEGG; ngo:NGO1909; -. DR PATRIC; 20337538; VBINeiGon24812_2296. DR HOGENOM; HOG000008425; -. DR KO; K02670; -. DR OMA; ATSPHEF; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NGON242231:GI2G-1812-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 158 310 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 408 AA; 45698 MW; 902A6EFA98E64585 CRC64; MNTDNLHDIL DETVQVYSQK KQSRSETPAE IGTHFHPLLD RLCETAEAQN ASDILISKGF PPSLKINSAL TPQPQKALTG EETAAIAAST MNAEQSEIFR RDGEINYSVQ SRSGTRYRAN AYYSQGSAGL VLRRINHVIP QMRELGLPEK LKDLAVAPRG LLIIVGPTGS GKSTTMATML EHRNKTLPGH IVTIEDPIEF IYKPRRCIFT QREIGVDTIN WQTAVQNAMR QSPDVVCIGE VRSRESMEYA MQLAQTGHLC IFTLHANTAP QSLERILNFY PKEQHNQILI DIALNLTGII CQRLALKKDK TGRTAVVDLL INTPAIQDFI LKGDLMNISK IMETAKTDGM QTMDQNLFEL YRHGIISYEE ALRQSVSANN LRLHIQLHKE GKTPELLYDR VNGLNLIS // ID Q5F7X4_NEIG1 Unreviewed; 502 AA. AC Q5F7X4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 54. DE SubName: Full=Exopolyphosphatase {ECO:0000313|EMBL:AAW89713.1}; GN ORFNames=NGO_1041 {ECO:0000313|EMBL:AAW89713.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89713.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89713.1; -; Genomic_DNA. DR RefSeq; WP_010951166.1; NC_002946.2. DR RefSeq; YP_208125.1; NC_002946.2. DR ProteinModelPortal; Q5F7X4; -. DR EnsemblBacteria; AAW89713; AAW89713; NGO_1041. DR GeneID; 3282578; -. DR KEGG; ngo:NGO1041; -. DR PATRIC; 20335306; VBINeiGon24812_1219. DR HOGENOM; HOG000258672; -. DR KO; K01524; -. DR OMA; HKHSWYL; -. DR OrthoDB; EOG6M6JN6; -. DR BioCyc; NGON242231:GI2G-958-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003695; Ppx_GppA. DR InterPro; IPR030673; PyroPPase_GppA_Ppx. DR Pfam; PF02541; Ppx-GppA; 1. DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 302 Ppx-GppA. {ECO:0000259|Pfam:PF02541}. SQ SEQUENCE 502 AA; 55828 MW; 95A5513D1F85AE27 CRC64; MTTNPANILA SVDLGSNSFR LQICESNNGQ LKVIDSFKQM VRFAAGLDEQ KNLSTSSQEQ ALDCLAKFGE RLRGFRPEQV RAVATNTFRV AKNIADFLPK AEAALGFPIE IIAGREEARL IYTGVIHTLP PCGGKMLVID IGGGSTEFVI GSTLNPDITE SLPLGCVTYS LRFFQNKITA KDFQAAISAA RNEIQRISKN MMREGWDFAV GTSGSAKSIR DVLAAEMPQE ADITYKGMRA LAERIIEAGS VKKAKFENLK PERIEVFAGG LAVMMAAFEE MKLDRMTVTE AALRDGVFYD LIGRGLNEDM RGQTVAEFQH RYHVSLNQAK RTAETAQTFM DSLCHAKNVT VQELALWQQY LGRAAALHEI GLDIAHTGYH KHSAYILENA DMPGFSRKEQ TILAQLVIGH RGDMKKMGGI IGGNEMLWYA VLSLRLAALF CRSRQDLSFP KNMQLRTDTE SCGFILRIDS KWLERHPLIA DALEYESVQW QKINMPFKVE AV // ID Q5FA31_NEIG1 Unreviewed; 220 AA. AC Q5FA31; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 68. DE SubName: Full=Phosphoglycolate phosphatase {ECO:0000313|EMBL:AAW88956.2}; GN ORFNames=NGO_0203 {ECO:0000313|EMBL:AAW88956.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88956.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88956.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FA31; -. DR EnsemblBacteria; AAW88956; AAW88956; NGO_0203. DR PATRIC; 20333339; VBINeiGon24812_0252. DR HOGENOM; HOG000248344; -. DR OMA; EYEADIC; -. DR OrthoDB; EOG6HB9PJ; -. DR BioCyc; NGON242231:GI2G-186-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. 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; TIGR01662; HAD-SF-IIIA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00455242}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 184 HAD-like_dom. {ECO:0000259|Pfam:PF13419}. SQ SEQUENCE 220 AA; 24213 MW; B7FAA4D838F829EA CRC64; MIQAVLFDLD GTLADTALDL GGALNTQLAR HGLPEKSMDE IRTQASHGAA GLLKLGANIT PEHPDYTAWR TEYLEEYDSR YAQDTTLFDG VNELIAELDR RGIKWGIITN KPMRFTDKLV PKLGFAVPPA TVVSGDTCGE PKPSIKPMLH ACGKIHADPQ HTLYVGDAER DIQAGRNAGM KTVLAEWGYI SDEDDTGSWQ ADFHIRTPLD LLECLDKIQP // ID Q5F8B6_NEIG1 Unreviewed; 636 AA. AC Q5F8B6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 84. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW89571.1}; GN ORFNames=NGO_0870 {ECO:0000313|EMBL:AAW89571.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89571.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89571.1; -; Genomic_DNA. DR RefSeq; WP_010951139.1; NC_002946.2. DR RefSeq; YP_207983.1; NC_002946.2. DR ProteinModelPortal; Q5F8B6; -. DR EnsemblBacteria; AAW89571; AAW89571; NGO_0870. DR GeneID; 3281835; -. DR KEGG; ngo:NGO0870; -. DR PATRIC; 20334912; VBINeiGon24812_1026. DR HOGENOM; HOG000271635; -. DR KO; K15738; -. DR OMA; VTSSWWF; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NGON242231:GI2G-813-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89571.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW89571.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 71731 MW; 89C73DAC047D8DAC CRC64; MNILSVENAS FAVGHVALLD KTSFQLDSGE KVGLIGRNGA GKSSFLKILT GVQKLDDGQI IVQNNLKIVY VPQESFFDKD ATVFDTVAEG LGEIRDLLRR YHHVSHELEN GSSELLLKEL NELQLEIEAK DGWKLDAAVK QTLGELGLPE NKKIGNLSGG QKKRVALAQA WVQKPDVLLL DEPTNHLDID AIIWLENLLK AFEGSLVVIT HDRRFLDNIA TRIVELDRGI LRSYPGSFSK YSEKKAQELA VEAEHNRLFD KFHAQEEAWI RKGIEARRTR NEGRVRRLEE LRRQRAERRN VQGQVNFKLD SGKKSGKIIA ELEHASFAYD DKVIMDKFSA ILQRGDKIGL IGPNGIGKTT FLKLILGELQ PTYGRIRIGS KQEVAYFDQF RSALNENDTV FYTLGQGNDY VEVGGKKKHV MSYLEDFLFP PARAQSPVSS LSGGERNRLL LAKLFTRPAN ILVLDEPTND LDIDTQELLE DLLRDYQGTV FLVSHDRMFL DNVITQSIVF EGQGRLKEYI GGYQDYIDAK SREDKIQTAS APKASDVEPA KEKPKANRTV KLSYKEQREL DALPDEIAAL ETEQAEINAQ LSDPGIFKDY EKAGALQNRA EEIEMLLLEK LERWELLETK QNGNAV // ID Q5F6V0_NEIG1 Unreviewed; 222 AA. AC Q5F6V0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90087.1}; GN ORFNames=NGO_1445 {ECO:0000313|EMBL:AAW90087.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90087.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90087.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F6V0; -. DR EnsemblBacteria; AAW90087; AAW90087; NGO_1445. DR PATRIC; 20336309; VBINeiGon24812_1703. DR HOGENOM; HOG000071349; -. DR OMA; YETRANA; -. DR OrthoDB; EOG69SK6G; -. DR BioCyc; NGON242231:GI2G-1352-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR Gene3D; 2.150.10.10; -; 2. DR InterPro; IPR008640; Adhesin_Head_dom. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. DR Pfam; PF05658; YadA_head; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 222 AA; 22826 MW; C024A19C5373E774 CRC64; MGLRQKLRGI IPNLATSIGT SAEANAPGAL ALGGSSEASK KFSIAEGYLA SSDGYGAIAI GSAAKIKQLE KGTINHIVGN DNKGLYVDAD GNVTKITVRT ESEKDILSRY GQTYGAVALG FRSSSHNLFA SSFGAFSTAT AIESLAVGDS SQSTGYRSAT FGSHSRALAE ESLALGYETR ANAYGSVALG AESVANEENT VSVSSDTLKR KIVNVADGTE DL // ID Q5F5A3_NEIG1 Unreviewed; 164 AA. AC Q5F5A3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90634.1}; GN ORFNames=NGO_2026 {ECO:0000313|EMBL:AAW90634.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90634.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90634.1; -; Genomic_DNA. DR RefSeq; WP_003694428.1; NC_002946.2. DR RefSeq; YP_209046.1; NC_002946.2. DR EnsemblBacteria; AAW90634; AAW90634; NGO_2026. DR GeneID; 3282721; -. DR KEGG; ngo:NGO2026; -. DR HOGENOM; HOG000137685; -. DR BioCyc; NGON242231:GI2G-1927-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 164 AA; 18982 MW; ADCB761D52B3BA47 CRC64; MRLTKYPYNS IRELEDYLIN TYQKYIILQE GGKEIYRCFI LSFYKEFNIG IGLAVSCISI PPKVLMLDDK NIFIGFDSVV FCISIQNSKV NILNIDGIVF DIYLLDNQKI CIIHELGAII TDKNLIRENS VSTDIISDWE IDKVNKLIIL KELDSEKIIS LNYD // ID Q5F814_NEIG1 Unreviewed; 250 AA. AC Q5F814; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 66. DE SubName: Full=Cysteine methyltransferase {ECO:0000313|EMBL:AAW89673.2}; GN ORFNames=NGO_0988 {ECO:0000313|EMBL:AAW89673.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89673.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89673.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F814; -. DR EnsemblBacteria; AAW89673; AAW89673; NGO_0988. DR PATRIC; 20335180; VBINeiGon24812_1158. DR HOGENOM; HOG000244137; -. DR OMA; RMITLPS; -. DR OrthoDB; EOG6T1WR0; -. DR BioCyc; NGON242231:GI2G-916-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89673.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89673.2}. FT DOMAIN 80 159 Methyltransf_1N. FT {ECO:0000259|Pfam:PF02870}. FT DOMAIN 163 242 DNA_binding_1. FT {ECO:0000259|Pfam:PF01035}. SQ SEQUENCE 250 AA; 28290 MW; 9D3585AB831557D9 CRC64; MITLPSLNNL PSKWDEIRHC LETRVFECGV MPYPNLTECE AGQFERDFWD NIGCAPEEYV RIRRAIRLLE LRYPDSLNEL VCAAIATPLG EMLAVFGVKG LCLLEFVGQK YLEQEIAAVQ KALRGRFVFR EDGRMQFLRQ ELDLYFKGHL KTFATPLEQI GTEFQKQAWD ALLAIPYGET RSYKEQAQRL GNPKAVRAVA AANGQNKVSV MIPCHRVIGS DGKLTGYAGG LNRKQFLLAL ERGEVQTALF // ID Q5FA73_NEIG1 Unreviewed; 264 AA. AC Q5FA73; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE SubName: Full=3'-5' exonuclease {ECO:0000313|EMBL:AAW88914.1}; GN ORFNames=NGO_0156 {ECO:0000313|EMBL:AAW88914.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88914.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88914.1; -; Genomic_DNA. DR RefSeq; WP_003686851.1; NC_002946.2. DR RefSeq; YP_207326.1; NC_002946.2. DR ProteinModelPortal; Q5FA73; -. DR EnsemblBacteria; AAW88914; AAW88914; NGO_0156. DR GeneID; 3281349; -. DR KEGG; ngo:NGO0156; -. DR PATRIC; 20333237; VBINeiGon24812_0201. DR HOGENOM; HOG000261053; -. DR KO; K07501; -. DR OMA; HLDLMDV; -. DR OrthoDB; EOG6ZWJDD; -. DR BioCyc; NGON242231:GI2G-144-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Exonuclease {ECO:0000313|EMBL:AAW88914.1}; KW Hydrolase {ECO:0000313|EMBL:AAW88914.1}; KW Nuclease {ECO:0000313|EMBL:AAW88914.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 263 DNA_pol_B_exo2. FT {ECO:0000259|Pfam:PF10108}. SQ SEQUENCE 264 AA; 30501 MW; 7F941805BE96CED3 CRC64; MNTILAFDIE TVPDVQGIRT LYDLPSSLPD DEVVLFAQQK RRAQTGGDFM QHHLHQVVAV SCCMRWGQDK VHVGTIGEMD DGEEVVIAKF FELVEKHTPQ LVSWNGGGFD LPVLHYRSLI YGINAARYWD TGDGDFGDSR DFKWNNYISR YHQRHCDLMD LLALYQPRAN VPLDDMAKLC GFPGKLGMDG SKVWEAFHAG RLKEIRNYCE TDAVNTYLMY LRFCLVSGRF DADEYEMEIK RIRNYLSAQT EDKPHWAEFV QAWK // ID Q5F978_NEIG1 Unreviewed; 49 AA. AC Q5F978; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89259.1}; GN ORFNames=NGO_0521 {ECO:0000313|EMBL:AAW89259.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89259.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89259.1; -; Genomic_DNA. DR RefSeq; WP_003689043.1; NC_002946.2. DR RefSeq; YP_207671.1; NC_002946.2. DR EnsemblBacteria; AAW89259; AAW89259; NGO_0521. DR GeneID; 3282928; -. DR KEGG; ngo:NGO0521; -. DR PATRIC; 20334088; VBINeiGon24812_0616. DR HOGENOM; HOG000218908; -. DR OrthoDB; EOG6ZWJNH; -. DR BioCyc; NGON242231:GI2G-499-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5671 MW; DB192F4D7C5BBCE6 CRC64; MNAEGFCEKQ TACRPDGRRN AGDRADLKAF EFAEQELANY REMLKRYAV // ID Q5F5G2_NEIG1 Unreviewed; 124 AA. AC Q5F5G2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90575.1}; GN ORFNames=NGO_1965 {ECO:0000313|EMBL:AAW90575.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90575.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90575.1; -; Genomic_DNA. DR RefSeq; WP_003713021.1; NC_002946.2. DR RefSeq; YP_208987.1; NC_002946.2. DR EnsemblBacteria; AAW90575; AAW90575; NGO_1965. DR GeneID; 3282657; -. DR KEGG; ngo:NGO1965; -. DR PATRIC; 20337685; VBINeiGon24812_2369. DR HOGENOM; HOG000218700; -. DR OrthoDB; EOG6CP3X6; -. DR BioCyc; NGON242231:GI2G-1865-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 124 AA; 14675 MW; B427181018DAAC1E CRC64; MIIQNEFNLY PSNMLPEGFC YPEKYVRISN DTSLIPYIQP HNFHWWFENY GTEGAEVAYI FRNSILPDLN LIPFASNGEW EAYFDGNDVT GNPRVIVINL DNIENHEFFN SFEEWLELAI KDTW // ID Q5F7U8_NEIG1 Unreviewed; 100 AA. AC Q5F7U8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89739.1}; GN ORFNames=NGO_1069 {ECO:0000313|EMBL:AAW89739.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89739.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89739.1; -; Genomic_DNA. DR RefSeq; WP_002234414.1; NC_002946.2. DR RefSeq; YP_208151.1; NC_002946.2. DR EnsemblBacteria; AAW89739; AAW89739; NGO_1069. DR GeneID; 3281784; -. DR KEGG; ngo:NGO1069; -. DR PATRIC; 20335372; VBINeiGon24812_1252. DR HOGENOM; HOG000218704; -. DR OMA; NSINKAM; -. DR OrthoDB; EOG6D2M23; -. DR BioCyc; NGON242231:GI2G-984-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR029080; Imm40. DR Pfam; PF15569; Imm40; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 91 Imm40. {ECO:0000259|Pfam:PF15569}. SQ SEQUENCE 100 AA; 11682 MW; C6420E6863B22F55 CRC64; MLNEIFEIYS RQGESLIGIG IREAALPVPT AIDILNLFIN ERILVLGGDI YIKKDNYFYQ TYDNWYYEGS NLFNSINKAM HYLSQIKLEN AYVSFVLKFI // ID Q5F9E7_NEIG1 Unreviewed; 468 AA. AC Q5F9E7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085}; DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085}; GN ORFNames=NGO_0451 {ECO:0000313|EMBL:AAW89190.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89190.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89190.1; -; Genomic_DNA. DR RefSeq; WP_010951043.1; NC_002946.2. DR RefSeq; YP_207602.1; NC_002946.2. DR ProteinModelPortal; Q5F9E7; -. DR EnsemblBacteria; AAW89190; AAW89190; NGO_0451. DR GeneID; 3282993; -. DR KEGG; ngo:NGO0451; -. DR PATRIC; 20333934; VBINeiGon24812_0541. DR HOGENOM; HOG000113196; -. DR KO; K02314; -. DR OMA; QNMERIV; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; NGON242231:GI2G-428-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89190.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:AAW89190.1}; KW Hydrolase {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAW89190.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362085, KW ECO:0000313|EMBL:AAW89190.1}; KW Primosome {ECO:0000256|RuleBase:RU362085}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 194 461 SF4 helicase. FT {ECO:0000259|PROSITE:PS51199}. SQ SEQUENCE 468 AA; 52185 MW; 157E6758CE4D88D9 CRC64; MNDYAAMPPE GREVGALSLP PHSMEAEQSV LGGLMLENPA WDRIADVVSG EDFYRHEHRL IFRSIAKLIN EGRPADVITV QEDLQRNEEL EAAGGFEYLI TLAQNTPSAA NIRRYAEIVR ERSIMRQLAE VGTEIARSAY NPQGRDAGRL LDEAENKVFQ IAESTAKSKQ GFLEMPDLLK EVVQRIDMLY SRDNPDEVTG VPTGFIDLDK KTSGLQPGDL IIVAGRPSMG KTAFSINIAE YVAIEKHLPV AVFSMEMGGA QLVMRMLGSV GRLDQSVLKT GRLEDEHWGR LNEAVVKLSD APVYIDETPG LTALELRARA RRLARQFNNK LGLIVIDYLQ LMAASGRSDN RASELGEISR SLKALAKELQ VPIIALSQLS RTVEQRTDKR PMMSDLRESG AIEQDADLIM FMYRDEYYNQ DSPMKGLAEC IIGKHRNGPV GKIFLTWTGQ FTKFDNAAYI PEEAKIED // ID Q5F6L1_NEIG1 Unreviewed; 548 AA. AC Q5F6L1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 59. DE SubName: Full=Cytochrome C biogenesis protein CcmE {ECO:0000313|EMBL:AAW90176.1}; GN ORFNames=NGO_1540 {ECO:0000313|EMBL:AAW90176.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90176.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90176.1; -; Genomic_DNA. DR RefSeq; WP_003693549.1; NC_002946.2. DR RefSeq; YP_208588.1; NC_002946.2. DR ProteinModelPortal; Q5F6L1; -. DR EnsemblBacteria; AAW90176; AAW90176; NGO_1540. DR GeneID; 3281506; -. DR KEGG; ngo:NGO1540; -. DR PATRIC; 20336578; VBINeiGon24812_1837. DR HOGENOM; HOG000027890; -. DR OMA; RWGKMET; -. DR OrthoDB; EOG6H1PW4; -. DR BioCyc; NGON242231:GI2G-1442-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 43 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 144 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 175 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 232 495 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 548 AA; 61162 MW; FB30BECA0BAA05CB CRC64; MKQSARIKNM DQTLKNTLGI CALLAFCFGA AIASGYHLEY EYGYRYSAVG ALASVVFLLL LARGFPRVSS VVLLIYVGTT ALYLPVGWLY GAPSYQIVGS ILESNPAEAR EFVGNLPGSL YFVQALFFIF GLTVWKYCVS VGVFADVKNY KRRSKIWLTI LLTLILSCAV MEKIAGDKDW REPDAGLLLN IFDLYYDLAS APAQYAAKRA HILEAAKKAS TWHIRHVAPK YKNYVVVIGE SARSDYMNVY GFPLPDTPFL SRTKGLLING YQSTAHATNL SLPQTLGLPG EPNNNIVSLA KQAGFRTAWL SNQGMLGHFA NEISTYALRS DYPWFTQRGD YGKSAGLSDR LLLPAFKRVL TGNAGTKPRL IVMHLMGSHS DFCTRLDKDA RRFQYQTEKI SCYVSTIAQT DKFLEDTVKI LNENKESWSL VYFSDHGLMH VGKGGERTLT HGEWKRQSYG VPLVKISSDD TRREMIKVRR SAFNFLRGFG SWTGIETDEL PDDGYDFWGN VPDVPGEGNN LAFIDRQSDD PAPWYAGKGK SAKNTSKK // ID Q5FAE1_NEIG1 Unreviewed; 413 AA. AC Q5FAE1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 71. DE SubName: Full=UDP-N-acetylgalactosaminyltransferase {ECO:0000313|EMBL:AAW88846.1}; GN ORFNames=NGO_0085 {ECO:0000313|EMBL:AAW88846.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88846.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:4M98, ECO:0000213|PDB:4M99} RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 197-403. RX PubMed=24064219; DOI=10.1074/jbc.M113.510560; RA Morrison M.J., Imperiali B.; RT "Biochemical analysis and structure determination of bacterial RT acetyltransferases responsible for the biosynthesis of UDP-N,N'- RT diacetylbacillosamine."; RL J. Biol. Chem. 288:32248-32260(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; AE004969; AAW88846.1; -; Genomic_DNA. DR RefSeq; WP_003704933.1; NC_002946.2. DR RefSeq; YP_207258.1; NC_002946.2. DR PDB; 4M98; X-ray; 1.67 A; A=197-403. DR PDB; 4M99; X-ray; 2.60 A; A/B/C=197-403. DR PDBsum; 4M98; -. DR PDBsum; 4M99; -. DR ProteinModelPortal; Q5FAE1; -. DR EnsemblBacteria; AAW88846; AAW88846; NGO_0085. DR GeneID; 3282309; -. DR KEGG; ngo:NGO0085; -. DR PATRIC; 20333057; VBINeiGon24812_0112. DR HOGENOM; HOG000218777; -. DR OMA; IVCDIPD; -. DR OrthoDB; EOG6ZD66R; -. DR BioCyc; NGON242231:GI2G-75-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR003362; Bact_transf. 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 SUPFAM; SSF51161; SSF51161; 1. DR TIGRFAMs; TIGR03570; NeuD_NnaD; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4M98, ECO:0000213|PDB:4M99}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88846.1}; 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; 44266 MW; 81FD30120CBDB73A CRC64; MSKAVKRLFD IIASASGLIV LSPVFLVLIY LIRKNLGSPV FFIRERPGKD GKPFKMVKFR SMRDALDSDG IPLPDSERLT DFGKKLRATS LDELPELWNV LKGEMSLVGP RPLLMQYLPL YNKFQNRRHE MKPGITGWAQ VNGRNALSWD EKFSCDVWYT DNFSFWLDMK ILFLTVKKVL IKEGISAQGE ATMPPFAGNR KLAVIGAGGH GKVVAELAAA LGTYGEIVFL DDRTQGSVNG FPVIGTTLLL ENSLSPEQFD ITVAVGNNRI RRQITENAAA LGFKLPVLIH PDATVSPSAI IGQGSVVMAK AVVQAGSVLK DGVIVNTAAT VDHDCLLDAF VHISPGAHLS GNTRIGEESR IGTGACSRQQ TTVGSGVTAG AGAVIVCDIP DGMTVAGNPA KPLTGKNPKT GTA // ID Q5F5V9_NEIG1 Unreviewed; 154 AA. AC Q5F5V9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90428.1}; GN ORFNames=NGO_1810 {ECO:0000313|EMBL:AAW90428.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90428.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90428.1; -; Genomic_DNA. DR RefSeq; WP_010951354.1; NC_002946.2. DR RefSeq; YP_208840.1; NC_002946.2. DR EnsemblBacteria; AAW90428; AAW90428; NGO_1810. DR GeneID; 3282299; -. DR KEGG; ngo:NGO1810; -. DR PATRIC; 20337272; VBINeiGon24812_2171. DR HOGENOM; HOG000071373; -. DR OMA; DENIHSD; -. DR OrthoDB; EOG6NWBQF; -. DR BioCyc; NGON242231:GI2G-1708-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 154 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256028. SQ SEQUENCE 154 AA; 17051 MW; 11B49FE69982CC72 CRC64; MKRFILPVLL SATTAPASPI VGTWHCIGTD ENIHSDTKVK YLQDGSFRGD AILKIDDDGN ILAYRVVGAG KWRFANNALT QSQIKYGEVS RQHSPETLAW LEKSEDARLL ESMMYTGLVA QMDKPGKDDV YQLDKSGKLV SEDGTSREAC TKVE // ID Q5F6Y3_NEIG1 Unreviewed; 119 AA. AC Q5F6Y3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90054.1}; GN ORFNames=NGO_1410 {ECO:0000313|EMBL:AAW90054.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90054.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90054.1; -; Genomic_DNA. DR RefSeq; WP_003689264.1; NC_002946.2. DR RefSeq; YP_208466.1; NC_002946.2. DR EnsemblBacteria; AAW90054; AAW90054; NGO_1410. DR GeneID; 3281161; -. DR KEGG; ngo:NGO1410; -. DR PATRIC; 20336225; VBINeiGon24812_1661. DR HOGENOM; HOG000277594; -. DR KO; K09790; -. DR OMA; SERLHSW; -. DR OrthoDB; EOG6KMB9V; -. DR BioCyc; NGON242231:GI2G-1319-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 114 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 119 AA; 13781 MW; 110425C2514B6B5B CRC64; MIRYLLIACG GISLLLGIIG IFLPLLPTTP FVLLSAACWA KASPRFHRWL HRHRYFGPMV HNWEQNGAVP RKAKIFAISM MTASCLMMFW QFPQRWWVGA VSSVFCSLVA IWMWRRPES // ID Q5FA66_NEIG1 Unreviewed; 179 AA. AC Q5FA66; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW88921.1}; GN ORFNames=NGO_0165 {ECO:0000313|EMBL:AAW88921.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88921.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88921.1; -; Genomic_DNA. DR RefSeq; WP_003687462.1; NC_002946.2. DR RefSeq; YP_207333.1; NC_002946.2. DR EnsemblBacteria; AAW88921; AAW88921; NGO_0165. DR GeneID; 3281391; -. DR KEGG; ngo:NGO0165; -. DR PATRIC; 20333253; VBINeiGon24812_0209. DR HOGENOM; HOG000218880; -. DR OrthoDB; EOG61P6VJ; -. DR BioCyc; NGON242231:GI2G-151-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 179 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255568. SQ SEQUENCE 179 AA; 19407 MW; 1D9961460754861C CRC64; MKKQITAAVM MLSMIAPAMA NGLDNQAFED QVFHTRADAP MQLAELSQKE MKETEGAFLP LAILGGAAIG MWTQHGFSYA TTGRPASVRD VAGGLGAIPG DVGAAGKVVS FAKYGREIKI GNNMRIAPFG NRTGHPIGKF PHYHRRVTDN TGKTLPGQGI GRHRPWESKS TDRSWKNRF // ID Q5F7K0_NEIG1 Unreviewed; 140 AA. AC Q5F7K0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Endonuclease {ECO:0000313|EMBL:AAW89837.1}; GN ORFNames=NGO_1173 {ECO:0000313|EMBL:AAW89837.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89837.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89837.1; -; Genomic_DNA. DR RefSeq; WP_003691751.1; NC_002946.2. DR RefSeq; YP_208249.1; NC_002946.2. DR ProteinModelPortal; Q5F7K0; -. DR REBASE; 10861; V.NgoAXIV. DR EnsemblBacteria; AAW89837; AAW89837; NGO_1173. DR GeneID; 3281942; -. DR KEGG; ngo:NGO1173; -. DR PATRIC; 20335625; VBINeiGon24812_1376. DR HOGENOM; HOG000239922; -. DR KO; K07458; -. DR OMA; HDCYLFK; -. DR OrthoDB; EOG6VXFGP; -. DR BioCyc; NGON242231:GI2G-1084-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR Gene3D; 3.40.960.10; -; 1. DR InterPro; IPR004603; DNA_mismatch_endonuc_vsr. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF03852; Vsr; 1. DR PIRSF; PIRSF018267; VSR_endonuc; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00632; vsr; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89837.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89837.1}; KW Nuclease {ECO:0000313|EMBL:AAW89837.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 16673 MW; 9A2A36CBA6DF554B CRC64; MTDIFTPSKR SFVMSKIHSK ETKPEVLVRK FLFSQGFRYR KNDKRYAGKP DIVLPKYKTV VFIHGCFWHG HSCNKGHIPK SNMDFWLEKI TKNRERDIKN ETELEKIGFK VIVVWECELK NKAICRERLN RLVEEIKDAV // ID Q5F787_NEIG1 Unreviewed; 60 AA. AC Q5F787; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89950.1}; GN ORFNames=NGO_1296 {ECO:0000313|EMBL:AAW89950.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89950.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89950.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89950; AAW89950; NGO_1296. DR PATRIC; 20335939; VBINeiGon24812_1524. DR HOGENOM; HOG000071324; -. DR OMA; FLRHSFK; -. DR OrthoDB; EOG651T4Q; -. DR BioCyc; NGON242231:GI2G-1208-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 60 AA; 6989 MW; 4D1582D2D541DD12 CRC64; MSLEKNIANL KNPRVLISAF LRHSFKGGNL ETKKQQEFIR NNKTYPPSSP RKRESSLLFK // ID Q5F765_NEIG1 Unreviewed; 172 AA. AC Q5F765; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89972.1}; GN ORFNames=NGO_1321 {ECO:0000313|EMBL:AAW89972.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89972.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89972.1; -; Genomic_DNA. DR RefSeq; WP_003691649.1; NC_002946.2. DR RefSeq; YP_208384.1; NC_002946.2. DR ProteinModelPortal; Q5F765; -. DR EnsemblBacteria; AAW89972; AAW89972; NGO_1321. DR GeneID; 3281817; -. DR KEGG; ngo:NGO1321; -. DR PATRIC; 20336007; VBINeiGon24812_1554. DR HOGENOM; HOG000283606; -. DR KO; K09857; -. DR OMA; IKRPFNI; -. DR OrthoDB; EOG6PZXDB; -. DR BioCyc; NGON242231:GI2G-1235-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 172 AA; 18800 MW; D801D23190BD4B01 CRC64; MRLFPIAAAL TLAACGTVQS TQYFVLPDSR YIRPATQGGE TAVEVRLAEP LKRGGLVYQT DPYRINTAQN HVWADTLDDM LEAALSNAFN RLDSTRTFVP ASRSGSTDKW TVYIDAFQGS YTGKTLISGY AVLPDGTNRP FHIETEQQGD GYAAMTAALE QGLKQAAQQM VE // ID Q5F8I4_NEIG1 Unreviewed; 356 AA. AC Q5F8I4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 52. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89503.1}; GN ORFNames=NGO_0789 {ECO:0000313|EMBL:AAW89503.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89503.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89503.1; -; Genomic_DNA. DR RefSeq; WP_003697066.1; NC_002946.2. DR RefSeq; YP_207915.1; NC_002946.2. DR DNASU; 3281901; -. DR EnsemblBacteria; AAW89503; AAW89503; NGO_0789. DR GeneID; 3281901; -. DR KEGG; ngo:NGO0789; -. DR PATRIC; 20334726; VBINeiGon24812_0935. DR HOGENOM; HOG000245155; -. DR OMA; RGAADTQ; -. DR OrthoDB; EOG6J74SC; -. DR BioCyc; NGON242231:GI2G-743-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 53 Helical. {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; 38825 MW; 2028C7E95717894C CRC64; MYRRKGRGIK PWMGAGAAFA ALVWLVYALG DTLTPFAVAA VLAYVLDPLV EWLQKKGLNR ASASMSVMVF SLILLLALLL IIVPMLVGQF NNLASRLPQL IGFMQNTLLP WLKNTIGGYV EIDQASIIAW FQAHTGELSN ALKAWFPVLM KQGGNIVSSI GNLLLPPLLL YYFLLDWQRW SCGIAKLVPR RFAGAYTRIT GNLNEVLGEF LRGQLLVMLI MGLVYGLGLM LVGLDSGFAI GMVAGILVFV PYLGAFTGLL LATVAALLQF GSWNGILAVW AVFAVGQFLE SFFITPKIVG DRIGLSPFWV IFSLMAFGEL MGFVGMLAGL PLAAVTLVLL REGAQKYFAG SFYRGR // ID Q5F5J9_NEIG1 Unreviewed; 218 AA. AC Q5F5J9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Multidrug MFS transporter {ECO:0000313|EMBL:AAW90538.1}; GN ORFNames=NGO_1925 {ECO:0000313|EMBL:AAW90538.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90538.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90538.1; -; Genomic_DNA. DR RefSeq; WP_002237424.1; NC_002946.2. DR RefSeq; YP_009115487.1; NC_002946.2. DR ProteinModelPortal; Q5F5J9; -. DR DNASU; 3282694; -. DR EnsemblBacteria; AAW90538; AAW90538; NGO_1925. DR GeneID; 22847895; -. DR PATRIC; 20337588; VBINeiGon24812_2321. DR HOGENOM; HOG000093113; -. DR OMA; PWHAMRA; -. DR OrthoDB; EOG6ZPT3P; -. DR BioCyc; NGON242231:GI2G-1828-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 218 AA; 24580 MW; 60A11F94CB688837 CRC64; MNKRLFCSRN GLRYYLLGGF CLSVFPLLLV FASSVWAVYR TGGQVLPPYV RADAALVLGA AAWDKRPSPV FRERINHAIA LYQSRRVGKI VFTGGRTKKG YMTEAEVGRR YALKQGVPAR NILFENTSRN TYENLNNIRP VLRANGIASV VIVSDPYHLA RAAEMAEDLG VRVYMSATPT TRFDAGNKKK IFMLQEGYAL SLYRLEKWGS RFLGWLSD // ID Q5F7S5_NEIG1 Unreviewed; 157 AA. AC Q5F7S5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89762.1}; GN ORFNames=NGO_1095 {ECO:0000313|EMBL:AAW89762.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89762.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89762.1; -; Genomic_DNA. DR RefSeq; WP_010951182.1; NC_002946.2. DR RefSeq; YP_208174.1; NC_002946.2. DR EnsemblBacteria; AAW89762; AAW89762; NGO_1095. DR GeneID; 3281498; -. DR KEGG; ngo:NGO1095; -. DR PATRIC; 20335444; VBINeiGon24812_1288. DR HOGENOM; HOG000137692; -. DR OMA; EENDVIM; -. DR OrthoDB; EOG6H7FR1; -. DR BioCyc; NGON242231:GI2G-1007-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR031876; DUF4760. DR Pfam; PF15956; DUF4760; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 157 AA; 17335 MW; 752B8F68FA9D9853 CRC64; MAGPGTCVAT AYPAFCAYIQ VKQGKHQARQ KAAIGLPVSG GGNPHYRQRR RVCLNMRRNR ENFTSLACKI QEKGEHESKN PVVSDVLNAI GFTAVGIKGG ISGESVYRRM GGGVLADRKT LKPYIMELRR LNNNDRLFCE FERLADRRGN NPSKTGP // ID Q5F6H1_NEIG1 Unreviewed; 138 AA. AC Q5F6H1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90216.1}; GN ORFNames=NGO_1588 {ECO:0000313|EMBL:AAW90216.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90216.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90216.1; -; Genomic_DNA. DR RefSeq; WP_003689511.1; NC_002946.2. DR RefSeq; YP_208628.1; NC_002946.2. DR EnsemblBacteria; AAW90216; AAW90216; NGO_1588. DR GeneID; 3281111; -. DR KEGG; ngo:NGO1588; -. DR PATRIC; 20336702; VBINeiGon24812_1897. DR HOGENOM; HOG000218752; -. DR OMA; YLPMIQT; -. DR OrthoDB; EOG6GFGMB; -. DR BioCyc; NGON242231:GI2G-1484-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 138 AA; 15811 MW; 625D9F5E61232271 CRC64; MKTSTIVFGG FFITDNGERI QIPILENPNI KEINNFFSVS NFEKKAGVLV FRIIPEPEFG NTELTIYFEK GYYLPIIQTI LEDGDIEVKN LKTENYSGNT MEILGDVYPI EHISKNISII QDIISEFIMK NKPITIMI // ID Q5F9B5_NEIG1 Unreviewed; 353 AA. AC Q5F9B5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89222.2}; GN ORFNames=NGO_0484 {ECO:0000313|EMBL:AAW89222.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89222.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89222.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89222; AAW89222; NGO_0484. DR PATRIC; 20334004; VBINeiGon24812_0574. DR HOGENOM; HOG000071250; -. DR OrthoDB; EOG64N9T4; -. DR BioCyc; NGON242231:GI2G-462-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 353 AA; 38707 MW; 19CAD6BD0DE5D998 CRC64; MKPSESLRAA GRPIAYYPKL AKPLGGVNAA ILFGHFFYWN DKTQYESGIY RTAEEIEIET GLSVQEQRTA RAKLRERGVL IETEKRIEHR IYYKLNLDAF DDLMLQHSGG GESTAPKCNI NSPELQNQHS GGGESTAPKC NINSPELQNQ HSGSEESTAV IRTEDLTEDL AVYTPLPPNA GNGKGGLNAD AFVSADAETC GRETGEPTSP KAESDSNGNG GLSGKPKNAN VPRRRKTHGV PLQEIADLYN EVLGGRLPSV QVLNDTRKRA IANRWCEMLG TAAPNGKVRF GDKETGLAWF AGFFRKVAMN PFWMGENQTG FAVGFDWIFK AGNFVKILEW HPPKTNQAAR GRA // ID Q5F8N5_NEIG1 Unreviewed; 259 AA. AC Q5F8N5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:AAW89452.1}; GN ORFNames=NGO_0734 {ECO:0000313|EMBL:AAW89452.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89452.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89452.1; -; Genomic_DNA. DR RefSeq; WP_003688701.1; NC_002946.2. DR RefSeq; YP_207864.1; NC_002946.2. DR ProteinModelPortal; Q5F8N5; -. DR EnsemblBacteria; AAW89452; AAW89452; NGO_0734. DR GeneID; 3282175; -. DR KEGG; ngo:NGO0734; -. DR PATRIC; 20334612; VBINeiGon24812_0878. DR HOGENOM; HOG000265758; -. DR KO; K00528; -. DR OMA; PFIAGQF; -. DR OrthoDB; EOG66F050; -. DR BioCyc; NGON242231:GI2G-692-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 106 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. SQ SEQUENCE 259 AA; 29216 MW; 28E4C4A6ABDAE08B CRC64; MAASPEAKFT EEKILWVKHH TPKLITFAIS RPESYRFKAG QFSRLGFYEG KGFIWRAYSV VSAEYADTLE YFAVLIQDGP MSALFAKMQQ GDTILLDKNA TGFLLPERFP DGKDLVMLCT GSGIAPFLSI LEQPEIRQRF DTVNLIHSVS FPEELIFNDR LAALSEHPLV GEYGHSFRFV PVTTRAANPS GLSGKRIPEL LKNNSIEQAL HTKLTPESTR FMICGNPEMV KDTFQTLLDM GYAMHRNRIP GQIMMENGF // ID Q5FA67_NEIG1 Unreviewed; 121 AA. AC Q5FA67; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88920.1}; GN ORFNames=NGO_0164 {ECO:0000313|EMBL:AAW88920.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88920.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88920.1; -; Genomic_DNA. DR RefSeq; WP_003687460.1; NC_002946.2. DR RefSeq; YP_207332.1; NC_002946.2. DR EnsemblBacteria; AAW88920; AAW88920; NGO_0164. DR GeneID; 3281392; -. DR KEGG; ngo:NGO0164; -. DR PATRIC; 20333251; VBINeiGon24812_0208. DR HOGENOM; HOG000218879; -. DR OMA; DSADMPS; -. DR OrthoDB; EOG6WHNSD; -. DR BioCyc; NGON242231:GI2G-150-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 121 AA; 13917 MW; 2FE591C904049451 CRC64; MEKPLLTPPF FLFEDVSLDI FQGLSELEKK IEPQDLMDDV YRAFDSVGNI LNFRIVEKEQ KGFWVSTKIK TVVFDSADMP SDDLFLKCLQ SSYKAYSETE PAGLDKRQLM KTLIQKCGFS C // ID Q5FA27_NEIG1 Unreviewed; 327 AA. AC Q5FA27; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 60. DE SubName: Full=Sugar transferase {ECO:0000313|EMBL:AAW88960.1}; GN ORFNames=NGO_0207 {ECO:0000313|EMBL:AAW88960.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88960.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88960.1; -; Genomic_DNA. DR RefSeq; WP_003704837.1; NC_002946.2. DR RefSeq; YP_207372.1; NC_002946.2. DR ProteinModelPortal; Q5FA27; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAW88960; AAW88960; NGO_0207. DR GeneID; 3281408; -. DR KEGG; ngo:NGO0207; -. DR PATRIC; 20333351; VBINeiGon24812_0258. DR HOGENOM; HOG000218825; -. DR OMA; EICEGFA; -. DR OrthoDB; EOG6ZSP5C; -. DR BioCyc; MetaCyc:MONOMER-17340; -. DR BioCyc; NGON242231:GI2G-190-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88960.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 278 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 320 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 138 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 327 AA; 37912 MW; FA834D2AB49A8A68 CRC64; MNLSIVVPIY NVESYLEACL NSIEPILSNE NVELILVNDG SKDGSEDICY KYIDKISNTK HQTPNTKYIY QDNQGLSEAR NTGIKNSNGK YIAFIDSDDF INCQVLLDFL GKDDSDMPDV VFLNAVKYDK GRVSYFGEDY QPEKILNQSK VEVLKGLCRF RKFPGSAWNK IIKRELIIRE KLFFEKGIYS EDIEWSMRLF NAATTFSYLD GCYYYYRQGR KDSITGTVSE KGIKSLLYIL EKNAKMEFNR DISSYLYSFL SYEYLVLLFI MTSKNIACDS DIKRRAYHLR FMLLKSNKLI YKLIFPIITL FGVDITGRIL KAIRGNI // ID Q5F583_NEIG1 Unreviewed; 62 AA. AC Q5F583; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90654.1}; GN ORFNames=NGO_2046 {ECO:0000313|EMBL:AAW90654.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90654.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90654.1; -; Genomic_DNA. DR RefSeq; WP_003691964.1; NC_002946.2. DR RefSeq; YP_209066.1; NC_002946.2. DR EnsemblBacteria; AAW90654; AAW90654; NGO_2046. DR GeneID; 3282701; -. DR KEGG; ngo:NGO2046; -. DR PATRIC; 20337887; VBINeiGon24812_2466. DR OrthoDB; EOG65J5B9; -. DR BioCyc; NGON242231:GI2G-1948-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 7085 MW; 82E784A91866DD1A CRC64; MRTASVPHLP FRIINRLPRR KTAKCRLKAW ACSKKGGISP PDRDGRSDGI ACRRFIVFAN QY // ID Q5F7X2_NEIG1 Unreviewed; 114 AA. AC Q5F7X2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAW89715.1}; GN ORFNames=NGO_1043 {ECO:0000313|EMBL:AAW89715.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89715.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89715.1; -; Genomic_DNA. DR RefSeq; WP_010358382.1; NC_002946.2. DR RefSeq; YP_208127.1; NC_002946.2. DR EnsemblBacteria; AAW89715; AAW89715; NGO_1043. DR GeneID; 3282593; -. DR KEGG; ngo:NGO1043; -. DR PATRIC; 20335308; VBINeiGon24812_1220. DR HOGENOM; HOG000027846; -. DR OrthoDB; EOG6JQGXN; -. DR BioCyc; NGON242231:GI2G-960-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000313|EMBL:AAW89715.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 114 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005697330. FT COILED 51 86 {ECO:0000256|SAM:Coils}. FT COILED 88 114 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 114 AA; 11412 MW; 9DE809A47870039B CRC64; MKKLLIAAMM AAALAACSQE AKQEVKEAAQ AVESDVKDTA ASAAESAASA VEEAKGQVKD AAADAKASAE EAVTEAKDAA AETKEAVSEA AKDTLNKAAD AAQEAADKMK DAAK // ID Q5F749_NEIG1 Unreviewed; 256 AA. AC Q5F749; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=Hydrolase {ECO:0000313|EMBL:AAW89988.1}; GN ORFNames=NGO_1338 {ECO:0000313|EMBL:AAW89988.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89988.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89988.1; -; Genomic_DNA. DR RefSeq; WP_010358842.1; NC_002946.2. DR RefSeq; YP_208400.1; NC_002946.2. DR ProteinModelPortal; Q5F749; -. DR EnsemblBacteria; AAW89988; AAW89988; NGO_1338. DR GeneID; 3281928; -. DR KEGG; ngo:NGO1338; -. DR PATRIC; 20336045; VBINeiGon24812_1572. DR HOGENOM; HOG000201521; -. DR KO; K03424; -. DR OMA; DLPVICH; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; NGON242231:GI2G-1252-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89988.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 256 AA; 28126 MW; D22B704B15A04D3D CRC64; MRLTDTHCHL ADSVLRGNLA QVLAEARQAG VWRFIVPATC PQDWQDVAEL SEMPSEHGQI RIALGIHPWF SDGIAEQDFS GLEAVLVRYP RAWVGEIGLD FYDKTQTPPQ RERQIQVFSR QLAIAQTLRR RVIIHNLKAT ADIAAAVKQT GFTQGGIVHA FSGSAEEARV LTKLGFKIGI GSLLLNPNAR KVRDTLKALN DGDFVLETDS PFMLENTVNT PANILRIAEI AAEIRGTGAA EIAAITERNA DSLLRP // ID Q5F8M0_NEIG1 Unreviewed; 218 AA. AC Q5F8M0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 85. DE SubName: Full=XRE family transcriptional regulator {ECO:0000313|EMBL:AAW89467.1}; GN ORFNames=NGO_0752 {ECO:0000313|EMBL:AAW89467.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89467.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89467.1; -; Genomic_DNA. DR RefSeq; WP_003688682.1; NC_002946.2. DR RefSeq; YP_207879.1; NC_002946.2. DR ProteinModelPortal; Q5F8M0; -. DR EnsemblBacteria; AAW89467; AAW89467; NGO_0752. DR GeneID; 3282599; -. DR KEGG; ngo:NGO0752; -. DR PATRIC; 20334650; VBINeiGon24812_0897. DR HOGENOM; HOG000034813; -. DR KO; K07684; -. DR OMA; IRATFHG; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NGON242231:GI2G-707-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000707, KW ECO:0000256|SAAS:SAAS00489599}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 23935 MW; D862980715748E25 CRC64; MTIKIILIDD HTLFRSGIKA LLSRQHGFEV IGEAADGLSG IKMISRLQPD VVLLDLDMPG MNGREALSQI ISINPQQAVI MLTVSEDSDD LTECMRIGAR GYLLKNINAD FLLESIRKAA EGDNVFSPEM TAKLVKSLIS PQPAQRTQAL SSLTPRELEI LGYLAAGHSN KIIARHLDLA ESTVKVHVQN LLRKLNLSSR VQAAVYAIRH NVPQPVPE // ID Q5F9C4_NEIG1 Unreviewed; 66 AA. AC Q5F9C4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89213.1}; GN ORFNames=NGO_0475 {ECO:0000313|EMBL:AAW89213.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89213.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89213.1; -; Genomic_DNA. DR RefSeq; WP_010359988.1; NC_002946.2. DR RefSeq; YP_207625.1; NC_002946.2. DR EnsemblBacteria; AAW89213; AAW89213; NGO_0475. DR GeneID; 3282972; -. DR KEGG; ngo:NGO0475; -. DR PATRIC; 20333988; VBINeiGon24812_0566. DR HOGENOM; HOG000071222; -. DR OrthoDB; EOG6NWC07; -. DR BioCyc; NGON242231:GI2G-453-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 7482 MW; A6349638CB2932B2 CRC64; MNELISRINR FGARAKDEQS LLLKVGEICR DAAATWTTRK SESLNHTAFT FTVKKDGLKE KVMIVL // ID Q5F692_NEIG1 Unreviewed; 286 AA. AC Q5F692; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. 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 ORFNames=NGO_1670 {ECO:0000313|EMBL:AAW90295.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90295.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90295.1; -; Genomic_DNA. DR RefSeq; WP_003689814.1; NC_002946.2. DR RefSeq; YP_208707.1; NC_002946.2. DR EnsemblBacteria; AAW90295; AAW90295; NGO_1670. DR GeneID; 3281275; -. DR KEGG; ngo:NGO1670; -. DR PATRIC; 20336892; VBINeiGon24812_1991. DR HOGENOM; HOG000248584; -. DR KO; K02654; -. DR OMA; VFWLFKL; -. DR OrthoDB; EOG6F55M8; -. DR BioCyc; NGON242231:GI2G-1564-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU003794}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methyltransferase {ECO:0000256|RuleBase:RU003794, KW ECO:0000313|EMBL:AAW90295.1}; KW Multifunctional enzyme {ECO:0000256|RuleBase:RU003794}; KW Protease {ECO:0000256|RuleBase:RU003794}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003794, KW ECO:0000313|EMBL:AAW90295.1}; 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; 31332 MW; A2941E7EDCACE275 CRC64; MSDLSVLSPF AVPLAAVLGL LVGSFLNVVI YRVPVMMERG WTVFAKEHLN LPLTDDESRT FNLMKPDSCC PKCRVPIRAW QNIPIVSYLL LRGKCASCQT KISIRYPLIE LLTGVLFGLV AWQYGWSWIT LGGLILTAFL ISLTFIDADT QYLPDSMTLP LIWLGLIFNL DGGFVPLQSA VLGAVAGYSS LWLLCAVYKL LTGKTGMGNG DFKLIAALGA WLGISALPVL IFVSSLIGLV AAIVMRVAKG RHFAFGPALT VSGWIIFTAN DSVWRAVNWW LTHPVR // ID Q5F7H8_NEIG1 Unreviewed; 1064 AA. AC Q5F7H8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 61. DE SubName: Full=ATP-dependent helicase {ECO:0000313|EMBL:AAW89859.2}; GN ORFNames=NGO_1199 {ECO:0000313|EMBL:AAW89859.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89859.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89859.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7H8; -. DR EnsemblBacteria; AAW89859; AAW89859; NGO_1199. DR PATRIC; 20335697; VBINeiGon24812_1407. DR HOGENOM; HOG000218727; -. DR OMA; NVTTWDI; -. DR OrthoDB; EOG6Q5NPH; -. DR BioCyc; NGON242231:GI2G-1111-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89859.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000313|EMBL:AAW89859.2}; KW Hydrolase {ECO:0000313|EMBL:AAW89859.2}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW89859.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 12 102 HA2. {ECO:0000259|SMART:SM00847}. SQ SEQUENCE 1064 AA; 120498 MW; 8CB21B539A859477 CRC64; MDARSNPANV SDGLQNSSGH IGTNTRYRLT KLGEQMARLP IDPKIARILL AAKKHDCMAE ILVIASALSI QDPRERPLEA RDAAAKAHER FTDKQSDFLT YLNIWDSFQR ERDKGLSNKQ LVQWCRQYFL SHLRMREWRE LHHQLAQTAI EMGLTTKEAA FRRPPEVKQL TSSENAGDQD LSAKLKQKQL DKKQHRTQIR ATKEAGYEQI HRALLTGLIA NVGMKSPDSN DYTGARGSRF HLFPASALFK AKPKWVMAAE LVETTRLYAR DVAVIQPEWI EQEAPHLVRY HYFEPHWEQK RGEVVASERV TFYGLTVLPR RPVSYGKVAP EEAREIFIRS ALVAQEYDLK ADFFVHNKKL IKEITELEHK SRKQDVLVDD EALFAFYHER LPDFYMADSV SEGLCPANPQ QTTPSPVGKG WGEGKTVAAQ TNFSATAANP LPNPLPQERE QSASVSTVSG SLKTMSCEAR LNFCEAKTKT ESSLHSQRLS ENYTPPFSDG LRPANPQQTT PSPVGEGWGE GKTVAAQTNF SATAANPLPQ EREQSASALT VSDDPKPKKQ PASQKGRLKP LPLADIRTFE AWLKTAERDN PRLLFLSRDD LMQHAAAHIT EEQFPKHWQT ADGKFKLSYR FEPHHPLDGV TLTLPLTVLN RISPAALEWL VPGMIREKIQ LQIKALPKQI RRICVPVPEF ITQFLSQNPD RNAPILPQLA QAIAKTAGDI RILEQINQDE WAAFRLPEHC YFNLRIIDDG EQELAMGRDL IQIQQQLGKA ATTTFRDNTQ EFERDNVTAW DIGILPESIK FARGKQQLTG YLGLQKEKDG RIALRLFDTS AAAGHAHRLG VIELMKLQLK EQVKDLNKGI QGFTQAAMLL KHINADTLRD DLTQAVCDRA FIGEDKLPRN EKAFKEQIKR ARSRLPAVKE ALSRYLQETA AAYAELNGKL GKHPLTHLLR LRLQTLLAPG FATRTPWAQW PRLPIYLKAM TLRLEKYSSN PARDAAREAD IQELEQMWQE KTDGLAKQGQ PVSDGLAAFK WMIEELRVSL FAQELKTPYP VSVKRLLKMW EILL // ID Q5FA51_NEIG1 Unreviewed; 256 AA. AC Q5FA51; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. 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 ORFNames=NGO_0181 {ECO:0000313|EMBL:AAW88936.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88936.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88936.1; -; Genomic_DNA. DR RefSeq; WP_003690632.1; NC_002946.2. DR RefSeq; YP_207348.1; NC_002946.2. DR EnsemblBacteria; AAW88936; AAW88936; NGO_0181. DR GeneID; 3281433; -. DR KEGG; ngo:NGO0181; -. DR PATRIC; 20333289; VBINeiGon24812_0227. DR HOGENOM; HOG000245379; -. DR KO; K03118; -. DR OMA; ATQIYKF; -. DR OrthoDB; EOG60SCQS; -. DR BioCyc; NGON242231:GI2G-166-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00902}; KW Protein transport {ECO:0000256|HAMAP-Rule:MF_00902}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 24 44 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 193 213 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. FT TRANSMEM 216 236 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00902}. SQ SEQUENCE 256 AA; 28515 MW; F6C25834095FA084 CRC64; MSETQNEQTV QPLVEHLIEL RRRLMWMVVG ILVCFFGMMP FAQQLYTFIA DPLMANLPKD TSMIATDVIA PFFVPVKVTL MAAFLVSLPH TLYQIWAFVA PALYQNEKRL ITPLVLSSVS LFFIGMAFAY FLVFPVIFKF LAGVTPVGVN MATDIDKYLS FILGMFVAFG TAFEVPIVVI LLTKIGAVTT EQLKHARPYV IVGAFVVAAV ITPPDIISQT LLAIPLILLY EAGIWFGRFF TPRSEQDGDI QPPAKT // ID Q5F7R7_NEIG1 Unreviewed; 111 AA. AC Q5F7R7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89770.2}; GN ORFNames=NGO_1103 {ECO:0000313|EMBL:AAW89770.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89770.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89770.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7R7; -. DR EnsemblBacteria; AAW89770; AAW89770; NGO_1103. DR HOGENOM; HOG000071253; -. DR OMA; FIGCIEM; -. DR OrthoDB; EOG6XSZW4; -. DR BioCyc; NGON242231:GI2G-1015-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.10.3790.10; -; 1. DR InterPro; IPR008711; Recombinase_NinB. DR Pfam; PF05772; NinB; 1. DR SUPFAM; SSF103370; SSF103370; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 111 AA; 13400 MW; A35864AA02F7A4A9 CRC64; MRSIWDSPDG WFENGNLEIT IRPRKSKRSV EQNRRLWFLY REISEKVFID GRRFSQDVWH EFLKRKFIGC IEMPNGQLMG ISTTKLSVRE MSEYQEKIIS WASMEHGVLW D // ID Q5F8I9_NEIG1 Unreviewed; 59 AA. AC Q5F8I9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89498.2}; GN ORFNames=NGO_0784 {ECO:0000313|EMBL:AAW89498.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89498.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89498.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89498; AAW89498; NGO_0784. DR PATRIC; 20334714; VBINeiGon24812_0929. DR HOGENOM; HOG000071288; -. DR OMA; DIMFWIK; -. DR OrthoDB; EOG6130KD; -. DR BioCyc; NGON242231:GI2G-738-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 7059 MW; 1561D9E89C5BBD8C CRC64; MMKKQENFWD KLGDLLFAPV DIMFWIKKVW AAYPVCRLPV IVLKVNVFPN TGYTYNCFR // ID Q5F6V1_NEIG1 Unreviewed; 53 AA. AC Q5F6V1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90086.2}; GN ORFNames=NGO_1444 {ECO:0000313|EMBL:AAW90086.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90086.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90086.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90086; AAW90086; NGO_1444. DR PATRIC; 20336307; VBINeiGon24812_1702. DR HOGENOM; HOG000071348; -. DR OMA; IRIKIFA; -. DR OrthoDB; EOG6TBHRF; -. DR BioCyc; NGON242231:GI2G-1351-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 5922 MW; ED2B1A15465145EF CRC64; MVGKNKKEAY FNGNPAAPPH ILPAKPYRIP PRCGRILHIP AIRIKIFAFP TLS // ID Q5F652_NEIG1 Unreviewed; 332 AA. AC Q5F652; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 71. 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 ORFNames=NGO_1714 {ECO:0000313|EMBL:AAW90335.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90335.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90335.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F652; -. DR EnsemblBacteria; AAW90335; AAW90335; NGO_1714. DR PATRIC; 20337020; VBINeiGon24812_2050. DR HOGENOM; HOG000219125; -. DR OMA; APNATHE; -. DR OrthoDB; EOG6M9DS4; -. DR BioCyc; NGON242231:GI2G-1610-MONOMER; -. DR Proteomes; UP000000535; 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; IPR027304; Trigger_fact/SurA_dom. DR SUPFAM; SSF109998; SSF109998; 1. DR PROSITE; PS01096; PPIC_PPIASE_1; 1. DR PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 21 332 Peptidylprolyl isomerase. FT {ECO:0000256|RuleBase:RU363014}. FT /FTId=PRO_5006528992. FT DOMAIN 190 288 PpiC. {ECO:0000259|PROSITE:PS50198}. SQ SEQUENCE 332 AA; 35805 MW; AE728E236116F57F CRC64; MKIKALMIAA ALLAAADVHA APQKAKTAPA KAVKAAATAQ KEAAPAQQQG GIRFSDGIAV VADNEVITNR RLAEAVAEAK ATLPEDAQIS ESELSRQVLM QLVNQSLIVQ AGKRRNIQAS EAEIDAVVAQ NPALKNLSPT QRRELADNII AEKVRQQAVM QNSRVSEAEI DAFLEQAQKQ GITLPEGAPL RQYRAQHILI KADSKNAAVG AESTIRKIYD QARNGTDFAG LARRYSQDAS AGNGGDLGWF ADGVMVPAFE EAVHALKPGQ VGAPVRTQFG WHIIKLNEVR DAGTPEERIR NSVRQYIFQQ KAGQATVNLL RDLHSGAYVD IR // ID Q5F8J5_NEIG1 Unreviewed; 144 AA. AC Q5F8J5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89492.1}; GN ORFNames=NGO_0778 {ECO:0000313|EMBL:AAW89492.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89492.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89492.1; -; Genomic_DNA. DR RefSeq; WP_003688638.1; NC_002946.2. DR RefSeq; YP_207904.1; NC_002946.2. DR EnsemblBacteria; AAW89492; AAW89492; NGO_0778. DR GeneID; 3281948; -. DR KEGG; ngo:NGO0778; -. DR PATRIC; 20334702; VBINeiGon24812_0923. DR HOGENOM; HOG000218961; -. DR OrthoDB; EOG67X1VD; -. DR BioCyc; NGON242231:GI2G-732-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 45 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 144 AA; 16079 MW; F879D3E464741C39 CRC64; MTEPKHETPT EEQVAARKKA KAKIRTIRIW AWVILALLAS TALLSQCAMS KPQAKQKIVE SCMKNIPFAE KWQNDLKARG LDADNTRLAV DYCKCMWEQP LDGLSEKQIS SFGKLGAQEQ LDLLGGANAF ETRDKQCVAD LKAD // ID Q5F826_NEIG1 Unreviewed; 61 AA. AC Q5F826; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Cytochrome oxidase maturation protein Cbb3 {ECO:0000313|EMBL:AAW89661.1}; GN ORFNames=NGO_0975 {ECO:0000313|EMBL:AAW89661.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89661.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89661.1; -; Genomic_DNA. DR RefSeq; WP_003688317.1; NC_002946.2. DR RefSeq; YP_208073.1; NC_002946.2. DR EnsemblBacteria; AAW89661; AAW89661; NGO_0975. DR GeneID; 3282873; -. DR KEGG; ngo:NGO0975; -. DR PATRIC; 20335144; VBINeiGon24812_1141. DR HOGENOM; HOG000277965; -. DR OMA; AILMDDD; -. DR OrthoDB; EOG6H1Q79; -. DR BioCyc; NGON242231:GI2G-903-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 61 AA; 7075 MW; E0A928A869E01D79 CRC64; MESMFILVPI SIILAFVIGW FFWWSGKNGQ FDDLEGPAHR ILMDDDSTSK LIEKEKENDG R // ID Q5F8W0_NEIG1 Unreviewed; 462 AA. AC Q5F8W0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 78. DE SubName: Full=RNA helicase {ECO:0000313|EMBL:AAW89377.1}; GN ORFNames=NGO_0650 {ECO:0000313|EMBL:AAW89377.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89377.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89377.1; -; Genomic_DNA. DR RefSeq; WP_003688859.1; NC_002946.2. DR RefSeq; YP_207789.1; NC_002946.2. DR ProteinModelPortal; Q5F8W0; -. DR EnsemblBacteria; AAW89377; AAW89377; NGO_0650. DR GeneID; 3282557; -. DR KEGG; ngo:NGO0650; -. DR PATRIC; 20334388; VBINeiGon24812_0766. DR HOGENOM; HOG000268807; -. DR OMA; PMQAEDY; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; NGON242231:GI2G-617-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89377.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:AAW89377.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAW89377.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAW89377.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 51139 MW; C597EC90BC3EBB41 CRC64; MSIKFADLNL DKNILSAVSS EGYESPTPIQ AQAIPFALEG CDIMASAQTG SGKTAAFLLP TLQRLTKRSE KPGKGPRALV LAPTRELAAQ VEKNALAYAK NMRWFRTVSI VGGTSFGYQT RALSKPVDLI VATPGRLTDL MQSGKVDFER LEVLILDEAD RMLDMGFIDD IETIVEATPA DRQTLLFSAT WDGAVGKLAR KLTKDSEIIE VERVDGQGKI EEQLLYCDDM RHKNRLLDHI LRDANIDQCV IFTSTKAMTE VIADELYEKG FAANCLHGDM PQGWRNRTLT DLRKGRCKIL VATDVAARGI DVPTITHVIN YDLPKQAEDY VHRIGRTGRA GRTGIAITFA EVNEYVKVHK IEKYINRKLP ELTIEGMEPA RKRKSAGGKP KGKGGWGDRK SGGRRGDHKP GKEGFGGKTR GEGFKKEGFK KDSFKKTGEG FKGKRKAGDS FAGKSERRYK DR // ID Q5F9E9_NEIG1 Unreviewed; 110 AA. AC Q5F9E9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=General secretion pathway protein GspG {ECO:0000313|EMBL:AAW89188.1}; GN ORFNames=NGO_0448 {ECO:0000313|EMBL:AAW89188.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89188.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89188.1; -; Genomic_DNA. DR RefSeq; WP_003687908.1; NC_002946.2. DR RefSeq; YP_207600.1; NC_002946.2. DR EnsemblBacteria; AAW89188; AAW89188; NGO_0448. DR GeneID; 3281655; -. DR KEGG; ngo:NGO0448; -. DR PATRIC; 20333924; VBINeiGon24812_0536. DR HOGENOM; HOG000218892; -. DR OrthoDB; EOG6MPWXT; -. DR BioCyc; NGON242231:GI2G-426-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 12075 MW; 7E24D02199C15029 CRC64; MQILSFQADI AERMLEGTEG ESVNENAQFV RTDNGYWIAW HEGVAALLAP DTPPGIPCFW VEGAESLEEL CAMVERGEFD EVEEFDGDDD AWLEAAKDCG HHGDACACGH // ID Q5F7C3_NEIG1 Unreviewed; 113 AA. AC Q5F7C3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89914.1}; GN ORFNames=NGO_1255 {ECO:0000313|EMBL:AAW89914.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89914.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89914.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89914; AAW89914; NGO_1255. DR BioCyc; NGON242231:GI2G-1172-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 113 AA; 12961 MW; DC39C9D296F3DC31 CRC64; MNTKTELQKL LEEDISTLKE TLIRVDALPP RYVRSIATPI VRRWLIDKQL NILAKEIGLT IELPILDTSL VFEKLSTLEN KVNFYSRLTK IRTRRRAADS TNSTARRGNA VPV // ID Q5F649_NEIG1 Unreviewed; 234 AA. AC Q5F649; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 72. DE SubName: Full=DSBA oxidoreductase {ECO:0000313|EMBL:AAW90338.1}; GN ORFNames=NGO_1717 {ECO:0000313|EMBL:AAW90338.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90338.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90338.1; -; Genomic_DNA. DR RefSeq; WP_010951331.1; NC_002946.2. DR RefSeq; YP_208750.1; NC_002946.2. DR ProteinModelPortal; Q5F649; -. DR EnsemblBacteria; AAW90338; AAW90338; NGO_1717. DR GeneID; 3281356; -. DR KEGG; ngo:NGO1717; -. DR PATRIC; 20337026; VBINeiGon24812_2053. DR HOGENOM; HOG000265318; -. DR KO; K03673; -. DR OMA; NAIHKQK; -. DR OrthoDB; EOG68Q0Q6; -. DR BioCyc; NGON242231:GI2G-1613-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256196. FT DOMAIN 28 231 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 77 80 Redox-active. FT {ECO:0000256|PIRSR:PIRSR001488-1}. SQ SEQUENCE 234 AA; 25420 MW; 34DAF6D65ECC5A15 CRC64; MKSRHLALAL GVAALFALAA CDSKVQTSVP ADSAPAASAA AAPAGLVEGQ NYTVLANPIP QQQAGKVEVL EFFGYFCPHC ARLEPVLSKH AKSFKDDMYL RTEHVVWQKE MLPLARLAAA VDMAAAESKD VANSHIFDAM VNQKIKLQEP EVLKKWLGEQ TAFDGKKVLA AYESPESQAR AGKMQELTET FQIDGTPTVI VGGKYKVEFA DWESGMNTID LLADKVREEQ KAAQ // ID Q5F8D5_NEIG1 Unreviewed; 220 AA. AC Q5F8D5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89552.1}; GN ORFNames=NGO_0847 {ECO:0000313|EMBL:AAW89552.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89552.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89552.1; -; Genomic_DNA. DR RefSeq; WP_003688556.1; NC_002946.2. DR RefSeq; YP_207964.1; NC_002946.2. DR ProteinModelPortal; Q5F8D5; -. DR EnsemblBacteria; AAW89552; AAW89552; NGO_0847. DR GeneID; 3282220; -. DR KEGG; ngo:NGO0847; -. DR PATRIC; 20334862; VBINeiGon24812_1001. DR HOGENOM; HOG000218931; -. DR KO; K07039; -. DR OMA; ANLMDDM; -. DR OrthoDB; EOG6N0HM6; -. DR BioCyc; NGON242231:GI2G-794-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 220 AA; 24724 MW; C33266B3C7762AD4 CRC64; MDSRKFTEAS KRRLGELLDA KSEQGNTMRC DEVQGFMTAL LSGPDKLAPL DWLPEVLGDE SQFTAAERSE IERLVLAMAM ETTAAMSDKK LPDLWLYDDG EGGSDFYTWC NAYLYGLDIV PTDWFEAADD EAFEELFYPV MALGGIYDEE ENGAIRLQFT EGELAELASE LPYALADIYR YWQAVINKPQ TVRREGEKTG RNDPCPCGSG RKYKACCGKN // ID Q5F933_NEIG1 Unreviewed; 598 AA. AC Q5F933; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 59. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89304.1}; GN ORFNames=NGO_0571 {ECO:0000313|EMBL:AAW89304.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89304.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89304.1; -; Genomic_DNA. DR RefSeq; WP_010951085.1; NC_002946.2. DR RefSeq; YP_207716.1; NC_002946.2. DR ProteinModelPortal; Q5F933; -. DR EnsemblBacteria; AAW89304; AAW89304; NGO_0571. DR GeneID; 3282528; -. DR KEGG; ngo:NGO0571; -. DR PATRIC; 20334206; VBINeiGon24812_0675. DR HOGENOM; HOG000218993; -. DR OMA; PEKFART; -. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; NGON242231:GI2G-544-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 598 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256074. FT DOMAIN 502 593 Peptidase_M23. FT {ECO:0000259|Pfam:PF01551}. FT COILED 183 238 {ECO:0000256|SAM:Coils}. FT COILED 320 361 {ECO:0000256|SAM:Coils}. FT COILED 387 455 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 598 AA; 65943 MW; 3CB46C3ACF089E20 CRC64; MRYKPLLLAL MLVFSTPAVA AHDAAHNRSA EVKKQAKNKK EQPEAAEGKK EKGKNAAVKD KKTGGKEAAK EFKKTAKNRK EAEKEATSRQ SARKGREGDK ESKAEHKKAH GKPVSGSKEK NAKTQPENKQ GKKGAKGQGN PRKGGKAEKD TVSANKKARS DKNGKAVKQD KKHTEEKNAK TDSDELKAAV AAATNDVENK KALLKQSEGM LLHVSNSLKQ LQEERIRQER IRQERIRQAR GNLASVNRKQ REAWDKFQKL NTELNRLKTE VAATKAQISR FVSGNYKNSR PNAVALFLKN AEPGQKNRFL RYTRYVNASN REVVKDLEKQ QKALAVQEQK INNELARLKK IQANVQSLLK KQGVTDAAEQ TESRRQNAKI SKDARKLLEQ KGNEQQLNKL LSNLEKKKAE HRIQDAEAKR KLAEAKLAAA EKARKEAAQQ KAEARRAEMS NLTAEDRNIQ APSVMGIGSA DGFSRMQGRL KKPVDGVPTG LFGQNRSGGD VWKGVFYSTA PATVESIAPG TVSYADELDG YGKVVVIDHG ENYISIYAGL SEISAGKGYT VAAGSKIGTS GSLPDGEEGL YLQIRYRGQV LNPSGWIR // ID Q5F4X4_NEIG1 Unreviewed; 83 AA. AC Q5F4X4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90763.1}; GN ORFNames=NGO_2170 {ECO:0000313|EMBL:AAW90763.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90763.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90763.1; -; Genomic_DNA. DR RefSeq; WP_003687181.1; NC_002946.2. DR RefSeq; YP_209175.1; NC_002946.2. DR EnsemblBacteria; AAW90763; AAW90763; NGO_2170. DR GeneID; 3282755; -. DR KEGG; ngo:NGO2170; -. DR PATRIC; 20338200; VBINeiGon24812_2622. DR HOGENOM; HOG000218753; -. DR OMA; DILCTYI; -. DR OrthoDB; EOG6GN75X; -. DR BioCyc; NGON242231:GI2G-2057-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 83 AA; 9950 MW; 68F8EAFCDA76123B CRC64; MKTLEKRMKA LDKRMMKFGK SLEGRLDARL IESALDYIHY SERFLAFDIL CTYIEDFDIR LTEQESREIS FINKEFEIES TSD // ID Q5F7W5_NEIG1 Unreviewed; 79 AA. AC Q5F7W5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89722.1}; GN ORFNames=NGO_1051 {ECO:0000313|EMBL:AAW89722.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89722.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89722.1; -; Genomic_DNA. DR RefSeq; WP_003688189.1; NC_002946.2. DR RefSeq; YP_208134.1; NC_002946.2. DR EnsemblBacteria; AAW89722; AAW89722; NGO_1051. DR GeneID; 3282604; -. DR KEGG; ngo:NGO1051; -. DR PATRIC; 20335332; VBINeiGon24812_1232. DR OrthoDB; EOG651T4M; -. DR BioCyc; NGON242231:GI2G-967-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 79 AA; 9333 MW; 1F764CB7E7FD645F CRC64; MILFFKPHSI RLKKAARIRK ANVQLNKDIV IILFFKNLIG TSPGFQTLAR PRHKIRKHRP KNLLRLLIIY TLEALCKRC // ID Q5F567_NEIG1 Unreviewed; 247 AA. AC Q5F567; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Acyl-phosphate glycerol 3-phosphate acyltransferase {ECO:0000313|EMBL:AAW90670.1}; GN ORFNames=NGO_2069 {ECO:0000313|EMBL:AAW90670.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90670.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90670.1; -; Genomic_DNA. DR RefSeq; WP_003687014.1; NC_002946.2. DR RefSeq; YP_209082.1; NC_002946.2. DR ProteinModelPortal; Q5F567; -. DR EnsemblBacteria; AAW90670; AAW90670; NGO_2069. DR GeneID; 3282848; -. DR KEGG; ngo:NGO2069; -. DR PATRIC; 20337969; VBINeiGon24812_2507. DR HOGENOM; HOG000026377; -. DR KO; K00655; -. DR OMA; FIQMILY; -. DR OrthoDB; EOG6XHC27; -. DR BioCyc; NGON242231:GI2G-1964-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90670.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90670.1}; 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; 27948 MW; 2B024542E862D1FE CRC64; MLIIRNLIYW LILCSSLIFL FPFMLLASPF RDGAHKMARV WVGILNWSLK HIVGLKYRII GAEHIPDRPS VICAKHQSGW ETLALQEIFP PQVYVAKREL FKIPFFGWGL KLVKTIGIDR NNRREANEQL IKQGLARKNE GYWITIFPEG TRLAPGKRGK YKLGGARMAK MFEMDIVPVA LNSGEFWPKN SFLKYPGEIT VIICPTIPHA SGSEAELMEK CEHLIETQQP LISGAGPFAA EMPSETA // ID Q5F6C3_NEIG1 Unreviewed; 205 AA. AC Q5F6C3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE SubName: Full=Putative DNA replication protein, putative phage associated protein {ECO:0000313|EMBL:AAW90264.1}; GN ORFNames=NGO_1636 {ECO:0000313|EMBL:AAW90264.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90264.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90264.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F6C3; -. DR DNASU; 3281380; -. DR EnsemblBacteria; AAW90264; AAW90264; NGO_1636. DR PATRIC; 20336808; VBINeiGon24812_1949. DR HOGENOM; HOG000120230; -. DR OMA; EYGLHDR; -. DR OrthoDB; EOG6TR0C9; -. DR BioCyc; NGON242231:GI2G-1533-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR002611; IstB_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01695; IstB_IS21; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 67 194 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 205 AA; 22151 MW; CA11C93E852E3995 CRC64; MAAYAETLRR GAMRDALEKR IGRSGIAPRF RNCRIENYAV SDSIPGMARA KAAAAEYAAN FADVLQTGRS MIFSGRRGTG KNHLACGIAR EVIAAGKSAL VITVGDMLRT VKDSFGGGGE AGAVGIFVKP DLLVLDEFGA GSLSETDGRI LFSVVNARYE RLMPMLVLTN LTAEAFRENT DARIRDRLRD GGGKLIPFDW ESYRA // ID Q5FA26_NEIG1 Unreviewed; 176 AA. AC Q5FA26; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Anhydrase {ECO:0000313|EMBL:AAW88961.1}; GN ORFNames=NGO_0208 {ECO:0000313|EMBL:AAW88961.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88961.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88961.1; -; Genomic_DNA. DR RefSeq; WP_003687524.1; NC_002946.2. DR RefSeq; YP_207373.1; NC_002946.2. DR ProteinModelPortal; Q5FA26; -. DR EnsemblBacteria; AAW88961; AAW88961; NGO_0208. DR GeneID; 3281351; -. DR KEGG; ngo:NGO0208; -. DR PATRIC; 20333353; VBINeiGon24812_0259. DR HOGENOM; HOG000049430; -. DR OMA; FFPYSAG; -. DR OrthoDB; EOG65XN5M; -. DR BioCyc; NGON242231:GI2G-191-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 176 AA; 19044 MW; F4B0B79E946F03F5 CRC64; MNAIRTFQNR TPEIHETCMI DEACVVIGEV SLAEDVSVWP CAVLRGDVNS ITVGARSNIQ DGSVLHVSHK TAAKPEGSPL VIGEDVTVGH KVMLHGCRIG NRVLVGMGST VLDDAVIEDD VMIGAGSLVP PRKRLEGGYL YIGSPVRQVR LLTDEEKAFL KYSAAHYVKL SKQYGM // ID Q5F7E1_NEIG1 Unreviewed; 217 AA. AC Q5F7E1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=AhpC/TSA family protein {ECO:0000313|EMBL:AAW89896.1}; GN ORFNames=NGO_1237 {ECO:0000313|EMBL:AAW89896.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89896.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89896.1; -; Genomic_DNA. DR RefSeq; WP_003692227.1; NC_002946.2. DR RefSeq; YP_208308.1; NC_002946.2. DR ProteinModelPortal; Q5F7E1; -. DR EnsemblBacteria; AAW89896; AAW89896; NGO_1237. DR GeneID; 3282589; -. DR KEGG; ngo:NGO1237; -. DR PATRIC; 20335793; VBINeiGon24812_1456. DR HOGENOM; HOG000258139; -. DR KO; K07152; -. DR OMA; KHAGRDY; -. DR OrthoDB; EOG6S26DB; -. DR BioCyc; NGON242231:GI2G-1149-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256053. FT DOMAIN 54 217 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 217 AA; 23107 MW; C6623B3BBE2247B7 CRC64; MFSVPRSFLP GVFVLAALAA CKPQDNSAAQ AASSSASAPA AENAAKPQTR GTDMRKEDIG GDFTLTDGEG KPFSLSDLKG KVVILSFGFT HCPDVCPTGL LTYSDTLKQL GGQAKDVKVV FVSIDPERDT PEIIGKYAKQ FNPDFIGLTA TGGQNLPVIK QQYRVVSAKI NQKDDSENYL VDHSSGAYLI DKNGEVAIFS PYGSEPETIA ADVRTLL // ID Q5FA06_NEIG1 Unreviewed; 128 AA. AC Q5FA06; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88981.1}; GN ORFNames=NGO_0228 {ECO:0000313|EMBL:AAW88981.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88981.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88981.1; -; Genomic_DNA. DR RefSeq; WP_010357075.1; NC_002946.2. DR RefSeq; YP_207393.1; NC_002946.2. DR EnsemblBacteria; AAW88981; AAW88981; NGO_0228. DR GeneID; 3281465; -. DR KEGG; ngo:NGO0228; -. DR PATRIC; 20333399; VBINeiGon24812_0281. DR HOGENOM; HOG000218830; -. DR OMA; CQAINIT; -. DR OrthoDB; EOG62ZHWC; -. DR BioCyc; NGON242231:GI2G-212-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 128 AA; 15074 MW; 996D1B8828865C40 CRC64; MWKIYKENST DLNFAIGSIY CQAINLTEFK MWVEKIIREV DLHEIPNYFF DLIDFQSLYD LIDIIGFVPE NNLSKNQDNA LTGIAFLRGI DVYDPPISKE KALKALEKHP EIYQKFQHFF PFVELPPL // ID Q5F6D1_NEIG1 Unreviewed; 60 AA. AC Q5F6D1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90256.1}; GN ORFNames=NGO_1628 {ECO:0000313|EMBL:AAW90256.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90256.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90256.1; -; Genomic_DNA. DR RefSeq; WP_003689143.1; NC_002946.2. DR RefSeq; YP_208668.1; NC_002946.2. DR ProteinModelPortal; Q5F6D1; -. DR EnsemblBacteria; AAW90256; AAW90256; NGO_1628. DR GeneID; 3281389; -. DR KEGG; ngo:NGO1628; -. DR HOGENOM; HOG000219175; -. DR OMA; GSHHHFR; -. DR OrthoDB; EOG6Q5P24; -. DR BioCyc; NGON242231:GI2G-1525-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003729; F:mRNA binding; IEA:InterPro. DR InterPro; IPR012933; HicA_mRNA_interferase. DR Pfam; PF07927; HicA_toxin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 60 AA; 6688 MW; C67CA1D548BBE59B CRC64; MNSLDVIALL KQDGWYKVAQ SGSHSQYKHP TKKGRVTVPH PKKDLPTGTV KNIYKQAGLK // ID Q5F7J5_NEIG1 Unreviewed; 112 AA. AC Q5F7J5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE SubName: Full=Nitrogen regulatory protein P-II 1 {ECO:0000313|EMBL:AAW89842.1}; GN ORFNames=NGO_1182 {ECO:0000313|EMBL:AAW89842.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89842.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89842.1; -; Genomic_DNA. DR RefSeq; WP_002218119.1; NC_002946.2. DR RefSeq; YP_208254.1; NC_002946.2. DR ProteinModelPortal; Q5F7J5; -. DR SMR; Q5F7J5; 1-112. DR EnsemblBacteria; AAW89842; AAW89842; NGO_1182. DR GeneID; 3281822; -. DR KEGG; ngo:NGO1182; -. DR PATRIC; 20335661; VBINeiGon24812_1389. DR HOGENOM; HOG000017847; -. DR KO; K04751; -. DR OMA; AIEVKGF; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NGON242231:GI2G-1094-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR602187-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 12297 MW; CD893CF2527A485F CRC64; MKKIEAIVKP FKLDDVREAL TEIGITGMTV SEVKGFGRQK GHTEIYRGAE YAVDFLPKVK IELVLADDAV ERAIDVIVEV ARSGKIGDGK IFVLPVEEAI RIRTGERSDA AV // ID Q5F868_NEIG1 Unreviewed; 125 AA. AC Q5F868; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:AAW89619.1}; GN ORFNames=NGO_0923 {ECO:0000313|EMBL:AAW89619.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89619.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89619.1; -; Genomic_DNA. DR RefSeq; WP_003688393.1; NC_002946.2. DR RefSeq; YP_208031.1; NC_002946.2. DR ProteinModelPortal; Q5F868; -. DR EnsemblBacteria; AAW89619; AAW89619; NGO_0923. DR GeneID; 3281694; -. DR KEGG; ngo:NGO0923; -. DR PATRIC; 20335029; VBINeiGon24812_1084. DR HOGENOM; HOG000160252; -. DR KO; K00241; -. DR OMA; IVKFIVW; -. DR OrthoDB; EOG647V36; -. DR BioCyc; NGON242231:GI2G-861-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 13834 MW; 1A8C507865BBC9D0 CRC64; MSVKLRPVYL DLPNIRLPIP GIVSILHRIS GVGLFIMLPF LLYFLSGTLS QESAFETYRA IVSHPLVKLV LIGILWAYLH HSLAGIRFLF LDAHKGLELN TARNTAKAVF ASALVLTVVL GALLW // ID Q5F8T2_NEIG1 Unreviewed; 84 AA. AC Q5F8T2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89405.1}; GN ORFNames=NGO_0678 {ECO:0000313|EMBL:AAW89405.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89405.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89405.1; -; Genomic_DNA. DR RefSeq; WP_003688807.1; NC_002946.2. DR RefSeq; YP_207817.1; NC_002946.2. DR EnsemblBacteria; AAW89405; AAW89405; NGO_0678. DR GeneID; 3282025; -. DR KEGG; ngo:NGO0678; -. DR PATRIC; 20334454; VBINeiGon24812_0799. DR HOGENOM; HOG000218977; -. DR OMA; ACASTWE; -. DR OrthoDB; EOG6XQ3QV; -. DR BioCyc; NGON242231:GI2G-645-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256068. SQ SEQUENCE 84 AA; 8784 MW; F0BCEF82F6194E78 CRC64; MNKLFVTALS ALALSACAGT WQGAKQDTAR NLDKTQAAAE RAAEQTGNAV EKGWDKTKEA VKKGGNAVGR GISHLGKKIE NATE // ID Q5F7I7_NEIG1 Unreviewed; 222 AA. AC Q5F7I7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 54. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89850.2}; GN ORFNames=NGO_1190 {ECO:0000313|EMBL:AAW89850.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89850.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89850.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7I7; -. DR MEROPS; C40.006; -. DR EnsemblBacteria; AAW89850; AAW89850; NGO_1190. DR PATRIC; 20335677; VBINeiGon24812_1397. DR HOGENOM; HOG000229978; -. DR OrthoDB; EOG6GTZPF; -. DR BioCyc; NGON242231:GI2G-1102-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 105 210 NLPC_P60. {ECO:0000259|Pfam:PF00877}. SQ SEQUENCE 222 AA; 24494 MW; 2C7A0661373743F3 CRC64; MDSFFKPAVW AVLWLMFAVR PALADELTNL LSSREQILRQ FAEDEQPVLP VNRAPARRAG NADELIGSAM GLNEQPVLPV NRAPARRAGN ADELIGSAMG LLGIAYRYGG TSVSTGFDCS GFMQHIFKRA MGINLPRTSA EQARMGAPVA RSELQPGDMV FFRTLGGSRI SHVGLYIGNN RFIHAPRTGK NIEITSLSHK YWSGKYAFAR RVKKNDPSRF LN // ID Q5F997_NEIG1 Unreviewed; 142 AA. AC Q5F997; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89240.1}; GN ORFNames=NGO_0502 {ECO:0000313|EMBL:AAW89240.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89240.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89240.1; -; Genomic_DNA. DR RefSeq; WP_003689076.1; NC_002946.2. DR RefSeq; YP_207652.1; NC_002946.2. DR EnsemblBacteria; AAW89240; AAW89240; NGO_0502. DR GeneID; 3282947; -. DR KEGG; ngo:NGO0502; -. DR PATRIC; 20334046; VBINeiGon24812_0595. DR HOGENOM; HOG000071315; -. DR OMA; YEAVENM; -. DR OrthoDB; EOG6CK7P8; -. DR BioCyc; NGON242231:GI2G-480-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 142 AA; 15510 MW; B12094EA51D71713 CRC64; MNREAVYSAL WAKLDALDGF VTKSRKLVHW NDVKRYDQPA LFMAQGDMQA LTLTGRETKW ILRADVYLYV QTAGQPPAPV MNPLIDAVCN AVNAVHPVTG KTDLTADGAD IEYCRVEGTV ETDEGTLGEQ AVCIIPIVIC AA // ID Q5F656_NEIG1 Unreviewed; 622 AA. AC Q5F656; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 60. DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:AAW90331.1}; GN ORFNames=NGO_1710 {ECO:0000313|EMBL:AAW90331.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90331.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90331.1; -; Genomic_DNA. DR RefSeq; WP_010951327.1; NC_002946.2. DR RefSeq; YP_208743.1; NC_002946.2. DR EnsemblBacteria; AAW90331; AAW90331; NGO_1710. DR GeneID; 3281153; -. DR KEGG; ngo:NGO1710; -. DR PATRIC; 20337012; VBINeiGon24812_2046. DR HOGENOM; HOG000218768; -. DR OMA; QINNQSI; -. DR OrthoDB; EOG6F81K8; -. DR BioCyc; NGON242231:GI2G-1606-MONOMER; -. DR Proteomes; UP000000535; 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 Acyltransferase {ECO:0000313|EMBL:AAW90331.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90331.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 170 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 219 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 235 251 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 257 274 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 316 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 344 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 356 377 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 8 339 Acyl_transf_3. FT {ECO:0000259|Pfam:PF01757}. SQ SEQUENCE 622 AA; 71041 MW; 178B0314A9D617A8 CRC64; MQAVRYRPEI DGLRAVAVLS VIIFHLNNRW LPGGFLGVDI FFVISGFLIT NIILSEIQNG SFSFRDFYTR RIKRIYPAFI AAVSLASVIA SQIFLYEDFN QMRKTIELST VFLSNIYLGF RLGYFDLSAD ENPVLHIWSL AVEEQYYLLY PLLLIFCYKK TKSLRVLRNI SIILFLILTA SSFLPAGFYT DILNQPNTYY LSTLRFPELL VGSLLAVYGQ TQNGRRQTEN GKRQLLSLLC FGALLVCLFV IDKHDPFIPG ITLLLPCLLT ALLIRSMQYG TLPTRILSAS PIVFVGKISY SLYLYHWIFI AFAHYITGDK QLGLPAVSAV AALTAGFSLL SYYLIEQPLR KRKMTFKKAF FCLYLAPSLM LVGYNLYSRG ILKQEHLRPL PGTPVAAENN FPETVLTLGD SHAGHLRGFL DYVGGREGWK AKILSLDSEC LVWVDEKLAD NPLCRKYRDE VEKAEAVFIA QFYDLRMGGQ PVPRFEAQSF LIPGFKARFR ETVKRIAAVK PVYVFANNTS ISRSPLREEK LKRFAINQYL RPIRAMGDIG KSNQAVFDLV KDIPNVHWVD AQKYLPKNTV EIHGRYLYGD QDHLTYFGSY YMGREFHKHE RLLKHSRGGA LQ // ID Q5F9Z7_NEIG1 Unreviewed; 190 AA. AC Q5F9Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=N-acetyl-anhydromuranmyl-L-alanine amidase {ECO:0000313|EMBL:AAW88990.1}; GN ORFNames=NGO_0237 {ECO:0000313|EMBL:AAW88990.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88990.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88990.1; -; Genomic_DNA. DR RefSeq; WP_003687579.1; NC_002946.2. DR RefSeq; YP_207402.1; NC_002946.2. DR ProteinModelPortal; Q5F9Z7; -. DR SMR; Q5F9Z7; 8-180. DR EnsemblBacteria; AAW88990; AAW88990; NGO_0237. DR GeneID; 3281496; -. DR KEGG; ngo:NGO0237; -. DR PATRIC; 20333423; VBINeiGon24812_0293. DR HOGENOM; HOG000255963; -. DR KO; K03806; -. DR OMA; RTRCNDF; -. DR OrthoDB; EOG60GRR5; -. DR BioCyc; NGON242231:GI2G-221-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 22 170 Ami_2. {ECO:0000259|SMART:SM00644}. SQ SEQUENCE 190 AA; 21337 MW; A66D67A4F70B7CC9 CRC64; MDNHAGAHWQ NGWLQSIRHT PSPNFSPRET GETVSLIVLH NISLPPFEYG TDAVEKLFAN RLDPDGHPFF SLIHTLHVSS HFLIARDGET VQFVSCGDMA YHAGASSFRG REKCNAFSIG IELEGCDFEP FAEAQYRSLE TLLAALCRRY PITAVTGHQD IAPGRKTDPG HFFDWRRIRE KGFPVDRNAV // ID Q5F9A6_NEIG1 Unreviewed; 73 AA. AC Q5F9A6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89231.1}; GN ORFNames=NGO_0493 {ECO:0000313|EMBL:AAW89231.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89231.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89231.1; -; Genomic_DNA. DR RefSeq; WP_003689095.1; NC_002946.2. DR RefSeq; YP_207643.1; NC_002946.2. DR EnsemblBacteria; AAW89231; AAW89231; NGO_0493. DR GeneID; 3282955; -. DR KEGG; ngo:NGO0493; -. DR PATRIC; 20334026; VBINeiGon24812_0585. DR OrthoDB; EOG6T4RXH; -. DR BioCyc; NGON242231:GI2G-471-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 73 AA; 7905 MW; BE254AA6A76C6D43 CRC64; MNNSVQISNI SIHQTEIGLF SLNDLHRASG GEDRHARLKA AANALEALSA HADAEHAEKI RPILPEIRNL SAV // ID Q5F581_NEIG1 Unreviewed; 441 AA. AC Q5F581; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 74. DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:AAW90656.1}; GN ORFNames=NGO_2048 {ECO:0000313|EMBL:AAW90656.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90656.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:2G6G} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 22-441, AND DISULFIDE BONDS. RX PubMed=16618494; DOI=10.1016/j.jmb.2006.03.023; RA Powell A.J., Liu Z.J., Nicholas R.A., Davies C.; RT "Crystal structures of the lytic transglycosylase MltA from RT N.gonorrhoeae and E.coli: insights into interdomain movements and RT substrate binding."; RL J. Mol. Biol. 359:122-136(2006). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90656.1; -; Genomic_DNA. DR RefSeq; WP_010951392.1; NC_002946.2. DR RefSeq; YP_209068.1; NC_002946.2. DR PDB; 2G6G; X-ray; 2.20 A; A=22-441. DR PDBsum; 2G6G; -. DR ProteinModelPortal; Q5F581; -. DR SMR; Q5F581; 32-441. DR CAZy; GH102; Glycoside Hydrolase Family 102. DR EnsemblBacteria; AAW90656; AAW90656; NGO_2048. DR GeneID; 3282730; -. DR KEGG; ngo:NGO2048; -. DR PATRIC; 20337893; VBINeiGon24812_2469. DR HOGENOM; HOG000255816; -. DR KO; K08304; -. DR OMA; DQNGHPY; -. DR OrthoDB; EOG6D2KR5; -. DR BioCyc; NGON242231:GI2G-1950-MONOMER; -. DR EvolutionaryTrace; Q5F581; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:2G6G}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256185. FT DOMAIN 144 335 MltA. {ECO:0000259|SMART:SM00925}. FT DISULFID 88 101 {ECO:0000213|PDB:2G6G}. SQ SEQUENCE 441 AA; 48017 MW; 3F88D629A8B9CBFB CRC64; MKKHLLRSAL YGIAAAILAA CQSRSIQTFP QPDTSVINGP DRPAGIPDPA GTTVAGGGAV YTVVPHLSMP HWAAQDFAKS LQSFRLGCAN LKNRQGWQDV CAQAFQTPVH SFQAKRFFER YFTPWQVAGN GSLAGTVTGY YEPVLKGDGR RTERARFPIY GIPDDFISVP LPAGLRGGKN LVRIRQTGKN SGTIDNAGGT HTADLSRFPI TARTTAIKGR FEGSRFLPYH TRNQINGGAL DGKAPILGYA EDPVELFFMH IQGSGRLKTP SGKYIRIGYA DKNEHPYVSI GRYMADKGYL KLGQTSMQGI KAYMRQNPQR LAEVLGQNPS YIFFRELAGS GNEGPVGALG TPLMGEYAGA IDRHYITLGA PLFVATAHPV TRKALNRLIM AQDTGSAIKG AVRVDYFWGY GDEAGELAGK QKTTGYVWQL LPNGMKPEYR P // ID Q5F8S6_NEIG1 Unreviewed; 392 AA. AC Q5F8S6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 71. 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 ORFNames=NGO_0684 {ECO:0000313|EMBL:AAW89411.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89411.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89411.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8S6; -. DR DNASU; 3281914; -. DR EnsemblBacteria; AAW89411; AAW89411; NGO_0684. DR PATRIC; 20334466; VBINeiGon24812_0805. DR HOGENOM; HOG000260368; -. DR OMA; DFLMTSA; -. DR OrthoDB; EOG60SCM2; -. DR BioCyc; NGON242231:GI2G-651-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. 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; 42693 MW; 50062913B9A31013 CRC64; MSGRTGRNSA TQAQPERVML VGVMLDKDDT GSNAARLNGF QTALAEAVEL VKAAGGDSVR VETAKRDRPH TALFVGTGKA AELSEAVAAD GIDLVVFNHE LTPTQERNLE KILQCRVLDR VGLILAIFAR RARTQEGRLQ VELAQLSHLA GRLIRGYGHL QSQRGGIGMK GPGETKLETD RRLTAHRINA LKKQLANLKK QRALRRKSRE SGRIKTFALV GYTNVGKSSL FNRLTKSGIY AKDQLFATLD TTARRLYISP ACSIILTDTV GFVSDLPHKL ISAFSATLEE TVQADVLLHV VDAAARNSGQ QIEDVENVLQ EIHAHDIPCI KVYNKTDLLP SEEQNTGIWR DAAGKIAAVR ISVAENTGID ALREAIAEYC AAAPNTDETE MP // ID Q5F7M6_NEIG1 Unreviewed; 67 AA. AC Q5F7M6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89811.1}; GN ORFNames=NGO_1144 {ECO:0000313|EMBL:AAW89811.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89811.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89811.1; -; Genomic_DNA. DR RefSeq; WP_003689736.1; NC_002946.2. DR RefSeq; YP_208223.1; NC_002946.2. DR EnsemblBacteria; AAW89811; AAW89811; NGO_1144. DR GeneID; 3282221; -. DR KEGG; ngo:NGO1144; -. DR PATRIC; 20335548; VBINeiGon24812_1339. DR HOGENOM; HOG000218818; -. DR OrthoDB; EOG6K405M; -. DR BioCyc; NGON242231:GI2G-1057-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7765 MW; 11A588CECA7495E1 CRC64; MSRYQQKFIV QELENHEFIY PDSFGDIGFT SNIKSAGKYD SYEDAFSSAL EEIGGEFVIF GFYEKED // ID Q5FAA7_NEIG1 Unreviewed; 42 AA. AC Q5FAA7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88880.1}; GN ORFNames=NGO_0120 {ECO:0000313|EMBL:AAW88880.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88880.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88880.1; -; Genomic_DNA. DR RefSeq; WP_003687390.1; NC_002946.2. DR RefSeq; YP_207292.1; NC_002946.2. DR EnsemblBacteria; AAW88880; AAW88880; NGO_0120. DR GeneID; 3282405; -. DR KEGG; ngo:NGO0120; -. DR PATRIC; 20333143; VBINeiGon24812_0155. DR HOGENOM; HOG000027876; -. DR OrthoDB; EOG6T4S66; -. DR BioCyc; NGON242231:GI2G-109-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 42 AA; 5160 MW; FE979C7F86803FBA CRC64; MKPDYSKRSS ENRFQTTFYL ITIKMLTTKN KPLFSVWRQI FN // ID Q5F5J3_NEIG1 Unreviewed; 334 AA. AC Q5F5J3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 74. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160}; GN ORFNames=NGO_1931 {ECO:0000313|EMBL:AAW90544.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90544.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90544.1; -; Genomic_DNA. DR RefSeq; WP_003688087.1; NC_002946.2. DR RefSeq; YP_208956.1; NC_002946.2. DR ProteinModelPortal; Q5F5J3; -. DR SMR; Q5F5J3; 4-332. DR PRIDE; Q5F5J3; -. DR EnsemblBacteria; AAW90544; AAW90544; NGO_1931. DR GeneID; 3282688; -. DR KEGG; ngo:NGO1931; -. DR PATRIC; 20337600; VBINeiGon24812_2327. DR HOGENOM; HOG000071678; -. DR KO; K00134; -. DR OMA; MKAASSE; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; NGON242231:GI2G-1834-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160, KW ECO:0000313|EMBL:AAW90544.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 35761 MW; BC812452B1665C7F CRC64; MSIKVAINGF GRIGRLALRQ IEKAHGIEVA AVNDLTPAEM LLHLFKYDST QGRFQGTAEL KDDAIVVNGR EIKVFANPNP EELPWGELGV DVVLECTGFF TNKTKAEAHI RAGARKVVIS APGGNDVKTV VYGVNQDILD GSETVISAAS CTTNCLAPMA AVLQKEFGVV EGLMTTIHAY TGDQNTLDAP HRKGDLRRAR AAALNIVPNS TGAAKAIGLV IPELNGKLDG SAQRVPVATG SLTELVSVLE RPATKEEINA AMKAASSESY GYNEDQIVSS DVVGIEYGSL FDATQTRVMT VGGKQLVKTV AWYDNEMSYT CQLVRTLEYF AGKI // ID Q5FAG0_NEIG1 Unreviewed; 363 AA. AC Q5FAG0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Ribosome-binding ATPase YchF {ECO:0000256|HAMAP-Rule:MF_00944}; GN Name=ychF {ECO:0000256|HAMAP-Rule:MF_00944, GN ECO:0000313|EMBL:AAW88827.1}; GN ORFNames=NGO_0063 {ECO:0000313|EMBL:AAW88827.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88827.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88827.1; -; Genomic_DNA. DR RefSeq; WP_003687306.1; NC_002946.2. DR RefSeq; YP_207239.1; NC_002946.2. DR ProteinModelPortal; Q5FAG0; -. DR SMR; Q5FAG0; 1-363. DR EnsemblBacteria; AAW88827; AAW88827; NGO_0063. DR GeneID; 3282306; -. DR KEGG; ngo:NGO0063; -. DR PATRIC; 20332978; VBINeiGon24812_0073. DR HOGENOM; HOG000087628; -. DR KO; K06942; -. DR OMA; CTIEPNI; -. DR OrthoDB; EOG6NSGJC; -. DR BioCyc; NGON242231:GI2G-56-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00944}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 39300 MW; 757FC4DF3312EF8A CRC64; MSLKCGIVGL PNVGKSTLFN ALTQSGIEAA NYPFCTIEPN VGIVEVPDPR MAELAKIVNP QKMQPAIVEF VDIAGLVAGA SKGEGLGNRF LANIRETDAI VNVVRCFDDD NIVHVSGKVD PIADIETIGT ELALADLASV EKAIVREEKR ARSGDKDAQK LVDLCKKLLP HLDEGKPVRS FGLDAEERAL LKPLFLLTAK PAMYVGNVAE DGFENNPHLD RLKELAAKEN APVVAVCAAM ESEIAELEDG EKAEFLAEMG LEEPGLNRLI RAGYDLLGLQ TYFTAGVKEV RAWTIHKGDT APQAAGVIHT DFERGFIRAQ VIAYDDFVSL GGEAKAKEAG KMRVEGKEYV VQDGDVMHFL FNV // ID Q5F6Q5_NEIG1 Unreviewed; 380 AA. AC Q5F6Q5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574}; GN ORFNames=NGO_1494 {ECO:0000313|EMBL:AAW90132.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90132.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90132.1; -; Genomic_DNA. DR RefSeq; WP_010951282.1; NC_002946.2. DR RefSeq; YP_208544.1; NC_002946.2. DR ProteinModelPortal; Q5F6Q5; -. DR PRIDE; Q5F6Q5; -. DR EnsemblBacteria; AAW90132; AAW90132; NGO_1494. DR GeneID; 3281586; -. DR KEGG; ngo:NGO1494; -. DR PATRIC; 20336442; VBINeiGon24812_1768. DR HOGENOM; HOG000263815; -. DR KO; K02055; -. DR OMA; TNFIHYA; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NGON242231:GI2G-1398-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Periplasm {ECO:0000256|PIRNR:PIRNR019574}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|PIRNR:PIRNR019574}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 380 Putrescine-binding periplasmic protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256038. SQ SEQUENCE 380 AA; 41257 MW; C6D6FDED99775FEA CRC64; MKKSVLAVLA ALSLAACGGS EKNAVQPQAG SAPAANAEAA ATDTLNIYNW SNYVDESTVE DFKKANNLKL TYDLYENNET LEAKMLTGKS GYDLVVPGIA FLPRQIEAGA YQKVNKDLIP NYKNIDPELL KMLEAADPGN QYAVPYFSGV NTVAITAKGK ELLGGKLPEN GWDLLFKPEY TRKLKSCGIA LWDTPSEMFP ILLNYLGKDP KGSNPEDLKA AAEVLKSIRP DVKRFSPSII DELARGDICL AAGNGGDLNL AKARSEEVKN NVGIEVLTPK GMGFWIESWL IPADAKNVAN AHKYINYTLD PEIAAKNGIA VTFAPASKPA REKMPAELVN TRSIFPNEQD MKDGFVMPQM SADAKKLSVS LWQKIKVGTN // ID Q5F895_NEIG1 Unreviewed; 1277 AA. AC Q5F895; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:AAW89592.1}; GN ORFNames=NGO_0893 {ECO:0000313|EMBL:AAW89592.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89592.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89592.1; -; Genomic_DNA. DR RefSeq; WP_010951146.1; NC_002946.2. DR RefSeq; YP_208004.1; NC_002946.2. DR ProteinModelPortal; Q5F895; -. DR EnsemblBacteria; AAW89592; AAW89592; NGO_0893. DR GeneID; 3281219; -. DR KEGG; ngo:NGO0893; -. DR PATRIC; 20334959; VBINeiGon24812_1049. DR HOGENOM; HOG000264473; -. DR OMA; FGLMGHE; -. DR OrthoDB; EOG6X9MH6; -. DR BioCyc; NGON242231:GI2G-834-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 141841 MW; 772B3AE3CE06FF34 CRC64; MTTTTAPQRI REIPYNYTSY TDREIVIRLL GDEAWHILQD LRGQRKTGRS ARMLFEVLGD IWVVVRNPYL VDDLLEHPKR RAALVREMRH RLNEIRKRRD DNQQADVLIA AAEKAVERFD GSFDETRQKR RQILERLSKI TKPHNIMFDG LARVTHVTDA TDWRVEYPFV VVNPDTEAEV APLVRALIEL DLVIIPRGGG TGYTGGAVPL DANSAVINTE KLDKHRGVEY VELAGLYGRH PIIRCGAGVV TRRVEETAHQ AGLVFAVDPT SADASCVGGN VAMNAGGKKA VLWGTALDNL AYWNMVNPQG EWLRIERVRH NFGKIHDEET AVFDVHTLDS DGINIVKTER LEIPGHKFRK VGLGKDVTDK FLSGLPGVQK EGTDGIITGV AFVLHKMPKY TRTVCMEFFG TAATATPSIV EIRDFLLAHD SVRLAGLEHL DWRYVRAVGY ATKAAGKGRP KMVLLADVVS DDEAAVEAAA EHICELARAR DGEGFIAVSP EARKTFWLDR SRTAAIAKHT NAFKINEDVV IPLERLGEYS DGIERINIEL SIQNKLKLCA ALEQYLSGKL PIDKMGTDLP TAELLGERGK HALAHVAAVK ARWDWLLAHL DAPLADYKSR YGTAVHAAPE AKDDESCFTA FRDFRLRVSV KADVMKPLAE IFSGKTDTKI IQGLGKIHTK TVRSRVFVAL HMHAGDGNVH TNIPVNSDDA EMLQTAYRSV ERIMKIARSL GGVISGEHGI GITKLEFLTD EDLQPFWNYK NQVDPKHTFN RHKLMKGSDL RNAYTPSFEL LGAESLIMEK SDLGTIADSV KDCLRCGKCK PVCSTHVPRA NLLYSPRNKI LGVGLLTEAF LYEEQTRRGV SVKHFEELMD IGDHCTVCHR CVKPCPVNID FGDVTVAVRN YLADSGHKRF APAASMGMAF LNATGPKTIK ALRAAMIQTG FPAQNFAYKI GKLLPIGTKK QKAEPKATVG KAPIKEQVIH FINRPLPKSV PAKTPRSLLG IEDGKSIPII HNPAAPEDAE AVFYFPGCGS ERLFSQIGLA VQAMLWHVGV QTVLPPGYMC CGYPQDAGGN KAKAEEMSTN NRVAFHRMAN TLNYLDIKTV VVSCGTCYDQ LEKYRFEEIF PGCRIIDIHE YLLEKGVKLD GVKGQQYLYH DPCHTPIKTM NATQMASSLM GQKVVLSDRC CGESGMFAVK RPDIATQVKF RKQEEIEKNL KELPQGEPVK MLTSCPACLQ GLSRYSDDNN MPADYIVIEM AKHILGENWL DEFVKKANNG GVEKVLL // ID Q5F6P8_NEIG1 Unreviewed; 153 AA. AC Q5F6P8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Phosphotransferase {ECO:0000313|EMBL:AAW90139.1}; GN ORFNames=NGO_1501 {ECO:0000313|EMBL:AAW90139.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90139.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90139.1; -; Genomic_DNA. DR RefSeq; WP_003703029.1; NC_002946.2. DR RefSeq; YP_208551.1; NC_002946.2. DR ProteinModelPortal; Q5F6P8; -. DR EnsemblBacteria; AAW90139; AAW90139; NGO_1501. DR GeneID; 3281583; -. DR KEGG; ngo:NGO1501; -. DR PATRIC; 20336476; VBINeiGon24812_1786. DR HOGENOM; HOG000052238; -. DR KO; K06925; -. DR OMA; LDIDIRY; -. DR OrthoDB; EOG6GBMHT; -. DR BioCyc; NGON242231:GI2G-1405-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90139.1}. SQ SEQUENCE 153 AA; 16648 MW; C00D01FC3A4E61E1 CRC64; MSDFSPVSRF LADEAATLDL GAAWSSRLNA PLVIYLEGDL GAGKTTLTRG ILRGLGHQGA VKSPTYAIVE SYPLERFALH HFDLYRFSFP EEWEDAGLDE LFAANSVCLI EWPQQGGEFT PPADITATLT HGGGGRKCLL TAHTERGRES LPL // ID Q5F5J7_NEIG1 Unreviewed; 131 AA. AC Q5F5J7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90540.1}; GN ORFNames=NGO_1927 {ECO:0000313|EMBL:AAW90540.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90540.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90540.1; -; Genomic_DNA. DR RefSeq; WP_003688080.1; NC_002946.2. DR RefSeq; YP_208952.1; NC_002946.2. DR EnsemblBacteria; AAW90540; AAW90540; NGO_1927. DR GeneID; 3282692; -. DR KEGG; ngo:NGO1927; -. DR PATRIC; 20337592; VBINeiGon24812_2323. DR HOGENOM; HOG000218688; -. DR OMA; ILYFLMV; -. DR OrthoDB; EOG6PGK70; -. DR BioCyc; NGON242231:GI2G-1830-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 64 105 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 131 AA; 14811 MW; 7E27C8329A051593 CRC64; MPSDVGMRLQ TAFRRKLNMK KILYFLMFVF STSVWAGGAE DNLLSIQSGY RALLQKQNNL DGKIIGMQSD LEDARRRLQA AQADIARLEA EIPAAMAQKA RQAEEMRQIG VRLDHAWNAV YGAGERKRRG N // ID Q5F6U3_NEIG1 Unreviewed; 396 AA. AC Q5F6U3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Aromatic amino acid aminotransferase {ECO:0000313|EMBL:AAW90094.1}; GN ORFNames=NGO_1452 {ECO:0000313|EMBL:AAW90094.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90094.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90094.1; -; Genomic_DNA. DR RefSeq; WP_003705754.1; NC_002946.2. DR RefSeq; YP_208506.1; NC_002946.2. DR ProteinModelPortal; Q5F6U3; -. DR SMR; Q5F6U3; 3-396. DR EnsemblBacteria; AAW90094; AAW90094; NGO_1452. DR GeneID; 3281656; -. DR KEGG; ngo:NGO1452; -. DR PATRIC; 20336323; VBINeiGon24812_1710. DR HOGENOM; HOG000185899; -. DR KO; K00813; -. DR OMA; SWANHAA; -. DR OrthoDB; EOG6C2WBK; -. DR BioCyc; NGON242231:GI2G-1359-MONOMER; -. DR Proteomes; UP000000535; 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 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:AAW90094.1}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAW90094.1}. FT DOMAIN 28 393 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. FT COILED 305 332 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 396 AA; 44065 MW; C651F68646210DEF CRC64; MFFKHIEAAP ADPILGLGEA FKAETRPEKV NLGIGVYKDA SGATPIVKAV KEAEKRLLES ETTKNYLTID GVADYNEQTQ ILLFGKDHEI IASRRAKTAQ SLGGTGALRI AAEFAKRQLN AQTIWISNPT WPNHNAIAKA VGIQDKPYRY YDAAKHCLDW DGMIEDLNQA QKGDIVLLHG CCHNPTGIDP TPEQWETLAK LSAEKGWLPL FDFAYQGFGN GLEEDAYGLR VFLKHNTELL IASSYSKNFG MYNERVGAFT LVAEDEETAA RAHSQIKTII RTLYSNPASH GANTIALVLK NDDLKAQWIA ELDEMRGRIK AMRQKFVELL KAKGSTQDFD FIIEQNGMFS FSGLTPEQVD RLKNEFAIYA VRSGRINVAG ITDDNIDYLC ESIVKV // ID Q5F6D7_NEIG1 Unreviewed; 91 AA. AC Q5F6D7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 39. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW90250.1}; GN ORFNames=NGO_1622 {ECO:0000313|EMBL:AAW90250.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90250.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90250.1; -; Genomic_DNA. DR RefSeq; WP_003694990.1; NC_002946.2. DR RefSeq; YP_208662.1; NC_002946.2. DR EnsemblBacteria; AAW90250; AAW90250; NGO_1622. DR GeneID; 3281266; -. DR KEGG; ngo:NGO1622; -. DR PATRIC; 20336784; VBINeiGon24812_1937. DR HOGENOM; HOG000137690; -. DR OrthoDB; EOG632D6X; -. DR BioCyc; NGON242231:GI2G-1519-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 91 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256202. SQ SEQUENCE 91 AA; 9715 MW; 45B35B13BCEAB170 CRC64; MKTRNIAFKF AVLAAVLAAG YAFGFAKGGG SRTAKGKPAD IAAMRMALAQ KQAQVAELSA EIWLEERHLN AEEEAGCRRV HGDAEVPEGK E // ID Q5F764_NEIG1 Unreviewed; 183 AA. AC Q5F764; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=DNA-3-methyladenine glycosylase {ECO:0000313|EMBL:AAW89973.1}; GN ORFNames=NGO_1322 {ECO:0000313|EMBL:AAW89973.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89973.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89973.1; -; Genomic_DNA. DR RefSeq; WP_003693800.1; NC_002946.2. DR RefSeq; YP_208385.1; NC_002946.2. DR ProteinModelPortal; Q5F764; -. DR EnsemblBacteria; AAW89973; AAW89973; NGO_1322. DR GeneID; 3281890; -. DR KEGG; ngo:NGO1322; -. DR PATRIC; 20336009; VBINeiGon24812_1555. DR HOGENOM; HOG000220753; -. DR KO; K01246; -. DR OMA; NEFLMST; -. DR OrthoDB; EOG661HDB; -. DR BioCyc; NGON242231:GI2G-1236-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 183 AA; 21049 MW; E9FEBC84D52103DD CRC64; MNYCEFAASL PENTDNPNKH YHDTQYGFPI KDDNGLFERL VLEINQAGLS WTLMLKKRQA FQTAFEGFDI DTVAAFGEAD IERLLTDAGI VRNRLKIDAA IFNARQIQAL QQEHGSFKNW LDAHHPRSKD EWVKLFKKHF KFVGGEIVGE FLMSTGYLKG AHAESCPVYR KTLKYHPKWL DAV // ID Q5F9D6_NEIG1 Unreviewed; 89 AA. AC Q5F9D6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89201.1}; GN ORFNames=NGO_0463 {ECO:0000313|EMBL:AAW89201.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89201.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89201.1; -; Genomic_DNA. DR RefSeq; WP_003687928.1; NC_002946.2. DR RefSeq; YP_207613.1; NC_002946.2. DR EnsemblBacteria; AAW89201; AAW89201; NGO_0463. DR GeneID; 3283077; -. DR KEGG; ngo:NGO0463; -. DR PATRIC; 20333964; VBINeiGon24812_0554. DR HOGENOM; HOG000071247; -. DR OMA; HIVIHNA; -. DR OrthoDB; EOG6G4W43; -. DR BioCyc; NGON242231:GI2G-441-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 89 AA; 9656 MW; 5FFF68CE561BA739 CRC64; MESSDVQGRM ETLAFATAPK KGGIRKSGFG RVILIKSGHI VIHNADGDSF ATGYGVIAAD IVSPDLKTDF DIFFPPESLL RYKKIGKKK // ID Q5F6P6_NEIG1 Unreviewed; 272 AA. AC Q5F6P6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Fic/DOC family protein {ECO:0000313|EMBL:AAW90141.2}; GN ORFNames=NGO_1503 {ECO:0000313|EMBL:AAW90141.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90141.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90141.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6P6; -. DR EnsemblBacteria; AAW90141; AAW90141; NGO_1503. DR PATRIC; 20336480; VBINeiGon24812_1788. DR HOGENOM; HOG000219091; -. DR OMA; LVCERIN; -. DR OrthoDB; EOG6S52JD; -. DR BioCyc; NGON242231:GI2G-1407-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 113 249 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 272 AA; 31148 MW; 7E2C545038DD895F CRC64; MKGMDKLRYQ RDFLNIRPIF TAGEQEYLTE LSDRLPLSVL TDSVRNIEEI GIDFVYSPAK LEGNTYNQYD TQALLKLGQT AGGKLYSDAV MLINLRESYR HLLSGLDSPK PFDWLDFLKT THSLISENLL EKGSGGVVRR DSVTISGTDY TPLSNPQSLD TELKWLLQEA PKIENPFDRA VYLHNNLAYL RYFKDCNKRT ARNCMTLSLM RSGFFPCVFS PDSYPAYAEA VVAYYETGDY GLFKKYFISA YENTVNKYGP QPDVDIFRNF SI // ID Q5FA12_NEIG1 Unreviewed; 77 AA. AC Q5FA12; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW88975.1}; GN ORFNames=NGO_0222 {ECO:0000313|EMBL:AAW88975.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88975.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88975.1; -; Genomic_DNA. DR RefSeq; WP_003704827.1; NC_002946.2. DR RefSeq; YP_207387.1; NC_002946.2. DR EnsemblBacteria; AAW88975; AAW88975; NGO_0222. DR GeneID; 3281455; -. DR KEGG; ngo:NGO0222; -. DR PATRIC; 20333383; VBINeiGon24812_0274. DR HOGENOM; HOG000218827; -. DR OMA; FRPNAMN; -. DR OrthoDB; EOG600DWR; -. DR BioCyc; NGON242231:GI2G-205-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 59 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 77 AA; 8373 MW; 4EA356ADED7F0E74 CRC64; MNRRKIYLLS VALFTLAFML PVLLGAYLLT AGSKTFAVAS FLFAFGALFG QIGALALYLR HKSLRAAPSS SQGNRYV // ID Q5F874_NEIG1 Unreviewed; 942 AA. AC Q5F874; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=2-oxoglutarate dehydrogenase {ECO:0000313|EMBL:AAW89613.1}; DE EC=1.2.4.2 {ECO:0000313|EMBL:AAW89613.1}; GN Name=sucA {ECO:0000313|EMBL:AAW89613.1}; GN ORFNames=NGO_0917 {ECO:0000313|EMBL:AAW89613.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89613.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89613.1; -; Genomic_DNA. DR RefSeq; WP_010358264.1; NC_002946.2. DR RefSeq; YP_208025.1; NC_002946.2. DR ProteinModelPortal; Q5F874; -. DR SMR; Q5F874; 86-942. DR EnsemblBacteria; AAW89613; AAW89613; NGO_0917. DR GeneID; 3281399; -. DR KEGG; ngo:NGO0917; -. DR PATRIC; 20335017; VBINeiGon24812_1078. DR HOGENOM; HOG000259588; -. DR KO; K00164; -. DR OMA; DWLDGRW; -. DR OrthoDB; EOG6V1M1F; -. DR BioCyc; NGON242231:GI2G-855-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89613.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 594 791 Transket_pyr. FT {ECO:0000259|SMART:SM00861}. SQ SEQUENCE 942 AA; 105118 MW; C241885BF1E847FC CRC64; MMDEKLNFSY LFGSNAPYIE ELYEAFLENP DAVDEKWKQY FTDLSKQPGT VAVDVAHTPI RESFVTLAKK KIASAVAGGA DEAMLKKQVS VLRLISAYRI QGVGAAQLDP LKRIPPRDIE ALDPKFHGLS DADMALRFNM GEGDFANRGK LLLSQIISNL 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 QVEADGYIQA YRDALDKGEH VEQTTLSNFQ RTQIDWSKYQ GKDWREKIET GLPAADIERL TEKFTAVPEG FALHPTAKRV IEARKAMASG KQAIDWGMAE TLAYASLLTK GHGVRISGED SGRGTFSHRH AVLHDQKREK WDDGTYVPLR NMGEGLGEFL 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 Q5F9D5_NEIG1 Unreviewed; 227 AA. AC Q5F9D5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89202.1}; GN ORFNames=NGO_0464 {ECO:0000313|EMBL:AAW89202.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89202.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89202.1; -; Genomic_DNA. DR RefSeq; WP_003706579.1; NC_002946.2. DR RefSeq; YP_207614.1; NC_002946.2. DR EnsemblBacteria; AAW89202; AAW89202; NGO_0464. DR GeneID; 3282982; -. DR KEGG; ngo:NGO0464; -. DR PATRIC; 20333966; VBINeiGon24812_0555. DR HOGENOM; HOG000225513; -. DR OMA; MATGCRC; -. DR OrthoDB; EOG6CGCCB; -. DR BioCyc; NGON242231:GI2G-442-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR024498; DUF2786. DR InterPro; IPR016868; Phage_B3_Orf5. DR Pfam; PF10979; DUF2786; 1. DR PIRSF; PIRSF028111; UCP028111; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 41 DUF2786. {ECO:0000259|Pfam:PF10979}. SQ SEQUENCE 227 AA; 25676 MW; BC406D6CAE45BB10 CRC64; MDKEKVLDKI KKCLALGRSV NEHEAAQALR QAQALMEKYK VNAEDIALSK VSEQKADRKM AFKLAGWQWG VANMIADIFG CKSYQRGKTM MFYGIGNRAE TSAYAFDVVY RQISADRRKF LKTCRAGKPS HRTYLADRFC GGWIASAWET VKKFEMSDEE KAIMDGYKKK EYPDMAEART RDAKSSILQG SKMEYEALTR GMESGKQVKL HYAVNGTGFV KQIGGQT // ID Q5F907_NEIG1 Unreviewed; 135 AA. AC Q5F907; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE SubName: Full=MerR family transcriptional regulator {ECO:0000313|EMBL:AAW89330.1}; GN ORFNames=NGO_0602 {ECO:0000313|EMBL:AAW89330.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89330.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89330.1; -; Genomic_DNA. DR RefSeq; WP_003688937.1; NC_002946.2. DR RefSeq; YP_207742.1; NC_002946.2. DR ProteinModelPortal; Q5F907; -. DR EnsemblBacteria; AAW89330; AAW89330; NGO_0602. DR GeneID; 3281382; -. DR KEGG; ngo:NGO0602; -. DR PATRIC; 20334280; VBINeiGon24812_0712. DR HOGENOM; HOG000266077; -. DR OMA; CLKNSGM; -. DR OrthoDB; EOG6Z0QGQ; -. DR BioCyc; NGON242231:GI2G-570-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000703}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 15461 MW; AA85F070E6ADD45E CRC64; MTYTTAKAAE KIGISAHTLR FYDKEGLLPN IGRDEYGNRC FTDNDLQWLY LLQCLKNTGM SLKDIKRFAE CTVIGDDTIE ERLSLFENQI ENVKCQIAEL KRYLDLLEYK LAFYQKAKAL GSVKAVNLPQ IPETA // ID Q5F5P3_NEIG1 Unreviewed; 54 AA. AC Q5F5P3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90494.1}; GN ORFNames=NGO_1874 {ECO:0000313|EMBL:AAW90494.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90494.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90494.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90494; AAW90494; NGO_1874. DR PATRIC; 20337442; VBINeiGon24812_2252. DR OrthoDB; EOG60PHMZ; -. DR BioCyc; NGON242231:GI2G-1778-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 54 AA; 5739 MW; 9A1C571B7F701432 CRC64; MQNPDLVGQN AFYPMESVSA RTEITAAVSL ADRYSELTKT GTALPRPGSK GTIP // ID Q5F6V7_NEIG1 Unreviewed; 261 AA. AC Q5F6V7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:AAW90080.1}; GN ORFNames=NGO_1438 {ECO:0000313|EMBL:AAW90080.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90080.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3GV1} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 126-261. RA Zhang Z., Burley S.K., Swaminathan S.; RT "The crystal structure of disulfide interchange protein from Neisseria RT gonorrhoeae."; RL Submitted (MAR-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; AE004969; AAW90080.1; -; Genomic_DNA. DR RefSeq; WP_003689299.1; NC_002946.2. DR RefSeq; YP_208492.1; NC_002946.2. DR PDB; 3GV1; X-ray; 2.00 A; A/B/C=126-261. DR PDBsum; 3GV1; -. DR ProteinModelPortal; Q5F6V7; -. DR DNASU; 3281709; -. DR EnsemblBacteria; AAW90080; AAW90080; NGO_1438. DR GeneID; 3281709; -. DR KEGG; ngo:NGO1438; -. DR PATRIC; 20336295; VBINeiGon24812_1696. DR HOGENOM; HOG000222078; -. DR KO; K03981; -. DR OMA; VWCAKDP; -. DR OrthoDB; EOG632D3W; -. DR BioCyc; NGON242231:GI2G-1345-MONOMER; -. DR EvolutionaryTrace; Q5F6V7; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3GV1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256598. FT DOMAIN 98 261 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 261 AA; 28706 MW; 5807D9B6C4F912D5 CRC64; MKTKLIKILT PFTVLPLLAC GQTPVSNANA ESAVKAESAG KSVAASLKAR LEKTYSAQDL KVLSVSETPV KGIYEVVVSG RQIIYTDAEG GYMFVGELIN IDTRKNLTEE RAADLNKIDF ASLPLDKAIK EVRGNGKLKV AVFSDPDCPF CKRLEHEFEK MTDVTVYSFM MPIAGLHPDA ARKAQILWCQ PDRAKAWTDW MRKGKFPVGG SICDNPVAET TSLGEQFGFN GTPTLVFPNG RTQSGYSPMP QLEEIIRKNQ Q // ID Q5F8T0_NEIG1 Unreviewed; 449 AA. AC Q5F8T0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 53. DE SubName: Full=Glutamate--cysteine ligase {ECO:0000313|EMBL:AAW89407.2}; GN ORFNames=NGO_0680 {ECO:0000313|EMBL:AAW89407.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89407.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89407.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89407; AAW89407; NGO_0680. DR PATRIC; 20334458; VBINeiGon24812_0801. DR HOGENOM; HOG000265033; -. DR OMA; GMHFVPL; -. DR OrthoDB; EOG69WFG3; -. DR BioCyc; NGON242231:GI2G-647-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR InterPro; IPR011718; GshA. DR Pfam; PF08886; GshA; 1. DR TIGRFAMs; TIGR02049; gshA_ferroox; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW89407.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 449 AA; 49659 MW; 33590FA2C99E755F CRC64; MKLPVMSPEH SAQLQAFEAK ILSNHAKIEA WFRTQWNAHR PPFYGSVDIR NAGYKISSID MNLFPGGFNN LNPNFIPLAA VAAQDAVQRA CETEKSVLII PENHTRNTFY LQNVYALGEI FRSAGCEVRL GSLNPEVTEP AEFETALGDK ILLEPLLRTR DRVHLADGFS PCVVLLNNDL SAGIPDILKG IGQTVLPPLH GGWTTRRKTN HFGAYNQVAA EFAKLIDIDE WQINPYFEKI GGLDFQGREG EDALAEAVER VLAKIQAKYD ESGIADKPFV IVKADAGTYG MGVMSVKSSD EVRGLNRKNR NKMAKVKEGL EVSEVIVQEG VYTYETLNGA VCEPVVYMMD RFVIGGFFRV HEGRGADENL NAGGMVFVPL SNSIPTGNGD NSQEAPEACK RVFEQWDSLG MPRSEKDCDV DNEHNRLYVY GVMARLSLLA ASIELEETA // ID Q5FAJ4_NEIG1 Unreviewed; 107 AA. AC Q5FAJ4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Sulfurtransferase {ECO:0000313|EMBL:AAW88789.1}; GN ORFNames=NGO_0020 {ECO:0000313|EMBL:AAW88789.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88789.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88789.1; -; Genomic_DNA. DR RefSeq; WP_003687228.1; NC_002946.2. DR RefSeq; YP_207201.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ4; -. DR EnsemblBacteria; AAW88789; AAW88789; NGO_0020. DR GeneID; 3283063; -. DR KEGG; ngo:NGO0020; -. DR PATRIC; 20332870; VBINeiGon24812_0020. DR HOGENOM; HOG000247776; -. DR OMA; DEEAAIC; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NGON242231:GI2G-17-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88789.1}. FT DOMAIN 17 105 Rhodanese. {ECO:0000259|PROSITE:PS50206}. SQ SEQUENCE 107 AA; 11999 MW; 0955757576522B03 CRC64; MDIVQLPSAA LKAWMDEGRM FCLLDVRTDE EAAVCSLPNA LHIPMNLIPL RQNELPDDVP LVVYCHHGIR SLHTAMYLAE AGFENLYNLQ GGIDAWAVEV DAEMARY // ID Q5F6X2_NEIG1 Unreviewed; 71 AA. AC Q5F6X2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90065.1}; GN ORFNames=NGO_1421 {ECO:0000313|EMBL:AAW90065.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90065.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90065.1; -; Genomic_DNA. DR RefSeq; WP_002214367.1; NC_002946.2. DR RefSeq; YP_208477.1; NC_002946.2. DR EnsemblBacteria; AAW90065; AAW90065; NGO_1421. DR GeneID; 3281766; -. DR KEGG; ngo:NGO1421; -. DR PATRIC; 20336251; VBINeiGon24812_1674. DR HOGENOM; HOG000273689; -. DR KO; K05952; -. DR OMA; IEKECDC; -. DR OrthoDB; EOG693GV2; -. DR BioCyc; NGON242231:GI2G-1330-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007495; NqrM. DR Pfam; PF04400; DUF539; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 7731 MW; 09F2958A257A13F1 CRC64; MKTLLLTFGI FLTVIIGMAV GYIFSKRTIK GSCGGITALG MKKMCDCDTP CDTLQKKLDE EKQAGGIRVD R // ID Q5F9M9_NEIG1 Unreviewed; 345 AA. AC Q5F9M9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 51. DE SubName: Full=Restriction endonuclease NgoFVII {ECO:0000313|EMBL:AAW89108.1}; GN ORFNames=NGO_0364 {ECO:0000313|EMBL:AAW89108.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89108.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:4RCT, ECO:0000213|PDB:4RD5, ECO:0000213|PDB:4RDM} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS). RX PubMed=25429979; DOI=10.1093/nar/gku1237; RA Tamulaitiene G., Silanskas A., Grazulis S., Zaremba M., Siksnys V.; RT "Crystal structure of the R-protein of the multisubunit ATP-dependent RT restriction endonuclease NgoAVII."; RL Nucleic Acids Res. 42:14022-14030(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; AE004969; AAW89108.1; -; Genomic_DNA. DR RefSeq; WP_003687776.1; NC_002946.2. DR RefSeq; YP_207520.1; NC_002946.2. DR PDB; 4RCT; X-ray; 2.25 A; A/B=1-345. DR PDB; 4RD5; X-ray; 2.70 A; A/B=179-345. DR PDB; 4RDM; X-ray; 2.70 A; A/B=178-345. DR PDBsum; 4RCT; -. DR PDBsum; 4RD5; -. DR PDBsum; 4RDM; -. DR REBASE; 5857; NgoAVII. DR EnsemblBacteria; AAW89108; AAW89108; NGO_0364. DR GeneID; 3283027; -. DR KEGG; ngo:NGO0364; -. DR PATRIC; 20333725; VBINeiGon24812_0440. DR HOGENOM; HOG000027904; -. DR OMA; GRWIKGR; -. DR OrthoDB; EOG6NPM4N; -. DR BioCyc; NGON242231:GI2G-343-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR019065; Res_endonuc_III_NgoFVII. DR Pfam; PF09565; RE_NgoFVII; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4RCT, ECO:0000213|PDB:4RD5, KW ECO:0000213|PDB:4RDM}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89108.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89108.1}; KW Nuclease {ECO:0000313|EMBL:AAW89108.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 345 AA; 39837 MW; 1FCA4D595ED42EF3 CRC64; MNTVFSNIAN AKITEKSLNA VWMDLFKSAD EVLMATGYVS NDAVVELHKI LELNDHIQKI DLLVGMHYLE GFSHLQYDSL CKLNDFLRHE KRGAVYVSPF VKFHGKMYSF KNYQKINGLI GSANLTCFWD STERTYETML HLNGKPAQIL QADIQSTIHK LGKNIQEVER PSKFIEHNSH LENCLGVQKI APEQIRQLFA QTSEYHFSIP AKTEEKSNLN VFFGEGRRDK RGFVKPRPWY EVELIVSKDI TSQEGYPVLK SFTVITDDGW QFQCKTSGDY SKNFRSENDL KTLGKWIKGR LESHGCLQNN EKITHETLRE YGNDHFELRS TDNPDVWLLS FKGKN // ID Q5F6R7_NEIG1 Unreviewed; 215 AA. AC Q5F6R7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90120.1}; GN ORFNames=NGO_1482 {ECO:0000313|EMBL:AAW90120.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90120.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90120.1; -; Genomic_DNA. DR RefSeq; WP_003689360.1; NC_002946.2. DR RefSeq; YP_208532.1; NC_002946.2. DR ESTHER; neig1-q5f6r7; Duf_452. DR EnsemblBacteria; AAW90120; AAW90120; NGO_1482. DR GeneID; 3281632; -. DR KEGG; ngo:NGO1482; -. DR PATRIC; 20336413; VBINeiGon24812_1754. DR HOGENOM; HOG000144228; -. DR KO; K09789; -. DR OMA; IVYFAGW; -. DR OrthoDB; EOG6S7XW4; -. DR BioCyc; NGON242231:GI2G-1386-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 215 AA; 24921 MW; A333C4ED218D7271 CRC64; MKTKFYNHQG EHLILYFAGW GMPPDAVNHL ILPENHDLLI CYDYQDLNLD FDFSAYRHIR LVAWSMGVWA AERALQGIRL KSATAVNGTG LPCDDNFGIP CAVFKGTLEN LTENTRSKFE RRICGDKASF EDYQQFPARP FDEIHQELTA LFAMIGQDRR TDLIRWTNAL FGSGDKIFIP ANQHRYWTPR CTVQETDGGH YLFSRFTHWS ALWNH // ID Q5F937_NEIG1 Unreviewed; 218 AA. AC Q5F937; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89300.1}; GN ORFNames=NGO_0567 {ECO:0000313|EMBL:AAW89300.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89300.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89300.1; -; Genomic_DNA. DR RefSeq; WP_003688991.1; NC_002946.2. DR RefSeq; YP_207712.1; NC_002946.2. DR ProteinModelPortal; Q5F937; -. DR EnsemblBacteria; AAW89300; AAW89300; NGO_0567. DR GeneID; 3282504; -. DR KEGG; ngo:NGO0567; -. DR PATRIC; 20334196; VBINeiGon24812_0670. DR HOGENOM; HOG000063753; -. DR OMA; LTKDMIF; -. DR OrthoDB; EOG657J9Z; -. DR BioCyc; NGON242231:GI2G-540-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 15 213 FAA_hydrolase. FT {ECO:0000259|Pfam:PF01557}. SQ SEQUENCE 218 AA; 23079 MW; 3D0B82A858B30504 CRC64; MASVFLEGEA VEVGNIFCIG RNYAAHVEEL KNEIPSEPVV FMKPSGSILN SGGTILLPEF SRDVQFECEL VLLIGRDSDG TGEGEDILGC VAGYGVGLDL TARDIQCRLK AQGLPWLKAK GFRHSACVSD FAAADRIGNQ DKVLFSLKQN GVLKQRGETG LMIYPIREIL HKLAADYGLG KGDLVFTGTP SGVGAIGAGD NLALELDGLV CASFTIGC // ID Q5F595_NEIG1 Unreviewed; 274 AA. AC Q5F595; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=DNA ligase {ECO:0000313|EMBL:AAW90642.1}; GN ORFNames=NGO_2034 {ECO:0000313|EMBL:AAW90642.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90642.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90642.1; -; Genomic_DNA. DR RefSeq; WP_010951387.1; NC_002946.2. DR RefSeq; YP_209054.1; NC_002946.2. DR ProteinModelPortal; Q5F595; -. DR DNASU; 3282713; -. DR EnsemblBacteria; AAW90642; AAW90642; NGO_2034. DR GeneID; 3282713; -. DR KEGG; ngo:NGO2034; -. DR PATRIC; 20337851; VBINeiGon24812_2449. DR HOGENOM; HOG000293070; -. DR KO; K10747; -. DR OMA; VRGYWDG; -. DR OrthoDB; EOG60919Q; -. DR BioCyc; NGON242231:GI2G-1935-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro. 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. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW90642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 45 193 DNA_LIGASE_A3. FT {ECO:0000259|Pfam:PF01068}. FT DOMAIN 207 271 DNA_ligase_OB_2. FT {ECO:0000259|Pfam:PF14743}. SQ SEQUENCE 274 AA; 30793 MW; 82F11159CF35F98D CRC64; MIKKIIGGII PIFTAVFIPA SAGAADLMLA QEYKGQDIAG WAMSEKLDGV RAYWDGKHLI SRQGYAFTPP KGFTAQFPPY PLDGELYSGR GQFEQISATV RSVSSDWRGI RLHVFDVPKA QGNLYQRLAV ATQWLKTHPN APITIIPQIK VRDRRHAMDF LKQIEVQGGE GVMLRQPESR YSGGRSSQLL KLKSQYDDEC TVTRHYEGKG RNAGRLGAVG CKNRHGEFRI GSGFKDKDRD NPPKIGTLIT YRYRGFTRKG TPKFATFVRV RTDR // ID Q5F7Y5_NEIG1 Unreviewed; 498 AA. AC Q5F7Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 68. DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AAW89702.1}; GN ORFNames=NGO_1026 {ECO:0000313|EMBL:AAW89702.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89702.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89702.1; -; Genomic_DNA. DR RefSeq; WP_003688230.1; NC_002946.2. DR RefSeq; YP_208114.1; NC_002946.2. DR ProteinModelPortal; Q5F7Y5; -. DR DNASU; 3281253; -. DR EnsemblBacteria; AAW89702; AAW89702; NGO_1026. DR GeneID; 3281253; -. DR KEGG; ngo:NGO1026; -. DR PATRIC; 20335266; VBINeiGon24812_1199. DR HOGENOM; HOG000284963; -. DR OMA; DKNTYIV; -. DR OrthoDB; EOG6WDSCH; -. DR BioCyc; NGON242231:GI2G-947-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 55517 MW; E7C0A9387BD6C553 CRC64; MTTENQAGSP ASGIGTSEQT KAAPKVKKTF 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 SGLIRYTTES ALEHEYAEKD IKKRLLRPRV AGYGAVLAVV VAAFLVGLST RKMVEVDILK DRGVMVRENA KGWLENAYSL RIINNSEKEQ LITASVKGFD EIALTGLPEG GIKVAPRETI TLPVQVSTIP EYADKGSHPI EFIFQYRESG ASDGKPVVLE EDATFIGE // ID Q5FAE6_NEIG1 Unreviewed; 67 AA. AC Q5FAE6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88841.1}; GN ORFNames=NGO_0080 {ECO:0000313|EMBL:AAW88841.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88841.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88841.1; -; Genomic_DNA. DR RefSeq; WP_003687334.1; NC_002946.2. DR RefSeq; YP_207253.1; NC_002946.2. DR EnsemblBacteria; AAW88841; AAW88841; NGO_0080. DR GeneID; 3282269; -. DR KEGG; ngo:NGO0080; -. DR PATRIC; 20333045; VBINeiGon24812_0106. DR HOGENOM; HOG000218770; -. DR OMA; WAEDENA; -. DR OrthoDB; EOG6VF37H; -. DR BioCyc; NGON242231:GI2G-70-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR019180; Oxidoreductase-like_N. DR Pfam; PF09791; Oxidored-like; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 19 58 Oxidoreductase-like. FT {ECO:0000259|Pfam:PF09791}. SQ SEQUENCE 67 AA; 7554 MW; 6D149064753EEC85 CRC64; MDTTLKHKAE ALLGEPLLDE PVRPESWECC GSDCGEACIQ TIYWADKARY DAQRKKLKEA GWPDDAV // ID Q5FA01_NEIG1 Unreviewed; 175 AA. AC Q5FA01; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW88986.1}; GN ORFNames=NGO_0233 {ECO:0000313|EMBL:AAW88986.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88986.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88986.1; -; Genomic_DNA. DR RefSeq; WP_003696762.1; NC_002946.2. DR RefSeq; YP_207398.1; NC_002946.2. DR ProteinModelPortal; Q5FA01; -. DR SMR; Q5FA01; 20-175. DR EnsemblBacteria; AAW88986; AAW88986; NGO_0233. DR GeneID; 3281494; -. DR KEGG; ngo:NGO0233; -. DR PATRIC; 20333411; VBINeiGon24812_0287. DR HOGENOM; HOG000218831; -. DR OMA; LNRASAH; -. DR OrthoDB; EOG6H1Q21; -. DR BioCyc; NGON242231:GI2G-217-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256086. FT DOMAIN 52 175 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 175 AA; 18478 MW; 44C05922D87FACF8 CRC64; MKKALAALIA LALPAAALAE GASGFYVQAD AAHAKASSSL GSAKGFSPRI SAGYRINDLR FAVDYTRYKN YKQAPSTDFK LYSIGASVIY DFDTQSPVKP YFGARLSLNR ASAHLGGSDS FSKTSAGLGV LAGVSYAVTP NVDLDAGYRY NYVGKVNNVK NVRSGELSAG VRVKF // ID Q5F8V7_NEIG1 Unreviewed; 157 AA. AC Q5F8V7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Iron-sulfur cluster repair protein DnrN {ECO:0000313|EMBL:AAW89380.1}; GN ORFNames=NGO_0653 {ECO:0000313|EMBL:AAW89380.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89380.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89380.1; -; Genomic_DNA. DR RefSeq; WP_003688853.1; NC_002946.2. DR RefSeq; YP_207792.1; NC_002946.2. DR ProteinModelPortal; Q5F8V7; -. DR EnsemblBacteria; AAW89380; AAW89380; NGO_0653. DR GeneID; 3282531; -. DR KEGG; ngo:NGO0653; -. DR PATRIC; 20334396; VBINeiGon24812_0770. DR HOGENOM; HOG000286324; -. DR KO; K07322; -. DR OMA; ACGTWTA; -. DR OrthoDB; EOG68DD4M; -. DR BioCyc; NGON242231:GI2G-620-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR012312; Haemerythrin-like. DR Pfam; PF01814; Hemerythrin; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 153 Hemerythrin. {ECO:0000259|Pfam:PF01814}. SQ SEQUENCE 157 AA; 17814 MW; 94AD46E15E4F18F8 CRC64; MTDFSVWEAA PFGATVDHIL QRYHNVHRAQ FEELVPLAQK VAQVHADTFP AEIAGLLADM RDELLMHMMK EERMLFPMIN QGVGRGAAMP ISVMMHEHEE HDRAIARLKE LTGNFHAPEG ACGSWTRLYA LAKEMADDLN DHIHLENDIL FARVLDS // ID Q5F719_NEIG1 Unreviewed; 469 AA. AC Q5F719; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90018.1}; GN ORFNames=NGO_1370 {ECO:0000313|EMBL:AAW90018.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90018.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90018.1; -; Genomic_DNA. DR RefSeq; WP_003702955.1; NC_002946.2. DR RefSeq; YP_208430.1; NC_002946.2. DR EnsemblBacteria; AAW90018; AAW90018; NGO_1370. DR GeneID; 3281374; -. DR KEGG; ngo:NGO1370; -. DR PATRIC; 20336127; VBINeiGon24812_1612. DR HOGENOM; HOG000129765; -. DR OMA; WWAMALP; -. DR OrthoDB; EOG6MPWQV; -. DR BioCyc; NGON242231:GI2G-1283-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 52177 MW; 754A7B19E3D7B4DF CRC64; MDTQIKTEAG QQNNRHYLSV WRWHFYAGLL VMPFLTLLAV TGLGMLLFAN ITGKEGERIH VFPQAVVQPL SVQAEAARGA INPETSSVVQ YIAPRADDMV AVFRVNNEGK ATMVAVDPYT AKVVNTMPRN QGWYHTMDEI HGDMMLGAAG DYLLETAASL TIIMVVSGLY LWWAKQRGIK AMLLPPKGRA RSWWRNLHGA FGTWVSLILL LFCLSGIAWA GIWGGKFVQA WSQFPAGKWG VEPNPVSVVP THGEVLNDGK VKEVPWILEL MPMPVSGTTV GENGINPSEP MTLETVDRFA REIGFKGRYQ LNLPKGEDGV WTLSQDSMSY DMISPFADRT VHIDQYSGKI LADIRFDDYN PFGKFMAASI ALHMGTLGWW SVLANVVFCL AVIFIGISGC VMWWKRRPSG VAGIVPPAQK IKLPVWWAMA LPLLLIALLF PTALLAIAVI WLLDTLLLSR IPVLRKWFK // ID Q5F857_NEIG1 Unreviewed; 193 AA. AC Q5F857; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Methionine biosynthesis protein MetW {ECO:0000313|EMBL:AAW89630.1}; GN ORFNames=NGO_0934 {ECO:0000313|EMBL:AAW89630.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89630.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89630.1; -; Genomic_DNA. DR RefSeq; WP_003688371.1; NC_002946.2. DR RefSeq; YP_208042.1; NC_002946.2. DR ProteinModelPortal; Q5F857; -. DR EnsemblBacteria; AAW89630; AAW89630; NGO_0934. DR GeneID; 3282567; -. DR KEGG; ngo:NGO0934; -. DR PATRIC; 20335051; VBINeiGon24812_1095. DR HOGENOM; HOG000266064; -. DR OMA; LPYEWYN; -. DR OrthoDB; EOG6SBT26; -. DR BioCyc; NGON242231:GI2G-872-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 193 AA; 21844 MW; A0C34495A1A0DEDD CRC64; MNLRDDLQLI YDRIPEGSRV LDLGCGDGEL LAALAEHKKC SGYGIEIDTD NVIAAMSRGV NVIQADLEEG LTAFNDQSFD VIVLSQTIQA MQNTEKILRC LMRLAKQAIV SFPNFGYWRN RVQIALGGHM PVSERMPYHW YDTPNIHWCT LKDFDLLCAK NNIRVLERAV MTGNRQVKHF PNLLGSLAFY RVG // ID Q5FA79_NEIG1 Unreviewed; 62 AA. AC Q5FA79; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88908.1}; GN ORFNames=NGO_0150 {ECO:0000313|EMBL:AAW88908.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88908.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88908.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88908; AAW88908; NGO_0150. DR PATRIC; 20333221; VBINeiGon24812_0193. DR OrthoDB; EOG6T4S88; -. DR BioCyc; NGON242231:GI2G-138-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 6934 MW; A7A4CD2F4A5AFD3E CRC64; MGPRFKKVRH CTFFKQDFQS ADAPAIGAGT VLWHNPHTNS RPRRSQAGSL FPRPIGFPLQ TA // ID Q5F7E8_NEIG1 Unreviewed; 53 AA. AC Q5F7E8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89889.1}; GN ORFNames=NGO_1230 {ECO:0000313|EMBL:AAW89889.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89889.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89889.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89889; AAW89889; NGO_1230. DR PATRIC; 20335775; VBINeiGon24812_1446. DR HOGENOM; HOG000027822; -. DR OrthoDB; EOG6CZQW1; -. DR BioCyc; NGON242231:GI2G-1141-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 5968 MW; 35F8D6523E7DF7CA CRC64; MPSEPLFRRH LFSLTHSRRH IAVPYYSGLN LNRYGVASPC RTICTVCGFA ALS // ID Q5F7T8_NEIG1 Unreviewed; 741 AA. AC Q5F7T8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:AAW89749.1}; DE EC=1.1.1.42 {ECO:0000313|EMBL:AAW89749.1}; GN ORFNames=NGO_1082 {ECO:0000313|EMBL:AAW89749.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89749.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89749.1; -; Genomic_DNA. DR RefSeq; WP_003706412.1; NC_002946.2. DR RefSeq; YP_208161.1; NC_002946.2. DR ProteinModelPortal; Q5F7T8; -. DR SMR; Q5F7T8; 7-741. DR PRIDE; Q5F7T8; -. DR EnsemblBacteria; AAW89749; AAW89749; NGO_1082. DR GeneID; 3281241; -. DR KEGG; ngo:NGO1082; -. DR PATRIC; 20335410; VBINeiGon24812_1271. DR HOGENOM; HOG000240860; -. DR KO; K00031; -. DR OMA; RDSGKMW; -. DR OrthoDB; EOG6DVJPP; -. DR BioCyc; NGON242231:GI2G-994-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89749.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 79949 MW; 7ACCDC90897C27CA CRC64; MTQKSTIVYT HTDEAPALAT QSLLPIVQAF ARHADIDVKT ADISLSGRIL AAFPEYLTEA QRVPDALAEL GELVKQPGAN VIKLPNISAS VPQLTAAIKE LQSKGFAVPD YPADPQTDEE KAVRERYDRI KGSAVNPVLR EGNSDRRAPK AVKNFAKKNP HSMGAWAKDS KTHVATMQSG DFFHNEQSVT VPDATSVSIV FTDKQGNKKE LREPVALKAG EIIDATVMSK KALLAFLAEQ VKDAKAKGVL FSLHMKATMM KVSDPIIFGH AVKVFFAPVF EKFGGKLAAA GVNVNNGFGN LIANLDKLDA DTRAAVEAEI AAVYAANPDL AMVDSDKGIT NLHVPSDVIV DASMPAMIRN SGRMWDKNGK AQDTKAVIPD SSYAGVYQAT IDFCREHGAF DPTTMGTVPN VGLMAQAAEE YGSHNKTFEI EADGQVQVID AAGNVLMQHD VEAGGIWRMC QTKDAPVKDW VQLAVNRARL SNTPAVFWLD ENRPHDKSLL AKVKAYLAEL DTNGLYIRVL APEEAAKFSL GRLKNGEDTI SVTGNVLRDY LTDLFPILEL GTSAKMLSIV PLMNGGGMFE TGAGGSAPKH VQQFLEENHL RWDSLGEFLA LAVSFEHLAQ KTGNAKAQVL ADTLDAATEK LLLNDKSPKR KAGELDNRGS HFYLTLYWAQ ELAAQDKDAE LKAAFAPLAA ALTADEAKIV EELSAVQGKA VDIGGYYAAN PEKAAQAMRP SATFNQVLNA L // ID Q5F6I3_NEIG1 Unreviewed; 318 AA. AC Q5F6I3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. 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 ORFNames=NGO_1575 {ECO:0000313|EMBL:AAW90204.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90204.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90204.1; -; Genomic_DNA. DR RefSeq; WP_003689496.1; NC_002946.2. DR RefSeq; YP_208616.1; NC_002946.2. DR ProteinModelPortal; Q5F6I3; -. DR EnsemblBacteria; AAW90204; AAW90204; NGO_1575. DR GeneID; 3281409; -. DR KEGG; ngo:NGO1575; -. DR PATRIC; 20336676; VBINeiGon24812_1884. DR HOGENOM; HOG000228429; -. DR KO; K00946; -. DR OMA; GRHFFAD; -. DR OrthoDB; EOG6RRKQ4; -. DR BioCyc; NGON242231:GI2G-1472-MONOMER; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000000535; 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:UP000000535}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:AAW90204.1}; 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:UP000000535}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128, KW ECO:0000313|EMBL:AAW90204.1}. FT DOMAIN 25 133 AIRS. {ECO:0000259|Pfam:PF00586}. FT DOMAIN 202 298 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; 34369 MW; 0DEFB176E556875F CRC64; MKEFDFIKRY LQTGTDKDVV LGIGDDAAIV RPREGFDLCF SADMLLKDRH FFADVKPEGL AWKVLAVNIS DMAAMGAIPR WVLLSAALPE LDEVWLERFC GSFFGLAKKF GVTLIGGDTT KGDMAFNVTI IGELPKGRAL RRDAAVAGDD IWVSGRVGMA AAALNCRLKR CVLPDDVFAE CEQKLLRPEP RVGLGLALLP FARAAQDVSD GLAQDLGHIL TASGVGAEIW ADSLPSLSVL KDILPRAQWL SYTLAGGDDY ELVFTAPESC RSRVLDAAER CGVPVTCIGK INGGCRLKVL DAGGRELELH SLGFDHFG // ID Q5F7B9_NEIG1 Unreviewed; 767 AA. AC Q5F7B9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. 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 ORFNames=NGO_1259 {ECO:0000313|EMBL:AAW89918.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89918.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89918.1; -; Genomic_DNA. DR RefSeq; WP_010951227.1; NC_002946.2. DR RefSeq; YP_208330.1; NC_002946.2. DR ProteinModelPortal; Q5F7B9; -. DR EnsemblBacteria; AAW89918; AAW89918; NGO_1259. DR GeneID; 3281849; -. DR KEGG; ngo:NGO1259; -. DR PATRIC; 20335849; VBINeiGon24812_1479. DR HOGENOM; HOG000076277; -. DR KO; K02621; -. DR OMA; RFTEDAY; -. DR OrthoDB; EOG661H5V; -. DR BioCyc; NGON242231:GI2G-1176-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:UP000000535}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00936}. FT DOMAIN 15 487 TOP4c. {ECO:0000259|SMART:SM00434}. 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; 84457 MW; FF1C176A37BA704E CRC64; MNTQPHASHT DSNTLMLGRY AERAYLEYAM SVVKGRALPE VSDGQKPVQR RILFAMRDMG LTAGAKPVKS ARVVGEILGK YHPHGDSSAY EAMVRMAQDF TLRYPLIDGI GNFGSRDGDG AAAMRYTEAR LTPIAELLLS EINQGTVDFM PNYDGAFDEP LHLPARLPMV LLNGASGIAV GMATEIPSHN LNEVTQAAIA LLKKPTLETA DLMQYIPAPD FAGGGQIITP ADELRRIYET GKGSVRVRAR YEIEKLARGQ WRVIVTELPP NANSAKILAE IEEQTNPKPK AGKKQLNQDR LNTKKLMLDL IDRVRDESDG EHPVRLVFEP KSSRIDTDTF INTLMAQTSL EGNVSMNLVM MGLDNRPAQK NLKTILQEWL DFRVVTVTRR LKFRLNQVEK RLHILEGRLK VFLHIDEVIK VIRESDDPKA DLMAVFGLTE IQAEDILEIR LRQLARLEGF KLEKELNELR EEQGRLNIFL GDENEKRKLI IKEMQADMKQ FGDARRTLVE EAGRAVLTQT AADEPITLIL SEKGWIRSRA GHNLDLSQTA FKEGDRLKQT LEGRTVLPVV ILDSSGRTYS IDAAEIPGGR GDGVPVSSLI ELQNGAKPVA MLTGLPEQHY LLSSSGGYGF IAKLGDMVGR VKAGKVVMTA DSGETVLPPV AVYASSFINP DCKIIAATSQ NRALAFPIGE LKIMAKGKGL QIIGLNAGES MTHTAVSSEP EILIESEGRR GAAHKDRLPV ALIEAKRGKK GRLLPISGSL KQLSSPK // ID Q5F6T3_NEIG1 Unreviewed; 59 AA. AC Q5F6T3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90104.1}; GN ORFNames=NGO_1463 {ECO:0000313|EMBL:AAW90104.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90104.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90104.1; -; Genomic_DNA. DR RefSeq; WP_010951276.1; NC_002946.2. DR RefSeq; YP_208516.1; NC_002946.2. DR EnsemblBacteria; AAW90104; AAW90104; NGO_1463. DR GeneID; 3281665; -. DR KEGG; ngo:NGO1463; -. DR PATRIC; 20336357; VBINeiGon24812_1727. DR BioCyc; NGON242231:GI2G-1369-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 59 AA; 6179 MW; C4BC624CC83A7374 CRC64; MFGLYCQLCR LKMPFARSCA LKMPSEGSDG IGIGESEKMP SEGSDGIGIG ESEAVAHAQ // ID Q5F8H1_NEIG1 Unreviewed; 89 AA. AC Q5F8H1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89516.1}; GN ORFNames=NGO_0802 {ECO:0000313|EMBL:AAW89516.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89516.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89516.1; -; Genomic_DNA. DR RefSeq; WP_003695196.1; NC_002946.2. DR RefSeq; YP_207928.1; NC_002946.2. DR EnsemblBacteria; AAW89516; AAW89516; NGO_0802. DR GeneID; 3282047; -. DR KEGG; ngo:NGO0802; -. DR PATRIC; 20334758; VBINeiGon24812_0949. DR HOGENOM; HOG000071287; -. DR OMA; CSTCCRE; -. DR OrthoDB; EOG64V2NJ; -. DR BioCyc; NGON242231:GI2G-758-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 89 AA; 10868 MW; 12C6BFF6865E325B CRC64; MFCGMFYPLP KPVRTQKAYP FKQYCSTCCR ETEPDTETRR GDMPLEKWRQ FLDWIGKTPS ETASRSRKAR PNKKYRLKFF RRHRVSFKH // ID Q5F9W0_NEIG1 Unreviewed; 267 AA. AC Q5F9W0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=Outer membrane protein assembly factor BamD {ECO:0000256|HAMAP-Rule:MF_00922}; DE Flags: Precursor; GN Name=bamD {ECO:0000256|HAMAP-Rule:MF_00922}; GN ORFNames=NGO_0277 {ECO:0000313|EMBL:AAW89027.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89027.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00922}. CC -!- SUBUNIT: Part of the Bam complex. {ECO:0000256|HAMAP- CC Rule:MF_00922}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000256|HAMAP- CC Rule:MF_00922}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_00922}. CC -!- SIMILARITY: Belongs to the BamD family. {ECO:0000256|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; AE004969; AAW89027.1; -; Genomic_DNA. DR RefSeq; WP_003687645.1; NC_002946.2. DR RefSeq; YP_207439.1; NC_002946.2. DR PRIDE; Q5F9W0; -. DR EnsemblBacteria; AAW89027; AAW89027; NGO_0277. DR GeneID; 3281625; -. DR KEGG; ngo:NGO0277; -. DR PATRIC; 20333527; VBINeiGon24812_0344. DR HOGENOM; HOG000260923; -. DR KO; K05807; -. DR OMA; IHVADYY; -. DR OrthoDB; EOG6WHNPP; -. DR BioCyc; NGON242231:GI2G-259-MONOMER; -. DR Proteomes; UP000000535; 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 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. PE 3: Inferred from homology; KW Cell outer membrane {ECO:0000256|HAMAP-Rule:MF_00922}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_00922}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00922}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_00922}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00922}. FT SIGNAL 1 16 {ECO:0000256|HAMAP-Rule:MF_00922}. FT CHAIN 17 267 Outer membrane protein assembly factor FT BamD. {ECO:0000256|HAMAP-Rule:MF_00922}. FT /FTId=PRO_5005078175. FT LIPID 17 17 N-palmitoyl cysteine. {ECO:0000256|HAMAP- FT Rule:MF_00922}. FT LIPID 17 17 S-diacylglycerol cysteine. FT {ECO:0000256|HAMAP-Rule:MF_00922}. SQ SEQUENCE 267 AA; 30839 MW; FF4F6BB1A0627EB4 CRC64; MKKILLTVSL GLALSACATQ GTADKDAQIT QDWSVEKLYA EAQDELNSSN YTRAVKLYEI LESRFPTSRH ARQSQLDTAY AYYKDDEKDK ALAAIERFRR LHPQHPNMDY ALYLRGLVLF NEDQSFLNKL ASQDWSDRDP KANREAYQAF AELVQRFPNS KYAADATARM VKLVDALGGN EMSVARYYMK RGAYIAAANR AKKIIGSYQN TRYVEESLAI LELAYKKLDK PQLAADTRRV LETNFPKSPF LTHAWQPDDM PWWRYWH // ID Q5F502_NEIG1 Unreviewed; 228 AA. AC Q5F502; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 74. DE SubName: Full=Methionine ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90735.1}; GN ORFNames=NGO_2138 {ECO:0000313|EMBL:AAW90735.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90735.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90735.1; -; Genomic_DNA. DR RefSeq; WP_003692419.1; NC_002946.2. DR RefSeq; YP_209147.1; NC_002946.2. DR ProteinModelPortal; Q5F502; -. DR EnsemblBacteria; AAW90735; AAW90735; NGO_2138. DR GeneID; 3282783; -. DR KEGG; ngo:NGO2138; -. DR PATRIC; 20338125; VBINeiGon24812_2585. DR HOGENOM; HOG000222815; -. DR KO; K02072; -. DR OMA; RYQTEVM; -. DR OrthoDB; EOG6P073X; -. DR BioCyc; NGON242231:GI2G-2029-MONOMER; -. DR Proteomes; UP000000535; 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: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 ATP-binding {ECO:0000313|EMBL:AAW90735.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW90735.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 24278 MW; 49B9193EC60A7114 CRC64; MADLTFEQAV STIVGMKDEI VRALGETFVM VGLSTTFAVI FGTLLGVLLF VTSSRQLHYN KPVNFLLDNL VNLMRAFPFV ILMIAMIPAT RAIVGSTIGP VAASLVLSVS GLFYFARLVE QNLREVPKGV IEAAAAMGAP PIAIVLKVLL NEARAGMVSS ITVLAIGLLS YSAAAGMIGG GGLGDLAIRY GYYRYQTEVI VFIVALLVLL VILIQSTGNA LARKLDKR // ID Q5F515_NEIG1 Unreviewed; 162 AA. AC Q5F515; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:AAW90722.1}; GN ORFNames=NGO_2124 {ECO:0000313|EMBL:AAW90722.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90722.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90722.1; -; Genomic_DNA. DR RefSeq; WP_003690423.1; NC_002946.2. DR RefSeq; YP_209134.1; NC_002946.2. DR ProteinModelPortal; Q5F515; -. DR EnsemblBacteria; AAW90722; AAW90722; NGO_2124. DR GeneID; 3282796; -. DR KEGG; ngo:NGO2124; -. DR PATRIC; 20338095; VBINeiGon24812_2570. DR HOGENOM; HOG000097217; -. DR OMA; EPEWDAL; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NGON242231:GI2G-2016-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 22 161 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 162 AA; 17539 MW; 65CC79AA7C47EBA8 CRC64; MKKILTAAAV ALIGILLATV LIPDSKTAPA FSLPDLHGKT VSNADLQGKV TLINFWFPSC PGCVSEMPKV TKTANDYKNK DFQVLAVAQP IDPIESVRQY VKDYGLPFTV IYDADKAVGQ AFGTQVYPTS VLIGKKGEIL KTYVGEPDFG KLYQEIDTAL AQ // ID Q5F9A1_NEIG1 Unreviewed; 499 AA. AC Q5F9A1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89236.1}; GN ORFNames=NGO_0498 {ECO:0000313|EMBL:AAW89236.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89236.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89236.1; -; Genomic_DNA. DR RefSeq; WP_010951063.1; NC_002946.2. DR RefSeq; YP_207648.1; NC_002946.2. DR EnsemblBacteria; AAW89236; AAW89236; NGO_0498. DR GeneID; 3282951; -. DR KEGG; ngo:NGO0498; -. DR PATRIC; 20334038; VBINeiGon24812_0591. DR HOGENOM; HOG000057660; -. DR OMA; QIEWPLR; -. DR OrthoDB; EOG6Z0Q67; -. DR BioCyc; NGON242231:GI2G-476-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 499 AA; 52621 MW; 734043ABD58D95EF CRC64; MNVNQLTQET IELMKSAQAG GGPPDKGFTQ PASFTAGLQT YDLSAPSQKL YPVLTPLRNR IPRVGGGRTI GSNWKAVTNI NVGNQRAGIG EGRRGGVINH ETVERNAQFR AIGLENQVTF EADYAARGFE DVKALAVAQT LQATMVAEEM ILLGGNTSLK AGVTPTPTAV VSADAAGKIS VSTLSVICVA LGLQAYWDVA GANNGATGQS PNIKTAQVPA KITRRNADGT TDTFGGGSAR KSAAASVSGI EAGKKVTAVI PAVRGAVAYA WYWGAAGSEK LGAVTTAAKV EISADAEGTQ TAASLPSEDN STSILEFDGL LTQIALPDSG AFWSDNKGGG LTSDNAGGVY EFEEAFAHFF TRYRLSPDTV YVNARDLAAL TKLIIGNSGA PLIKLNVDVN NTANIRAGVV VGSYMNKITG DDLNIVVHPN LPAGTYLFYS SRLPAYVQGV GNLLQVRTRQ EYYQIEWPLR TRMYEYGVYA DEVLQGMFMP AFGMITNVG // ID Q5F5M8_NEIG1 Unreviewed; 335 AA. AC Q5F5M8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Modification methylase HphIB {ECO:0000313|EMBL:AAW90509.1}; GN ORFNames=NGO_1893 {ECO:0000313|EMBL:AAW90509.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90509.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90509.1; -; Genomic_DNA. DR RefSeq; WP_003690162.1; NC_002946.2. DR RefSeq; YP_208921.1; NC_002946.2. DR ProteinModelPortal; Q5F5M8; -. DR REBASE; 10866; M1.NgoAXVI. DR DNASU; 3282158; -. DR EnsemblBacteria; AAW90509; AAW90509; NGO_1893. DR GeneID; 3282158; -. DR KEGG; ngo:NGO1893; -. DR PATRIC; 20337490; VBINeiGon24812_2276. DR HOGENOM; HOG000071364; -. DR OMA; QSHKEIL; -. DR OrthoDB; EOG69WFFJ; -. DR BioCyc; NGON242231:GI2G-1793-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. 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. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW90509.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90509.1}. SQ SEQUENCE 335 AA; 39477 MW; 8BD6FD601D4DA5A1 CRC64; MNKKYPKINY IGNKEKIASW ICDQLPSDVD TVADVFSGGC SFAYEAKKRG YRVITNDILA INYQIALALI ENNHETLNDD DVAMIFSGSP HAGFMSQRYS EKFYFHDECQ QLDLYRKNIG KLNNQYKRAL AFTLMRRAMI RKMPYSRFTI PWEKVKQLRD EEYSYAKYGR RRAYHNESFQ SHFLQNLDDY NQAVFNNGWR HHAFNQDIFD LLPNIQADAV YLDPPYTGTM NNYFGFYGLL DSYITSSIPK PFANHFMDKK QAVELFKRVI NHLKPFKYWL LSYNNASYPN RDELEEMLGK NGRNVQILET PHVYKVTGKE KKQSHKEILF LVENT // ID Q5F8Q2_NEIG1 Unreviewed; 481 AA. AC Q5F8Q2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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 ORFNames=NGO_0715 {ECO:0000313|EMBL:AAW89435.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89435.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89435.1; -; Genomic_DNA. DR RefSeq; WP_003693052.1; NC_002946.2. DR RefSeq; YP_207847.1; NC_002946.2. DR ProteinModelPortal; Q5F8Q2; -. DR EnsemblBacteria; AAW89435; AAW89435; NGO_0715. DR GeneID; 3282883; -. DR KEGG; ngo:NGO0715; -. DR PATRIC; 20334558; VBINeiGon24812_0851. DR HOGENOM; HOG000046191; -. DR KO; K00036; -. DR OMA; DNIYENT; -. DR OrthoDB; EOG61308Z; -. DR BioCyc; NGON242231:GI2G-675-MONOMER; -. DR UniPathway; UPA00115; UER00408. DR Proteomes; UP000000535; 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:UP000000535}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 53889 MW; 87FC1F27DB908BF4 CRC64; MSTQTNFDLV LFGATGDLAM RKLLPCLYQA HVAGLLHPEG RILGVSRSEL DTEGFLAKVE TSSKIHVKEN FSGEAWASFV ERLAYLKVDV TQPDDFAALG DLVKARKETD NVVIYLSTAP KFFAQACENL AAIGLNADNV RVVLEKPLGT DLASSQQINT DVARYFKEGQ IYRIDHYLGK ESLQNLLALR FANVMFEPLW NNKYIESVQL TIAEQLGVEE RGEFYDITGA LRDMVQNHLM QMLCMTAMEA PAGLDADAVR DEKVKVIKSL KPLTIESVNE NVVRGQYTAA KGMNGYLEEI NVPQDSFTET YVAIKAEIEN ERWKGVPFYL RTGKRMAGKV AEIVLNFRPL QNHIFDNSQT APNRLVIELQ PNESVRLYTQ VKTPGAGNKV EVTPLGVDLG KAVEGRRAEA YERLLLDVIN GKLALFNRRD ELEAAWEYVM PILENWANNT TPPHGYGAHS WGPEAARELL ARDGNKWHEE Q // ID Q5F7U6_NEIG1 Unreviewed; 94 AA. AC Q5F7U6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89741.1}; GN ORFNames=NGO_1072 {ECO:0000313|EMBL:AAW89741.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89741.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89741.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89741; AAW89741; NGO_1072. DR PATRIC; 20335380; VBINeiGon24812_1256. DR HOGENOM; HOG000220773; -. DR OMA; PRWPHEE; -. DR OrthoDB; EOG651SXH; -. DR BioCyc; NGON242231:GI2G-986-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10541 MW; 0AF9FB32BDC42377 CRC64; MAGGNKSLKI GTQSVEKSTG RTIPNNLKEQ LAMEEVKANP QGKTPARIPP MSDTKNGWLA KDGWVKRVQN INKVEIHYIE NTRTGEKTDF KFKD // ID Q5F572_NEIG1 Unreviewed; 160 AA. AC Q5F572; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Damage-inducible protein CinA {ECO:0000313|EMBL:AAW90665.1}; GN ORFNames=NGO_2058 {ECO:0000313|EMBL:AAW90665.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90665.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90665.1; -; Genomic_DNA. DR RefSeq; WP_003694396.1; NC_002946.2. DR RefSeq; YP_209077.1; NC_002946.2. DR ProteinModelPortal; Q5F572; -. DR EnsemblBacteria; AAW90665; AAW90665; NGO_2058. DR GeneID; 3282738; -. DR KEGG; ngo:NGO2058; -. DR PATRIC; 20337917; VBINeiGon24812_2481. DR HOGENOM; HOG000242527; -. DR KO; K03743; -. DR OMA; TVWFAWA; -. DR OrthoDB; EOG61S359; -. DR BioCyc; NGON242231:GI2G-1959-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 150 CinA. {ECO:0000259|Pfam:PF02464}. SQ SEQUENCE 160 AA; 16801 MW; 8365BB7691C35077 CRC64; MDALHTIARN LTKKRQTVSC AESCTGGMLA AAFTSVAGSS QWFDQSFVTY SNKAKEYRLG VLPETLLEHG AVSRQTVYEM ARGAKAVAQA DYAVGISGIA GPGGGESKPV GTVWFGFAFP GGSCEAMRRF DGNRESVRAQ AVAFALERLA GLVENGGDAV // ID Q5F6P7_NEIG1 Unreviewed; 416 AA. AC Q5F6P7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 60. DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AAW90140.2}; GN Name=amiC {ECO:0000313|EMBL:AAW90140.2}; GN ORFNames=NGO_1502 {ECO:0000313|EMBL:AAW90140.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90140.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90140.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6P7; -. DR DNASU; 3281582; -. DR EnsemblBacteria; AAW90140; AAW90140; NGO_1502. DR PATRIC; 20336478; VBINeiGon24812_1787. DR HOGENOM; HOG000263827; -. DR OMA; KRYFAAN; -. DR OrthoDB; EOG6CP3X3; -. DR BioCyc; NGON242231:GI2G-1406-MONOMER; -. DR Proteomes; UP000000535; 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; -; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 416 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364408. FT DOMAIN 251 405 Ami_3. {ECO:0000259|SMART:SM00646}. SQ SEQUENCE 416 AA; 45133 MW; F1E08493382E09A7 CRC64; MTKLTRRQII RRTAGTLFAL SPIASAVAKT VRAPQFTAAR IWPSHTYTRL TLESTAALKY QHFALDNPGR LVVDIQNANI NTVLHGLSQK VMADDPFIRS IRAGQNTPTT VRLVIDLKQP THAQVFALPP VGGFKDRLVV DLYPHGMDAD DPMMALLNGS LNKTLRGSPE ADPAQNTTPR PGRGKNGRRP VIMLDPGHGG EDPGAVSPGG LQEKHVVLSI ARETKKQLEA LGYNVFMTRN EDVFIPLGVR VAKGRARRAD VFVSIHADAF TSPSARGTGV YMLNTKGATS SAAKFLEQTQ NNADAVGGVP TSGNRNVDTA LLDMTQTATL RDSRKLGKLV LEELGRLNHL HKGRVDEANF AVLRAPDMPS ILVETAFLSN PAEEKLLGSE SFRRQCAQSI ASGVQRYINT SVLKRG // ID Q5F8U4_NEIG1 Unreviewed; 142 AA. AC Q5F8U4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=YSIRK family Signal peptide {ECO:0000313|EMBL:AAW89393.1}; GN ORFNames=NGO_0666 {ECO:0000313|EMBL:AAW89393.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89393.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89393.1; -; Genomic_DNA. DR RefSeq; WP_003688825.1; NC_002946.2. DR RefSeq; YP_207805.1; NC_002946.2. DR EnsemblBacteria; AAW89393; AAW89393; NGO_0666. DR GeneID; 3282058; -. DR KEGG; ngo:NGO0666; -. DR PATRIC; 20334428; VBINeiGon24812_0786. DR HOGENOM; HOG000218997; -. DR OMA; EILMNFA; -. DR OrthoDB; EOG6GBMBP; -. DR BioCyc; NGON242231:GI2G-633-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 142 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256626. FT DOMAIN 13 67 DUF4124. {ECO:0000259|Pfam:PF13511}. FT COILED 72 116 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 142 AA; 15821 MW; 44D36D5038A41F93 CRC64; MNFALSVITF TLASFLPVPP AGTAVFTWKD GGGNSYSDVP KQLHPDQSQI LNLRTLQTKP AVKPKPAVDT NADSAKENEK DIAEKNGQLE EEKKKIAETE RQNKEENCRI SKMNLKAVGN SNAKNKDDLI RKYNNAVNKY CR // ID Q5F9T9_NEIG1 Unreviewed; 137 AA. AC Q5F9T9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Restriction endonuclease HpaII {ECO:0000313|EMBL:AAW89048.1}; GN ORFNames=NGO_0300 {ECO:0000313|EMBL:AAW89048.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89048.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89048.1; -; Genomic_DNA. DR RefSeq; WP_003690774.1; NC_002946.2. DR RefSeq; YP_207460.1; NC_002946.2. DR ProteinModelPortal; Q5F9T9; -. DR REBASE; 10868; V.NgoAXIII. DR EnsemblBacteria; AAW89048; AAW89048; NGO_0300. DR GeneID; 3281315; -. DR KEGG; ngo:NGO0300; -. DR PATRIC; 20333585; VBINeiGon24812_0372. DR HOGENOM; HOG000239922; -. DR KO; K07458; -. DR OMA; HGCPEHH; -. DR OrthoDB; EOG6VXFGP; -. DR BioCyc; NGON242231:GI2G-281-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR Gene3D; 3.40.960.10; -; 1. DR InterPro; IPR004603; DNA_mismatch_endonuc_vsr. DR InterPro; IPR007569; DUF559. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF04480; DUF559; 1. DR Pfam; PF03852; Vsr; 1. DR PIRSF; PIRSF018267; VSR_endonuc; 1. DR SUPFAM; SSF52980; SSF52980; 1. DR TIGRFAMs; TIGR00632; vsr; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89048.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89048.1}; KW Nuclease {ECO:0000313|EMBL:AAW89048.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 93 134 DUF559. {ECO:0000259|Pfam:PF04480}. SQ SEQUENCE 137 AA; 16002 MW; BA9B9CD0031C1B2B CRC64; MDKLTPEQRK KCMQSNKSTG TKPELVLAKA MWALGLRYRK NSGSIFGKPD FSFKKYKVAV FVDGEFWHGK DWEQKKAVIK GNREFWIAKI ERNIQRDIEV TGRLKAEGWT VLRFWSNDVV KNTTCCAEKV KEIIQTR // ID Q5F9T2_NEIG1 Unreviewed; 433 AA. AC Q5F9T2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 79. 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 ORFNames=NGO_0308 {ECO:0000313|EMBL:AAW89055.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89055.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89055.1; -; Genomic_DNA. DR RefSeq; WP_003687694.1; NC_002946.2. DR RefSeq; YP_207467.1; NC_002946.2. DR ProteinModelPortal; Q5F9T2; -. DR SMR; Q5F9T2; 8-432. DR EnsemblBacteria; AAW89055; AAW89055; NGO_0308. DR GeneID; 3281697; -. DR KEGG; ngo:NGO0308; -. DR PATRIC; 20333599; VBINeiGon24812_0379. DR HOGENOM; HOG000020209; -. DR KO; K00833; -. DR OMA; MAVQYQQ; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NGON242231:GI2G-288-MONOMER; -. DR UniPathway; UPA00078; UER00160. DR Proteomes; UP000000535; 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:AAW89055.1}; KW Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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:UP000000535}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00834, KW ECO:0000313|EMBL:AAW89055.1}. 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; 47968 MW; 2FDE2F82D79D554E CRC64; MPSEHQHTSS LLNFDRTHLL HPYTSMTDPL PVYPVKRAEG VFIELADGTR LIDGMSSWWC AIHGYNHPVL NQAVENQMKQ MAHVMFGGLT HEPAVELGKL LVGILPQGLD RIFYADSGSV SVEVALKMAV QYQQARGLTA KQNIATVRRG YHGDTWNAMS VCDPETGMHH IFGSALPQRY FVDNPKNRFD DEWDGADLQP VRALFEAHHV DIAAFILEPV VQGAGGMYFY HPQYLRGLRD LCDEFDIVLI FDEIATGFGR TGKMFACEHA EVVPDIMCIG KGLSGGYMTL AAAITSQKVT ETISRGEAGV FMHGPTFMAN PLACAVACAS VKLLLSQDWQ ANIRRIESIL KGRLKAAWDI RGVKDVRVLG AIGVIELEKG VDMARFQADC VAQGIWVRPF GRLVYLMPPY IISDGILTKL ADKTVQILKE HSK // ID Q5F9R6_NEIG1 Unreviewed; 124 AA. AC Q5F9R6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=SirB family protein {ECO:0000313|EMBL:AAW89071.1}; GN ORFNames=NGO_0324 {ECO:0000313|EMBL:AAW89071.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89071.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89071.1; -; Genomic_DNA. DR RefSeq; WP_003687714.1; NC_002946.2. DR RefSeq; YP_207483.1; NC_002946.2. DR EnsemblBacteria; AAW89071; AAW89071; NGO_0324. DR GeneID; 3281761; -. DR KEGG; ngo:NGO0324; -. DR PATRIC; 20333637; VBINeiGon24812_0396. DR HOGENOM; HOG000270268; -. DR OMA; AIAWVVY; -. DR OrthoDB; EOG65F8WK; -. DR BioCyc; NGON242231:GI2G-306-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 117 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 124 AA; 14571 MW; DD962E8BED93F50B CRC64; MQYLIVKYSH QIFVTITILV FNIRFFLLWK NPEKPLVGFW KALPHLNDTM LLFTGLWLMK ITHFSPFNAP WLGTKILLLF AYIALGMVMM RARPRSTKFY TVYLLAMCCI ACIVYLAKTK VLPF // ID Q5F7Z4_NEIG1 Unreviewed; 144 AA. AC Q5F7Z4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89693.1}; GN ORFNames=NGO_1010 {ECO:0000313|EMBL:AAW89693.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89693.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89693.1; -; Genomic_DNA. DR RefSeq; WP_010951161.1; NC_002946.2. DR RefSeq; YP_208105.1; NC_002946.2. DR EnsemblBacteria; AAW89693; AAW89693; NGO_1010. DR GeneID; 3282182; -. DR KEGG; ngo:NGO1010; -. DR PATRIC; 20335228; VBINeiGon24812_1182. DR OrthoDB; EOG6Z3KT3; -. DR BioCyc; NGON242231:GI2G-936-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 144 AA; 16790 MW; 79DCB7F13DD3F5C7 CRC64; MALMETTDDL FSRTLAILKE ANQPQEELLP QLSQLYQKEI GLVPEVDKKT NMIFLETFQS SISQSSILSD IRSLLNEKKY IAKRIKENAE EMYFFSQPAA LLVYWLIEKV GADEVWKKWP LPAYNKNLKF ICTDLDKQPS HELF // ID Q5F673_NEIG1 Unreviewed; 81 AA. AC Q5F673; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90314.1}; GN ORFNames=NGO_1690 {ECO:0000313|EMBL:AAW90314.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90314.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90314.1; -; Genomic_DNA. DR RefSeq; WP_003689849.1; NC_002946.2. DR RefSeq; YP_208726.1; NC_002946.2. DR EnsemblBacteria; AAW90314; AAW90314; NGO_1690. DR GeneID; 3281217; -. DR KEGG; ngo:NGO1690; -. DR PATRIC; 20336944; VBINeiGon24812_2016. DR HOGENOM; HOG000219119; -. DR OMA; IADYISH; -. DR OrthoDB; EOG6ND0N9; -. DR BioCyc; NGON242231:GI2G-1584-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 81 AA; 9499 MW; 6822FD82B057DC52 CRC64; MLKSIELNSH IRNRLAAYLK GRGLDFQTAM QEEEGNKEIA AIVHSGLPTL VRKLYSEQKM QKFFWEKRDL IADYISRRMQ G // ID Q5F8L5_NEIG1 Unreviewed; 144 AA. AC Q5F8L5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Periplasmic protein {ECO:0000313|EMBL:AAW89472.1}; GN ORFNames=NGO_0757 {ECO:0000313|EMBL:AAW89472.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89472.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89472.1; -; Genomic_DNA. DR RefSeq; WP_003688677.1; NC_002946.2. DR RefSeq; YP_207884.1; NC_002946.2. DR EnsemblBacteria; AAW89472; AAW89472; NGO_0757. DR GeneID; 3281881; -. DR KEGG; ngo:NGO0757; -. DR PATRIC; 20334662; VBINeiGon24812_0903. DR HOGENOM; HOG000218967; -. DR OMA; NCHNTIF; -. DR OrthoDB; EOG6MH5CF; -. DR BioCyc; NGON242231:GI2G-712-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 144 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256622. SQ SEQUENCE 144 AA; 16615 MW; 15403472ECF0D366 CRC64; MPLPAPCRFA KPAASFLSMA LLSCQLSHAA TAYIPPNDFQ PNCDIRRLGL TQGQHNELRK IRAAFKMAGD RARLKVMHSE HSRRRSVVEI ISSDVFNRNE ARDYVESRYH SSMDFAVDEL EIQHRFFHIL TPQQQQMWLS SCLK // ID Q5FAA6_NEIG1 Unreviewed; 384 AA. AC Q5FAA6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Cupin {ECO:0000313|EMBL:AAW88881.1}; GN ORFNames=NGO_0121 {ECO:0000313|EMBL:AAW88881.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88881.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88881.1; -; Genomic_DNA. DR RefSeq; WP_003694771.1; NC_002946.2. DR RefSeq; YP_207293.1; NC_002946.2. DR ProteinModelPortal; Q5FAA6; -. DR DNASU; 3282395; -. DR EnsemblBacteria; AAW88881; AAW88881; NGO_0121. DR GeneID; 3282395; -. DR KEGG; ngo:NGO0121; -. DR PATRIC; 20333145; VBINeiGon24812_0156. DR HOGENOM; HOG000220698; -. DR OMA; HWDIRDV; -. DR OrthoDB; EOG676Z13; -. DR BioCyc; NGON242231:GI2G-110-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 95 238 JmjC. {ECO:0000259|PROSITE:PS51184}. SQ SEQUENCE 384 AA; 44410 MW; E687DD98181E60B2 CRC64; MGIHLDFGIS PKTFRQTYLY QKPKLFKGAV RNLEAASCKY INEIYQRADP TAPLFHLRKK GAIVPKEEYV ESFDDLGKTR YRFIKSVIYE HMKNGASLVY NHINNEPFSD HIARQVARFA GAHTIVSGYL AFGSDESYKN HWDTRDVYAI QLFGKKRWQL TAPDFPMPLY MQQTKDTDIS IPEHIDMDII LEAGDVLYIP RGWWHRPIPL GCETFHFAVG TFPPNGYNYL EWLMKKFPTI ESLRHSFSDW EQDRTRINDT AAQIAAMIAD PVNYEAFSED FLGKERTDTA FHLEQFANPN ATPLSDDVRL RLNANNLDTL EKGYLIGNGM KISVDELGKK VLEHIGKNEP LLLKNLLVNF NQAKHEEVRK LIYQLIELDF LEIL // ID Q5F905_NEIG1 Unreviewed; 561 AA. AC Q5F905; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 65. DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111}; GN Name=rpsA {ECO:0000313|EMBL:AAW89332.1}; GN ORFNames=NGO_0604 {ECO:0000313|EMBL:AAW89332.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89332.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|PIRNR:PIRNR002111}. CC -!- SIMILARITY: Belongs to the ribosomal protein S1P family. CC {ECO:0000256|PIRNR:PIRNR002111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89332.1; -; Genomic_DNA. DR RefSeq; WP_003691321.1; NC_002946.2. DR RefSeq; YP_207744.1; NC_002946.2. DR ProteinModelPortal; Q5F905; -. DR SMR; Q5F905; 360-402. DR PRIDE; Q5F905; -. DR EnsemblBacteria; AAW89332; AAW89332; NGO_0604. DR GeneID; 3281472; -. DR KEGG; ngo:NGO0604; -. DR PATRIC; 20334284; VBINeiGon24812_0714. DR HOGENOM; HOG000044052; -. DR KO; K02945; -. DR OMA; SRRYPQG; -. DR OrthoDB; EOG6WT8CC; -. DR BioCyc; NGON242231:GI2G-572-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111, KW ECO:0000313|EMBL:AAW89332.1}; KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111, KW ECO:0000313|EMBL:AAW89332.1}; KW RNA-binding {ECO:0000256|PIRNR:PIRNR002111}. FT DOMAIN 22 88 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT DOMAIN 106 172 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT DOMAIN 193 261 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT DOMAIN 278 348 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT DOMAIN 365 435 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT DOMAIN 452 521 S1 motif. {ECO:0000259|PROSITE:PS50126}. SQ SEQUENCE 561 AA; 61190 MW; D532A442F1480EFD CRC64; MSMENFAQLL EESFTLQEMN PGEVITAEVV AIDQNFVTVN AGLKSESLID VAEFKNAQGE IEVKVGDFVT VTIESVENGF GETKLSREKA KRAADWIALE EAMENGNILS GIINGKVKGG LTVMISSIRA FLPGSLVDVR PVKDTSHFEG KEIEFKVIKL DKKRNNVVVS RRAVLEATLG EERKALLENL QEGSVIKGIV KNITDYGAFV DLGGIDGLLH ITDLAWRRVK HPSEVLEVGQ EVEAKVLKFD QEKQRVSLGM KQLGEDPWSG LTRRYPQATR 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 Q5F759_NEIG1 Unreviewed; 279 AA. AC Q5F759; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Cytochrome {ECO:0000313|EMBL:AAW89978.1}; GN ORFNames=NGO_1328 {ECO:0000313|EMBL:AAW89978.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89978.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89978.1; -; Genomic_DNA. DR RefSeq; WP_002216672.1; NC_002946.2. DR RefSeq; YP_208390.1; NC_002946.2. DR ProteinModelPortal; Q5F759; -. DR EnsemblBacteria; AAW89978; AAW89978; NGO_1328. DR GeneID; 3281927; -. DR KEGG; ngo:NGO1328; -. DR PATRIC; 20336023; VBINeiGon24812_1562. DR HOGENOM; HOG000254082; -. DR OMA; VNDRIKP; -. DR OrthoDB; EOG6HMX9R; -. DR BioCyc; NGON242231:GI2G-1241-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F770_NEIG1 Unreviewed; 157 AA. AC Q5F770; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Excinuclease {ECO:0000313|EMBL:AAW89967.1}; GN ORFNames=NGO_1315 {ECO:0000313|EMBL:AAW89967.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89967.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89967.1; -; Genomic_DNA. DR RefSeq; WP_003705875.1; NC_002946.2. DR RefSeq; YP_208379.1; NC_002946.2. DR EnsemblBacteria; AAW89967; AAW89967; NGO_1315. DR GeneID; 3281855; -. DR KEGG; ngo:NGO1315; -. DR PATRIC; 20335989; VBINeiGon24812_1545. DR HOGENOM; HOG000219068; -. DR OMA; SCKVIRG; -. DR OrthoDB; EOG6F81R1; -. DR BioCyc; NGON242231:GI2G-1230-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 157 AA; 15936 MW; C4BE4A5AD3F6F919 CRC64; MLAACQSGRA LKNAHTASAG TPAGESCKVI RGDTAGGGKN IIYRCSNGQA AINAATAAGV LESGIPVSFG GGVPVANGRN LVTRQAANGI GKSDSEACEH ALINAARKFQ QTAGKLGGRS VTGFHSYFGK QSLQGGQYDC QAGSFHVRAV MRANVVR // ID Q5F6C4_NEIG1 Unreviewed; 71 AA. AC Q5F6C4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Putative phage associated protein {ECO:0000313|EMBL:AAW90263.1}; GN ORFNames=NGO_1635 {ECO:0000313|EMBL:AAW90263.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90263.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90263.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90263; AAW90263; NGO_1635. DR PATRIC; 20336806; VBINeiGon24812_1948. DR OrthoDB; EOG69D38Q; -. DR BioCyc; NGON242231:GI2G-1532-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 7456 MW; 551B09E9C0D8DCD5 CRC64; MRLIAADAEK CGMTALQAAE YAIASGWASF RAEWLQNKTF GGSGNRGGPT HNQTAAVLDA GSYGDMPTTD F // ID Q5F6Y2_NEIG1 Unreviewed; 473 AA. AC Q5F6Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 55. DE SubName: Full=Sodium:proton antiporter {ECO:0000313|EMBL:AAW90055.2}; GN ORFNames=NGO_1411 {ECO:0000313|EMBL:AAW90055.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90055.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90055.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90055; AAW90055; NGO_1411. DR PATRIC; 20336229; VBINeiGon24812_1663. DR HOGENOM; HOG000257989; -. DR OMA; GNAPNLM; -. DR OrthoDB; EOG622PQ3; -. DR BioCyc; NGON242231:GI2G-1320-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5005364415. 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; 51681 MW; 56315E427C6751E5 CRC64; MRHLPLFSLM LFPASVYAAD SDGANLNLLW GLPFALILLS IALGPLFFSH TWHHHYGKIT AFWTLLFLIP FSLVFGASAG IHTVAHALVE EYIPFILLLL ALYTISGGIL VWGDLNGTPK LNTALLAVGT ALASIMGTTG AAMLMIRPLL KANQDRTRRV HIVIFFIFLV ANIGGGLTPL GDPPLFLGFL KGVDFMWTVK HMFAPVLIST AVLLTAFYFI DNRFFKQESI AQDTPAQQEK PEKIAIFGKW NFLLLSGVVG AVLMSGLWKP EHPGFEILGS RYALQNLVRD VILITLTAVS MAITPKQVRA GNEFNFEPIA EVGKLFLGIF ITIFPVLSIL KAGEAGALGG VVSLVHDTAG HPINTMYFWM SGILSAFLDN APTYLVFFNM AGGDAQALMT GPLFHSLLAV SMGSVFMGAL TYIGNAPNFM VKAIAEQRGV PMPTFFGYMM WSVAFLTPVF IVHTLVFFVF KLL // ID Q5F9Z3_NEIG1 Unreviewed; 67 AA. AC Q5F9Z3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88994.1}; GN ORFNames=NGO_0241 {ECO:0000313|EMBL:AAW88994.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88994.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88994.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88994; AAW88994; NGO_0241. DR PATRIC; 20333433; VBINeiGon24812_0298. DR HOGENOM; HOG000071236; -. DR OMA; NRANFCK; -. DR OrthoDB; EOG6QVRQ9; -. DR BioCyc; NGON242231:GI2G-225-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 67 AA; 7703 MW; 4A0B2237020AA0BB CRC64; MAIYPKLQNK PPPVMTTGQW VLTMIVFMIP LVNIVMFFVW AFGRGNPNRA NFCKALFLFT LLVRLSV // ID Q5F8W3_NEIG1 Unreviewed; 166 AA. AC Q5F8W3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89374.1}; GN ORFNames=NGO_0647 {ECO:0000313|EMBL:AAW89374.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89374.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89374.1; -; Genomic_DNA. DR RefSeq; WP_010357954.1; NC_002946.2. DR RefSeq; YP_207786.1; NC_002946.2. DR EnsemblBacteria; AAW89374; AAW89374; NGO_0647. DR GeneID; 3281594; -. DR KEGG; ngo:NGO0647; -. DR PATRIC; 20334382; VBINeiGon24812_0763. DR HOGENOM; HOG000219001; -. DR OMA; RDFSPML; -. DR OrthoDB; EOG6KDKQX; -. DR BioCyc; NGON242231:GI2G-614-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 166 AA; 18675 MW; 724E268E1FBF9B89 CRC64; MDAMPQTAVQ NENLHTCSII VDDAQDFSPM LLDAGRDDTL ISESMIPQIR TVAALIAAER HDFSRSSPAE FTDAADFFAA RILVLGVRRF HLDVSLLQIL KTANKRACRF AEKHRLFFTP AQAELSLNKH KNRRLLTIET EHEVENKGNP VANSLAFVRK LHTLPL // ID Q5F6W2_NEIG1 Unreviewed; 325 AA. AC Q5F6W2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90075.1}; GN ORFNames=NGO_1432 {ECO:0000313|EMBL:AAW90075.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90075.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90075.1; -; Genomic_DNA. DR RefSeq; WP_003705777.1; NC_002946.2. DR RefSeq; YP_208487.1; NC_002946.2. DR ProteinModelPortal; Q5F6W2; -. DR EnsemblBacteria; AAW90075; AAW90075; NGO_1432. DR GeneID; 3281737; -. DR KEGG; ngo:NGO1432; -. DR PATRIC; 20336283; VBINeiGon24812_1690. DR HOGENOM; HOG000146188; -. DR KO; K02051; -. DR OMA; VGVHEWK; -. DR OrthoDB; EOG6NPM9G; -. DR BioCyc; NGON242231:GI2G-1340-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR015168; SsuA/THI5. DR InterPro; IPR006311; TAT_signal. DR InterPro; IPR019546; TAT_signal_bac_arc. DR InterPro; IPR027024; UCP027386_ABC_sbc_TM0202. DR Pfam; PF09084; NMT1; 1. DR Pfam; PF10518; TAT_signal; 1. DR PIRSF; PIRSF027386; UCP027386_ABC_sbc_TM0202; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS51318; TAT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 325 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256047. FT DOMAIN 57 160 NMT1. {ECO:0000259|Pfam:PF09084}. SQ SEQUENCE 325 AA; 34980 MW; AEF6F0BDAE57B99E CRC64; MDMKRRDFLK MTAALAAAGV SPSLLAAGKE QFTVYGAPAM PSVTIAVAAL QGKLAKQADV SLKIWRSPDQ LRAGVASGQF KVMMSPSNVG VNLRNQGQKV GMVNILTNGI TQLVCKGSAI ASPQDLVGKK ILVPFKNDMP DIVLQALLKK LKIDAHKVSI TYAATPPEAV GLFPSKGYHA VILPEPMATA SLLKGKTIGI NVVHGFDLVK AWGQAFDTKP LIPMAGIIAN EEYFHAHKAQ FDIFHQDLKN ALNWILANRQ NAAKIGKNYL PAPEPALVMG LDGARLTVSK GSEVKNEILK FYEILMQFNP ELLGGKLPDN GFFLA // ID Q5FA30_NEIG1 Unreviewed; 275 AA. AC Q5FA30; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:AAW88957.1}; GN ORFNames=NGO_0204 {ECO:0000313|EMBL:AAW88957.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88957.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88957.1; -; Genomic_DNA. DR RefSeq; WP_010951011.1; NC_002946.2. DR RefSeq; YP_207369.1; NC_002946.2. DR DNASU; 3281097; -. DR EnsemblBacteria; AAW88957; AAW88957; NGO_0204. DR GeneID; 3281097; -. DR KEGG; ngo:NGO0204; -. DR PATRIC; 20333341; VBINeiGon24812_0253. DR HOGENOM; HOG000261987; -. DR OMA; WRFAGMP; -. DR OrthoDB; EOG6GR36Q; -. DR BioCyc; NGON242231:GI2G-187-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 275 AA; 31290 MW; 2E0BE1F242D8496D CRC64; MNPDIYALPE RALLSGDPDE KGRLTDEAFA AVQNADGAEA NAPPADFPRA GRPDTPVLVA PSQLTPRKMN TAEGYAAMLH AITHIEFNAV NLALDAAYRF RTLPFQFVRD WVKVAKEEVY HFRLVRDRLR AFGFDYGSFE AHNHLWDMAY KTAYDPLLRM ALVPRVLEAR GLDVMPGIRA KVEQRGDSAT CGVLDIIYRD EVGHVAIGNR WYQHLCRERG LEPVALFRSL IARYDMFIFR GYVNIEAREK AGFSRFELDM LEDFEQGLKQ NKHAV // ID Q5F6T9_NEIG1 Unreviewed; 90 AA. AC Q5F6T9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90098.1}; GN ORFNames=NGO_1457 {ECO:0000313|EMBL:AAW90098.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90098.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90098.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90098; AAW90098; NGO_1457. DR BioCyc; NGON242231:GI2G-1363-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 90 AA; 10195 MW; 6B0BF2CB1F722BEF CRC64; MPSETPNRLQ TASVADENSK SAYRHSCENS SSQPSGSRHL YPEIPSFPRK WESRNEKQQE FIGNNRNRTD WIPACAGMTR KSGLWAGLVE // ID Q5FAI5_NEIG1 Unreviewed; 279 AA. AC Q5FAI5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Factor H binding protein {ECO:0000313|EMBL:AAW88802.2}; GN ORFNames=NGO_0033 {ECO:0000313|EMBL:AAW88802.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88802.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88802.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FAI5; -. DR EnsemblBacteria; AAW88802; AAW88802; NGO_0033. DR PATRIC; 20332896; VBINeiGon24812_0033. DR HOGENOM; HOG000218761; -. DR OMA; PLDHKDK; -. DR OrthoDB; EOG69GZJZ; -. DR BioCyc; NGON242231:GI2G-30-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 126 279 Lipoprot_C. {ECO:0000259|Pfam:PF08794}. SQ SEQUENCE 279 AA; 29883 MW; 948BA4F2E9CCB474 CRC64; MNRTTFCCLS LTAGPDSDRL QQRRGGGGGV AADIGTGLAD ALTAPLDHKD KGLKSLTLEA SIPQNGTLTL SAQGAEKTFK AGGKDNSLNT GKLKNDKISR FDFVQKIEVD GQTITLASGE FQIYKQDHSA VVALRIEKIN NPDKIDSLIN QRSFLVSDLG GEHTAFNQLP DGKAEYHGKA FSSDDADGKL TYTIDFAAKQ GHGKIEHLKT PEQNVELASA ELKADEKSHA VILGDTRYGG EEKGTYRLAL FGDRAQEIAG SATVKIGEKV HEIGIADKQ // ID Q5F5D1_NEIG1 Unreviewed; 193 AA. AC Q5F5D1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=RDD family protein {ECO:0000313|EMBL:AAW90606.1}; GN ORFNames=NGO_1998 {ECO:0000313|EMBL:AAW90606.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90606.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90606.1; -; Genomic_DNA. DR RefSeq; WP_003686897.1; NC_002946.2. DR RefSeq; YP_209018.1; NC_002946.2. DR EnsemblBacteria; AAW90606; AAW90606; NGO_1998. DR GeneID; 3282626; -. DR KEGG; ngo:NGO1998; -. DR PATRIC; 20337765; VBINeiGon24812_2409. DR HOGENOM; HOG000218717; -. DR OMA; QNDRRCL; -. DR OrthoDB; EOG6VXFB9; -. DR BioCyc; NGON242231:GI2G-1896-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 21132 MW; 1A4B9B95EC68BB06 CRC64; MEEKNDYTDA VSDNRNGQEI EVGIAGAGDR ILAALLNQLF TFLILLVPFV GLIAFAVKNE GRIGGREEIF GLLLGMTSFW VGLAGILAYT VIQIYYMSRD GQSLGKKIMR IRVLKTDGRN PGFVGTVLVR EIAWSVLVAI IAAVIGLAVG ENGENAINLL AFLANFVLLF MVKRDRRTLY DILADTVVVK LPK // ID Q5F639_NEIG1 Unreviewed; 154 AA. AC Q5F639; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 62. 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 ORFNames=NGO_1727 {ECO:0000313|EMBL:AAW90348.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90348.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90348.1; -; Genomic_DNA. DR RefSeq; WP_003689916.1; NC_002946.2. DR RefSeq; YP_208760.1; NC_002946.2. DR ProteinModelPortal; Q5F639; -. DR SMR; Q5F639; 1-154. DR EnsemblBacteria; AAW90348; AAW90348; NGO_1727. DR GeneID; 3281271; -. DR KEGG; ngo:NGO1727; -. DR PATRIC; 20337050; VBINeiGon24812_2065. DR HOGENOM; HOG000272756; -. DR KO; K03216; -. DR OMA; AGLDYWH; -. DR OrthoDB; EOG6RG038; -. DR BioCyc; NGON242231:GI2G-1623-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01885}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01885, KW ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:AAW90348.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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:AAW90348.1}; 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; 16845 MW; FAF558DC33AA3598 CRC64; MLTIVLYQPE IPPNTGNIIR LCANTGADLH LVKPLGFPLD SAKMKRAGLD YHEFASLTVH ENFDDCLKSL AGRRIFALTT KGTARPDETA FQKGDVLLFG PETRGLPADI LDSLPAAQKI RLPMRPGSRS MNLSNTVSVI LFEAWRQHGY AGGV // ID Q5F744_NEIG1 Unreviewed; 297 AA. AC Q5F744; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 63. DE SubName: Full=Chorismate mutase {ECO:0000313|EMBL:AAW89993.1}; GN ORFNames=NGO_1343 {ECO:0000313|EMBL:AAW89993.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89993.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89993.1; -; Genomic_DNA. DR RefSeq; WP_003691684.1; NC_002946.2. DR RefSeq; YP_208405.1; NC_002946.2. DR ProteinModelPortal; Q5F744; -. DR DNASU; 3282054; -. DR EnsemblBacteria; AAW89993; AAW89993; NGO_1343. DR GeneID; 3282054; -. DR KEGG; ngo:NGO1343; -. DR PATRIC; 20336059; VBINeiGon24812_1579. DR HOGENOM; HOG000027872; -. DR OMA; HEHEFAE; -. DR OrthoDB; EOG690MBS; -. DR BioCyc; NGON242231:GI2G-1257-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00456513}. FT DOMAIN 141 293 DAHP_synth_1. {ECO:0000259|Pfam:PF00793}. SQ SEQUENCE 297 AA; 31884 MW; 328481360206027C CRC64; MIIVMSRRAA EADIAGVVAF IRSRGLREHI SHGDERTVIG AIGDDRVLSV REVQTLPEVE KAVRILDTWK TVSRENRAED SRVAAKGVAF GGGETVRIAA EPSVWSNADA VFLDPFFTSA NLYDTLSADE GRGRCRRLAE QAASAHGAGK PVLVRVRNVR HVEAALNAGA DILYLGGGLM SDLAVLNEAG SLNIPLVLCK DKHHSAEDWL NAAEYVVSRG NRHLILGESG VLGHTKGHPY RLDVESIVKV RQISHLPVIA NITGLWSRDM PQEILYGLAK AAGACGIVGT CFEKAGG // ID Q5F523_NEIG1 Unreviewed; 266 AA. AC Q5F523; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 83. DE SubName: Full=Toluene ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90714.2}; GN ORFNames=NGO_2116 {ECO:0000313|EMBL:AAW90714.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90714.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90714.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F523; -. DR EnsemblBacteria; AAW90714; AAW90714; NGO_2116. DR PATRIC; 20338077; VBINeiGon24812_2561. DR OMA; IRSIVLM; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-2008-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90714.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90714.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 266 AA; 29245 MW; 24CF1585CB4EC919 CRC64; MSPSPFIEMK DVAFAYGDRP ILNDINFSIP QGNFAAVMGG SGSGKTTLMR LITGQIRPQS GQVLIEGRDL AGFSADELYE HRRRMGVLFQ HGALFTDLSV FDNIAFPMRE LTQLPEAVIR DLVLLKLNAV GLRGVENLMP SELSGGMSRR VALARTIALD PEIMLYDEPF TGLDPISLGV IAHLISRVNK ALRSTSIMVT HDIEKSLEIV DQVIFLAHGE IMFSGSPQEM RELDSPWVRQ FVGGLADGPV AYRYPAQTSL QQDLLG // ID Q5F5D8_NEIG1 Unreviewed; 315 AA. AC Q5F5D8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_1991 {ECO:0000313|EMBL:AAW90599.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90599.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90599.1; -; Genomic_DNA. DR RefSeq; WP_010951379.1; NC_002946.2. DR RefSeq; YP_209011.1; NC_002946.2. DR ProteinModelPortal; Q5F5D8; -. DR REBASE; 3568; M.NgoAI. DR EnsemblBacteria; AAW90599; AAW90599; NGO_1991. DR GeneID; 3282633; -. DR KEGG; ngo:NGO1991; -. DR PATRIC; 20337751; VBINeiGon24812_2402. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; SIWHENI; -. DR OrthoDB; EOG600DK3; -. DR BioCyc; NGON242231:GI2G-1889-MONOMER; -. DR Proteomes; UP000000535; 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; 2. 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90599.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90599.1}. FT DOMAIN 2 164 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. FT DOMAIN 226 295 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 315 AA; 35310 MW; D329B2154F680C68 CRC64; MYKTIDLFSG IGGIRLGFEK YGCTNVFSSE WDKYARQVYE ANFGEKPFGD INGIDPSDIP DHDILLAGFP CQPFSIAGKG LGFEDTRGTL FFNIAEILKT KQPKAFLLEN VKRLTTHDSG RTFRIILETL KQLGYTVYFK VLNTLDFGLP QKRERIYIVG FSDNIPFYFP EPINQYRPLG ELLENDRDVE PSYFLSDTLK QKRLAALKKA PPTPSIWHEN IGGNVSALPY SCALRAGGSY NYLVVNGVRR LTGREMLRLQ GFPDDFEINI PYSQVRKVAG NSVSVPVIEA IAENMLASLS GKVEQKGQLD LLEAG // ID Q5F7J2_NEIG1 Unreviewed; 103 AA. AC Q5F7J2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE SubName: Full=ArsR family transcriptional regulator {ECO:0000313|EMBL:AAW89845.1}; GN ORFNames=NGO_1185 {ECO:0000313|EMBL:AAW89845.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89845.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89845.1; -; Genomic_DNA. DR RefSeq; WP_003689616.1; NC_002946.2. DR RefSeq; YP_208257.1; NC_002946.2. DR ProteinModelPortal; Q5F7J2; -. DR EnsemblBacteria; AAW89845; AAW89845; NGO_1185. DR GeneID; 3281880; -. DR KEGG; ngo:NGO1185; -. DR PATRIC; 20335667; VBINeiGon24812_1392. DR HOGENOM; HOG000144508; -. DR OMA; EIANEST; -. DR OrthoDB; EOG690MM0; -. DR BioCyc; NGON242231:GI2G-1097-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000711}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transcription {ECO:0000256|RuleBase:RU000711}; KW Transcription regulation {ECO:0000256|RuleBase:RU000711}. FT DOMAIN 4 99 HTH arsR-type DNA-binding. FT {ECO:0000259|PROSITE:PS50987}. SQ SEQUENCE 103 AA; 11751 MW; 16A9EFACAE3C5D7D CRC64; MPQQTMNLMR ECIPIFTVLS DENRHQILHV LWKHGRMNVN ELTEHLHLSR PAVSHHLKIM LQAGAVAVEQ VGKERFYSIA MADAVARLKQ LADLMAQNCP LSK // ID Q5F8R1_NEIG1 Unreviewed; 533 AA. AC Q5F8R1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=N-6 DNA methylase {ECO:0000313|EMBL:AAW89426.1}; GN ORFNames=NGO_0702 {ECO:0000313|EMBL:AAW89426.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89426.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89426.1; -; Genomic_DNA. DR RefSeq; WP_003688773.1; NC_002946.2. DR RefSeq; YP_207838.1; NC_002946.2. DR ProteinModelPortal; Q5F8R1; -. DR REBASE; 10860; M.NgoAXVII. DR EnsemblBacteria; AAW89426; AAW89426; NGO_0702. DR GeneID; 3281871; -. DR KEGG; ngo:NGO0702; -. DR PATRIC; 20334514; VBINeiGon24812_0829. DR HOGENOM; HOG000249628; -. DR KO; K03427; -. DR OMA; FFAPIFE; -. DR OrthoDB; EOG66TG4Z; -. DR BioCyc; NGON242231:GI2G-666-MONOMER; -. DR Proteomes; UP000000535; 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; -; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89426.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89426.1}. FT DOMAIN 167 485 N6_Mtase. {ECO:0000259|Pfam:PF02384}. SQ SEQUENCE 533 AA; 60023 MW; 298C15FE16322A85 CRC64; MTEQHFTEQI KSLIDSLKTI CANYGLGNDG NEFKIISQAF LYKFLNDKYD FEVKKIRKEK PDEPIEFVNM DIDGKTAVLK PEHSIKYLSE RQNGADFAKL FDDTLTDIAA HNAELFSVKT EGGAKIVLFE RISQYITDEG RRDDFCRALI SKLAGFSFEA IFAQKFDFFA TIFEYLIKDY NSNSGGKYAE YYTPHAVARI MADILVPEDV RGQIRSVDVY DPSAGSGTLL MNVAHAIGED KCMIYTQDIS QKSSNLLRLN LILNNLVHSL NNVVQGNTIL SPAHKDASGC LKKFDFIVSN PPFKLDFSDF RDRLESDENH ERFFAGIPKI KPTKKEKMEI YQLFIQHILF SLKENGKAAI VLPTGFITAK SGIDKKIREY LVENKMLAGV VSMPSNIFAT TGTNVSILFI DKTNKDKVVL IDASGLGEKI KDGKNQKTVL SCEEEQKICN TFTNKQAVED FSVVVGYDEI KAKNHSLSAG QYFEVKIDYV DISADEFAQK IAGFSADLDK LFAESAELEK EIKDRLAMLK FNS // ID Q5F5V6_NEIG1 Unreviewed; 306 AA. AC Q5F5V6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 73. DE SubName: Full=LysR family transcriptional regulator {ECO:0000313|EMBL:AAW90431.1}; GN ORFNames=NGO_1813 {ECO:0000313|EMBL:AAW90431.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90431.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90431.1; -; Genomic_DNA. DR RefSeq; WP_003690049.1; NC_002946.2. DR RefSeq; YP_208843.1; NC_002946.2. DR ProteinModelPortal; Q5F5V6; -. DR EnsemblBacteria; AAW90431; AAW90431; NGO_1813. DR GeneID; 3282273; -. DR KEGG; ngo:NGO1813; -. DR PATRIC; 20337286; VBINeiGon24812_2178. DR HOGENOM; HOG000233514; -. DR KO; K04761; -. DR OMA; CPEFARF; -. DR OrthoDB; EOG6N6848; -. DR BioCyc; NGON242231:GI2G-1711-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 34104 MW; 325BA7C36D03DF4C CRC64; MTLTELRYIV AVAQERHFGR AARRCFVSQP TLSIAIKKLE EELAVSLFDR SSNDIITTEA GERIVAQARK VLKEAELIRH LANEEQNELE GAFKLGLIFT VAPYLLPKLI VSLRRTAPKM PLMLEENYTH TLTESLKRGD VDAIIVAEPF QEPGIVTEPL YDEPFFVIVP KGHSFEELDA VSPRMLGEEQ VLLLTEGNCM RDQVLSSCSE LAAKQRIQGL TNTLQGSSIN TIRHMVASGL AISVLPATAL TENDHMLFSI IPFEGTPPSR RVVLAYRRNF VRPKALSAMK AAIMQSQLHG VSFIHD // ID Q5F5F9_NEIG1 Unreviewed; 69 AA. AC Q5F5F9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90578.1}; GN ORFNames=NGO_1969 {ECO:0000313|EMBL:AAW90578.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90578.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90578.1; -; Genomic_DNA. DR RefSeq; WP_003688150.1; NC_002946.2. DR RefSeq; YP_208990.1; NC_002946.2. DR EnsemblBacteria; AAW90578; AAW90578; NGO_1969. DR GeneID; 3282654; -. DR KEGG; ngo:NGO1969; -. DR PATRIC; 20337703; VBINeiGon24812_2378. DR HOGENOM; HOG000218646; -. DR OrthoDB; EOG60W7ZR; -. DR BioCyc; NGON242231:GI2G-1868-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 69 AA; 8020 MW; 8A1816E71316A131 CRC64; MKLIDFEGNL VKISLDKDEL YIIQAIVGEI YSGVCVDCRD FEIIHGVEKN KVLLLDKELK KIYDTWDKC // ID Q5F7S8_NEIG1 Unreviewed; 1977 AA. AC Q5F7S8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89759.1}; GN ORFNames=NGO_1092 {ECO:0000313|EMBL:AAW89759.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89759.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89759.1; -; Genomic_DNA. DR RefSeq; WP_010951179.1; NC_002946.2. DR RefSeq; YP_208171.1; NC_002946.2. DR EnsemblBacteria; AAW89759; AAW89759; NGO_1092. DR GeneID; 3281125; -. DR KEGG; ngo:NGO1092; -. DR PATRIC; 20335436; VBINeiGon24812_1284. DR HOGENOM; HOG000071257; -. DR OMA; AYHARIE; -. DR OrthoDB; EOG6JQGXN; -. DR BioCyc; NGON242231:GI2G-1004-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 1336 1363 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1977 AA; 211826 MW; 398A5839B57A7ED7 CRC64; MPDGLARQYA DMAAKYRAKP SEAVGIDPDD GAVSAAAALA ADSGAAVPSA VSDDMEARSV ADDAPSGRSA DADRGGVPSA YGNVRPGGAP RGAASVAPGG SAAAASGGIA RVAPLPAGQY FDGLDTRGRK ALAKEAGLDI KGVADFGQIA APVRRKIEQA YHARIEADYQ AASEAKQGYL PPPVRMADAV PVPKKGFSVP ADALDKESRR RFDALPEWVR RHAQTVADYT ADGIMRREAG MADMRGHYPE GLAESAGAVR AYRAQHPESA DVLDRLNRAV YGYRRNNGWS VPLLSREGER LQGVRTALPD DGASEAVVGG GRGLTRALPT EDKGLAQDVR QDVRQGLTQG GRGLTPDAGA DANAAALQGL PGSAVASGNA PARRQNLQVR ARAEGAAPGL SASENLAGTD GGKRAPVAGK RPDTVLPVLN PQVAESAGRV SPKKRMADAA ADFTRRLAAD RRRPEKAGVP LGGGEYRFEH TDRRHIDALA GVPGRPGKGG MPEEFADMAG PSNSDGLVSD GRRYLKGREA ETLRAGGLSE AVPSEPGRDY RPTQEARAPA KVMARPRDAA ADGKPAGRAQ PARAKDTPVA GKAAAAKNAA TEKPSSDKVR NIEAGKSRFD GGKGKSAAAQ GAATEKPSEK TGKAKPETFA KTASDNPEEA RRKARVLQGG PVYTVKERQA PQGFKALREH AESIKKRLAE SIGGLAERVD VAAVSETAPD KAQMLLSQRV EGWFDGRTGK ITLVAENLTP ERAVWAAWHE LGHRGFAADG FAKYREELER ADGNGLIRRI ADAVQEGREG TGDAAASVRP AAVEEAVAEL YAAQRTGGWA GIENRYGVKV GNGLKRGIAG VLARIGALLR RVLQRLAGKA GGAMSDADVF AMLADLHGNV EGARDAPWGG NHRAVMFARA EDGAAERSKS ESLEKLRRAE TIRISGREVP EGGNLREYKR NALEYGKSLR GPYVNKDTGR EISLGRSGIT EILRHDYKDA EHLQSIAAIP QIIENAVYID TLPNEDLAKN GDIQGYEYYV SGLNVGGADY TVRAAVAVSR NGNRYYDHKL TKIEKGNLLS LLDRVSTTGA SESKSPLSGI DDKRLLQILQ DKDAGKGGIA DFDTEAVRFS RAANIEAAIG RITGKKSDLR NALKDRWDAS KGIQLQFLGR RQIEDIYGGV LDGLKEYGRL SELFGADANK AVTEADKVVR EWGRLKEEDA KALADLMHDA TLAKVDADPL MRKDAQKRLD GIRTALDIAD GKIEKAEAAV ASAGARIARA DAAYNKAQRA ADKAAYALEK AQEKHGREIL ADEADMRLRR LFYADSEAKR ALRRAGADVA AESRAKTDAV RMLEQARADV KRLEKDEVGA QKALEGLALL NRRFAGLPDA AQRVYRKARD DYRAHFGQVR DALAERLARA GQDAETVRRL KERFDNELGG VYFPLARFGD YLVVVKDADG NSANVSRAET LSEAEKLRDA LKADFGAGFK VSPVMKSRDY IRSRDAVGSG FMRELGEAVG MLDLDPAQRA RLNDTLTQLY LNSLPDTSWA KHGIHRKGVP GFSDDARRAY AQNMGSGANY LAKLRYADRM AEQLDVMQDF VDGRKYEEGF DQRQLQRVAD EMRKRHEAVM NPNPSKLAQA LTGFGFLWMM GMSPASAVVN LSQTAMVAYP VMAAKWGYAG AARELLRASK QIGLRFGEKF NTIEDSLNGD EKAAFRKAAD YGVIDLSQAH DLAGVANGDP GLAGSAWQKV MDKAAWLFHH AEKFNRQVTF VAAYRLAKRA GADSEAAFEQ AKKATYDGHF DYAAQNRPRF MMGNAAKVVF LFKQYSQNIL YALGRNAYLA FKGDKEARKT LAGLLVSHAM ASGILGLPFV STLLAVASML GSDDDDPWDA EAALRNMLAD AFGDKAGEVL AKGFSRLTPL DVSGRLGLNQ LVFPDIQDGL EGKKWAESLV VGSTGAVVGA GIGAADGVRT RSSVPRTANT LSLMKSW // ID Q5F8H8_NEIG1 Unreviewed; 157 AA. AC Q5F8H8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=Bacterioferritin {ECO:0000256|RuleBase:RU000623}; GN ORFNames=NGO_0795 {ECO:0000313|EMBL:AAW89509.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89509.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU000623}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. CC {ECO:0000256|RuleBase:RU000623}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000256|RuleBase:RU003668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89509.1; -; Genomic_DNA. DR RefSeq; WP_002213535.1; NC_002946.2. DR RefSeq; YP_207921.1; NC_002946.2. DR ProteinModelPortal; Q5F8H8; -. DR SMR; Q5F8H8; 1-152. DR PRIDE; Q5F8H8; -. DR EnsemblBacteria; AAW89509; AAW89509; NGO_0795. DR GeneID; 3282018; -. DR KEGG; ngo:NGO0795; -. DR PATRIC; 20334738; VBINeiGon24812_0941. DR HOGENOM; HOG000262383; -. DR KO; K03594; -. DR OMA; EMKHADQ; -. DR OrthoDB; EOG6WDSKP; -. DR BioCyc; NGON242231:GI2G-749-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Heme {ECO:0000256|RuleBase:RU000623}; KW Iron {ECO:0000256|RuleBase:RU000623}; KW Iron storage {ECO:0000256|RuleBase:RU000623}; KW Metal-binding {ECO:0000256|RuleBase:RU000623}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000259|PROSITE:PS50905}. 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 Q5F7E2_NEIG1 Unreviewed; 575 AA. AC Q5F7E2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591}; DE EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591}; GN ORFNames=NGO_1236 {ECO:0000313|EMBL:AAW89895.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89895.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89895.1; -; Genomic_DNA. DR RefSeq; WP_003692228.1; NC_002946.2. DR RefSeq; YP_208307.1; NC_002946.2. DR ProteinModelPortal; Q5F7E2; -. DR EnsemblBacteria; AAW89895; AAW89895; NGO_1236. DR GeneID; 3282600; -. DR KEGG; ngo:NGO1236; -. DR PATRIC; 20335789; VBINeiGon24812_1453. DR HOGENOM; HOG000258448; -. DR KO; K01652; -. DR OMA; MVWPMVP; -. DR OrthoDB; EOG6KT2NW; -. DR BioCyc; NGON242231:GI2G-1147-MONOMER; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000535; 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:UP000000535}; KW Magnesium {ECO:0000256|RuleBase:RU003591}; KW Metal-binding {ECO:0000256|RuleBase:RU003591}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}; KW Transferase {ECO:0000256|RuleBase:RU003591, KW ECO:0000313|EMBL:AAW89895.1}. 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; 62856 MW; 515871D8F52D838E CRC64; MQLSGAQIIV QSLKAEGVEY VFGYPGGAVI EIYDALFQLN KFKHILTRHE QAAVHAADAY ARVSGKVGVA LVTSGPGVTN ALTGIATAYT DSIPMVVISG QVGNSLIGTD AFQEVDTVGI TRPCVKHNFL VTDINELVET IKKAFQIAAS GRPGPVVLDV PKDVTQAMAK FSYPQEDIFI RSYQPVVQGH IGQIKKAVQM LASAKRPVVY FGGGVVLGNA SEELTRFVRM TGAPCTGTLM GLGAYPSGDR QFLGMLGMHG TYEANLAMQN ADVVLAVGAR FDDRVVSVPS KFFEKAKKVI HIDVDPSSIA KRVKADIPIV GDVKNILSEM VALWQKQESV PSEDALGKWW KTIEEWRSRD CLWFDNGSEI IKPQYVIQKL AEITGNSAII TSDVGQHQMF AAQYYPFERP RQWLNSGGLG TMGVGLPYAI GAKLAAPDQD VFCITGDGSI QMNIQELSTC FQYRIPVNVI TLNNGYLGMV RQWQEIYYGG RESETYFDSL PDFVKLAEAY GHIGIRVDNK SDVEGALLEA LNQKDRLVFI DFLTDQKQNV MPMVGNGKGL DEMVLPPHMR TDGKA // ID Q5F6J4_NEIG1 Unreviewed; 48 AA. AC Q5F6J4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90193.1}; GN ORFNames=NGO_1560 {ECO:0000313|EMBL:AAW90193.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90193.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90193.1; -; Genomic_DNA. DR RefSeq; WP_003693532.1; NC_002946.2. DR RefSeq; YP_208605.1; NC_002946.2. DR EnsemblBacteria; AAW90193; AAW90193; NGO_1560. DR GeneID; 3281446; -. DR KEGG; ngo:NGO1560; -. DR BioCyc; NGON242231:GI2G-1461-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5089 MW; 4DE5E86954528A34 CRC64; MDNVSPFAGK PQIAAGGVQV GPTLQTLPPY RDTPVTSSFK QIFNQNAV // ID Q5F9I9_NEIG1 Unreviewed; 514 AA. AC Q5F9I9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE SubName: Full=Restriction endonuclease, M subunit {ECO:0000313|EMBL:AAW89148.1}; GN ORFNames=NGO_0404 {ECO:0000313|EMBL:AAW89148.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89148.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89148.1; -; Genomic_DNA. DR RefSeq; WP_003687840.1; NC_002946.2. DR RefSeq; YP_207560.1; NC_002946.2. DR ProteinModelPortal; Q5F9I9; -. DR REBASE; 5503; M.NgoAV. DR EnsemblBacteria; AAW89148; AAW89148; NGO_0404. DR GeneID; 3283005; -. DR KEGG; ngo:NGO0404; -. DR PATRIC; 20333817; VBINeiGon24812_0486. DR HOGENOM; HOG000239472; -. DR KO; K03427; -. DR OMA; WASADIL; -. DR OrthoDB; EOG64JFNB; -. DR BioCyc; NGON242231:GI2G-383-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro. 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:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89148.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89148.1}; KW Nuclease {ECO:0000313|EMBL:AAW89148.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 57480 MW; FC08537EBECA8393 CRC64; MMTEMQQRAQ LHRQIWKIAD EVRGAVDGWD FKQYVLGTLF YRFISENFTD YMQAGDSSID YAAMPDSIIT PEIKDDAVKV KGYFIYPGQL FCNIAAEAHQ NEELNTKLKE IFTAIESSAS GYPSEQGIKG LFDDFDTTSS RLGSTVADKN KRLAAVLKGV AELDFGNFED HRIDLFGDAY EYLISNYAAN AGKSGGEFFT PQSVSKLIAR LAVHGQEKVN KIYDPACGSG SLLLQAKKQF DEHIIEEGFF GQEINHTTYN LARMNMFLHN VNYNKFHIEL GDTLTNPKLK DSKPFDAVVS NPPYSIDWIG SDDPTLINDD RFAPAGVLAP KSKADFAFIL HALNYLSGRG RAAIVSFPGI FYRGGAEQKI RQYLVEGNYV ETVIALAPNL FYGTCIAVNI LVLSKHKDNT DIQFIDASGF FKKETNNNVL TEEHIAEIVK LFADKADVPH IAQNAAQQTV KDNGYNLAVS SYVEAEDTRE VIDIRQLNAE ISETVAKIER LRREIDEVIA EIET // ID Q5F7J9_NEIG1 Unreviewed; 48 AA. AC Q5F7J9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89838.1}; GN ORFNames=NGO_1176 {ECO:0000313|EMBL:AAW89838.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89838.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89838.1; -; Genomic_DNA. DR RefSeq; WP_003691757.1; NC_002946.2. DR RefSeq; YP_208250.1; NC_002946.2. DR EnsemblBacteria; AAW89838; AAW89838; NGO_1176. DR GeneID; 3281940; -. DR KEGG; ngo:NGO1176; -. DR PATRIC; 20335635; VBINeiGon24812_1381. DR HOGENOM; HOG000027848; -. DR OrthoDB; EOG615VQW; -. DR BioCyc; NGON242231:GI2G-1085-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5801 MW; 0494F8C1F0197607 CRC64; MSRIYLPLLF PPHIVERGLL YFQQDKVRDV QKISLGRYRA KVFDSENY // ID Q5F8N7_NEIG1 Unreviewed; 94 AA. AC Q5F8N7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89450.1}; GN ORFNames=NGO_0731 {ECO:0000313|EMBL:AAW89450.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89450.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89450.1; -; Genomic_DNA. DR RefSeq; WP_003706224.1; NC_002946.2. DR RefSeq; YP_207862.1; NC_002946.2. DR EnsemblBacteria; AAW89450; AAW89450; NGO_0731. DR GeneID; 3282077; -. DR KEGG; ngo:NGO0731; -. DR PATRIC; 20334604; VBINeiGon24812_0874. DR HOGENOM; HOG000027799; -. DR OMA; HKPRERL; -. DR OrthoDB; EOG63RGV7; -. DR BioCyc; NGON242231:GI2G-690-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10684 MW; 0A34FBDF8AEEBDDD CRC64; MNRAALFNRY PEWIIGQDGA SRFITHCRYP RLIAKIHRQT DGECPGGHYR HSENGITLYD FIFFGGKPAD EARFAAVLTE TCRRAVKKIG SVPD // ID Q5F5S0_NEIG1 Unreviewed; 49 AA. AC Q5F5S0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90467.1}; GN ORFNames=NGO_1846 {ECO:0000313|EMBL:AAW90467.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90467.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90467.1; -; Genomic_DNA. DR RefSeq; WP_003694341.1; NC_002946.2. DR RefSeq; YP_208879.1; NC_002946.2. DR EnsemblBacteria; AAW90467; AAW90467; NGO_1846. DR GeneID; 3282414; -. DR KEGG; ngo:NGO1846; -. DR PATRIC; 20337368; VBINeiGon24812_2219. DR HOGENOM; HOG000218662; -. DR OrthoDB; EOG61047R; -. DR BioCyc; NGON242231:GI2G-1747-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5818 MW; 8F5FAD264B6A9C01 CRC64; MSAALWHKKL SWKGFTPQIN FRYNKNNSNM PAFYSHSGKG WFVSMEKTY // ID Q5F8D7_NEIG1 Unreviewed; 376 AA. AC Q5F8D7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89550.1}; GN ORFNames=NGO_0845 {ECO:0000313|EMBL:AAW89550.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89550.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89550.1; -; Genomic_DNA. DR RefSeq; WP_003688558.1; NC_002946.2. DR RefSeq; YP_207962.1; NC_002946.2. DR ProteinModelPortal; Q5F8D7; -. DR EnsemblBacteria; AAW89550; AAW89550; NGO_0845. DR GeneID; 3282199; -. DR KEGG; ngo:NGO0845; -. DR PATRIC; 20334858; VBINeiGon24812_0999. DR HOGENOM; HOG000262545; -. DR OMA; FAYFEPY; -. DR OrthoDB; EOG6X10TC; -. DR BioCyc; NGON242231:GI2G-792-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 106 356 Peptidase_M14. FT {ECO:0000259|SMART:SM00631}. SQ SEQUENCE 376 AA; 41986 MW; B5E09BA576E380C7 CRC64; MIKISTRFDA GSVVVKDLTD PSNIRLALRP DNASDFAQWF YFRLQGAAYQ NCIMHFENAA EAAYPKGWEG YQACASYDRR NWFRVPTSYE NGVLTVNHTP LSNSVYYAYF EPYSEEQHLN LLGDAQGSGL CRIDDLGSTV QGRDINLLTI GNQVESDMKI WITARQHPGE TMAEWFVEGL LGRLLDSQDP TARTLLDRAT FYIVPNMNPD GSALGNLRTN AAGANLNREW ENPTLEKSPE VFFVRGKMLE TGVDLFLDIH GDEGLPFVFV AGTEGVPNYN PRISALEAQF KTALLNASPD FQDEYGYEKD APGKANMTLA TNWVGNRFNC LAYTLEMPFK DNANLPDDDF GWNGQRSLRL GEAVLSAILN VAGDLR // ID Q5F7Y0_NEIG1 Unreviewed; 174 AA. AC Q5F7Y0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524}; DE Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984}; GN ORFNames=NGO_1031 {ECO:0000313|EMBL:AAW89707.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89707.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00984}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00984}. CC -!- SIMILARITY: Contains 1 SSB domain. {ECO:0000256|HAMAP- CC Rule:MF_00984, ECO:0000256|RuleBase:RU000524}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89707.1; -; Genomic_DNA. DR RefSeq; WP_003695064.1; NC_002946.2. DR RefSeq; YP_208119.1; NC_002946.2. DR ProteinModelPortal; Q5F7Y0; -. DR EnsemblBacteria; AAW89707; AAW89707; NGO_1031. DR GeneID; 3281124; -. DR KEGG; ngo:NGO1031; -. DR PATRIC; 20335282; VBINeiGon24812_1207. DR HOGENOM; HOG000106483; -. DR KO; K03111; -. DR OMA; PYDEGYG; -. DR OrthoDB; EOG6M9F32; -. DR BioCyc; NGON242231:GI2G-952-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00984}; KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_00984}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00984}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00984}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00984, KW ECO:0000256|RuleBase:RU000524, ECO:0000256|SAAS:SAAS00522039, KW ECO:0000313|EMBL:AAW89707.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 107 SSB. {ECO:0000256|HAMAP-Rule:MF_00984}. FT MOTIF 169 174 Important for interaction with partner FT proteins. {ECO:0000256|HAMAP- FT Rule:MF_00984}. SQ SEQUENCE 174 AA; 19449 MW; 9374404D4B3B6F9A CRC64; MSLNKVILIG RLGRDPEVRY MPNGEAVCNF SVATSETWND RNGQRVERTE WHNITMYRKL AEIAGQYLKK GGLVYLEGRI QSRKYQGKDG IERTAYDIVA NEMKMLGGRN ENSGGAPYDE GYGQSQEAYQ RPAQQSRQPA PDAPSHPQEA PAAPRRQPVP AAAPVEDIDD DIPF // ID Q5F500_NEIG1 Unreviewed; 189 AA. AC Q5F500; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 61. DE RecName: Full=Flavin prenyltransferase UbiX {ECO:0000256|HAMAP-Rule:MF_01984}; DE EC=2.5.1.129 {ECO:0000256|HAMAP-Rule:MF_01984}; GN Name=ubiX {ECO:0000256|HAMAP-Rule:MF_01984}; GN ORFNames=NGO_2140 {ECO:0000313|EMBL:AAW90737.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90737.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01984}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl phosphate + FMNH(2) = prenylated CC FMNH(2) + phosphate. {ECO:0000256|HAMAP-Rule:MF_01984}. CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000256|HAMAP- CC Rule:MF_01984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90737.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F500; -. DR EnsemblBacteria; AAW90737; AAW90737; NGO_2140. DR PATRIC; 20338131; VBINeiGon24812_2588. DR HOGENOM; HOG000225437; -. DR OMA; IIMPREM; -. DR OrthoDB; EOG6C8MXR; -. DR BioCyc; NGON242231:GI2G-2031-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01984}; KW FMN {ECO:0000256|HAMAP-Rule:MF_01984}; KW Prenyltransferase {ECO:0000256|HAMAP-Rule:MF_01984}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01984}. FT DOMAIN 4 127 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT NP_BIND 11 13 FMN. {ECO:0000256|HAMAP-Rule:MF_01984}. FT NP_BIND 88 91 FMN. {ECO:0000256|HAMAP-Rule:MF_01984}. FT BINDING 37 37 FMN. {ECO:0000256|HAMAP-Rule:MF_01984}. FT BINDING 123 123 FMN. {ECO:0000256|HAMAP-Rule:MF_01984}. FT BINDING 153 153 DMAP. {ECO:0000256|HAMAP-Rule:MF_01984}. SQ SEQUENCE 189 AA; 20495 MW; B7879421C107037F CRC64; MVRRLIIGIS GASGFQYGVK ALELLRAQDV ETHLVVSKGA EMARASETDY TKDEVYALAD FVHPIGNIGA CIASGTFKTD GMLVAPCSMR TLASVAHGFG DNLLTRAADV VLKERRRLVL MVRETPLNLA HLDNMKRVTE MGGVVFPPVP AMYRKPQTAD DIVAHSIAHT LSLFGIDTPD LAEWQGMAD // ID Q5F838_NEIG1 Unreviewed; 258 AA. AC Q5F838; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Heme biosynthesis protein HemY {ECO:0000313|EMBL:AAW89649.1}; GN ORFNames=NGO_0960 {ECO:0000313|EMBL:AAW89649.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89649.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89649.1; -; Genomic_DNA. DR RefSeq; WP_003696991.1; NC_002946.2. DR RefSeq; YP_208061.1; NC_002946.2. DR ProteinModelPortal; Q5F838; -. DR EnsemblBacteria; AAW89649; AAW89649; NGO_0960. DR GeneID; 3282611; -. DR KEGG; ngo:NGO0960; -. DR PATRIC; 20335108; VBINeiGon24812_1123. DR HOGENOM; HOG000263839; -. DR OMA; DMDDICV; -. DR OrthoDB; EOG628F8J; -. DR BioCyc; NGON242231:GI2G-891-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 22 256 ThiF. {ECO:0000259|Pfam:PF00899}. SQ SEQUENCE 258 AA; 27744 MW; 2B19A06C16FC3DB5 CRC64; MSDNALTSSR RFGGIARLYG DSALTHFSQA HVCVVGVGGV GSWAVEALAR TGIGRLTLID LDNVAESNAN RQLHALTGDF GKAKVTALRE RITQINPQCE VFEIEDFVTE DNLPEYFGKG FDFVIDAIDQ VRVKAAMAAY FVERKQPFVL SGGAGGQKNP ALIQTADLSR VTHDPLLANL RYTLRKRYGF SRDTKEKMRV PCVYSTENIM PPQSGAACSA DAAPQGLSCA GYGASMLVTA SFGLYCAQAA VEHIAGKK // ID Q5FA64_NEIG1 Unreviewed; 71 AA. AC Q5FA64; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88923.1}; GN ORFNames=NGO_0167 {ECO:0000313|EMBL:AAW88923.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88923.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88923.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88923; AAW88923; NGO_0167. DR BioCyc; NGON242231:GI2G-153-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 8437 MW; DDE8260E4B20CF4A CRC64; MLMKFHVICL NNIFNDIFNT DCFFLINICL LLYCTREGRL KTSYLIFRRP FAFSNSNQSN GFIASSRWSR L // ID Q5F9J8_NEIG1 Unreviewed; 459 AA. AC Q5F9J8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Multidrug transporter {ECO:0000313|EMBL:AAW89139.1}; GN ORFNames=NGO_0395 {ECO:0000313|EMBL:AAW89139.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89139.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:5C6P} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 5-459. RX PubMed=26246409; DOI=10.1038/ncomms8995; RA Radchenko M., Symersky J., Nie R., Lu M.; RT "Structural basis for the blockade of MATE multidrug efflux pumps."; RL Nat. Commun. 6:7995-7995(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; AE004969; AAW89139.1; -; Genomic_DNA. DR RefSeq; WP_003687823.1; NC_002946.2. DR RefSeq; YP_207551.1; NC_002946.2. DR PDB; 5C6P; X-ray; 3.00 A; A=5-459. DR PDBsum; 5C6P; -. DR EnsemblBacteria; AAW89139; AAW89139; NGO_0395. DR GeneID; 3283014; -. DR KEGG; ngo:NGO0395; -. DR PATRIC; 20333797; VBINeiGon24812_0476. DR HOGENOM; HOG000038538; -. DR KO; K03327; -. DR OMA; IILNHIG; -. DR OrthoDB; EOG6423C5; -. DR BioCyc; NGON242231:GI2G-374-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015297; F:antiporter activity; IEA:InterPro. DR GO; GO:0015238; F:drug transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5C6P}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 190 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 221 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 310 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 322 345 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 357 376 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 397 417 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 423 445 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 459 AA; 49811 MW; 0B0AC1EDC75DA7FB CRC64; MLLDLDRFSF SVFLKEIRLL TALALPMLLA QVAQVGIGFV DTVMAGGAGK EDLAAVALGS SAFATVYITF MGIMAALNPM IAQLYGAGKT GEAGETGRQG IWFGLILGIF GMILMWAAIT PFRNWLTLSD YVEGTMAQYM LFTSLAMPAA MVHRALHAYA SSLNRPRLIM LVSFAAFVLN VPLNYIFVYG KFGMPALGGA GCGVATMAVF WFSALALWIY IAKEKFFRPF GLTAKFGKPD WAVFKQIWKI GAPIGLSYFL EASAFSFIVF LIAPFGEDYV AAQQVGISLS GILYMIPQSV GSAGTVRIGF SLGRREFSRA RYISGVSLVS GWVLAVITVL SLVLFRSPLA SMYNDDPAVL SIASTVLLFA GLFQPADFTQ CIASYALRGY KVTKVPMFIH AAAFWGCGLL PGYLLAYRFD MGIYGFWTAL IASLTIAAVA LVWCLEKYSM ELVKSHKAV // ID Q5F762_NEIG1 Unreviewed; 102 AA. AC Q5F762; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89975.2}; GN ORFNames=NGO_1324 {ECO:0000313|EMBL:AAW89975.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89975.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89975.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89975; AAW89975; NGO_1324. DR PATRIC; 20336015; VBINeiGon24812_1558. DR HOGENOM; HOG000219071; -. DR OMA; YRRASLM; -. DR OrthoDB; EOG6SV5CZ; -. DR BioCyc; NGON242231:GI2G-1238-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 39 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 72 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 102 AA; 11037 MW; 0EFF9CD3D0E29000 CRC64; MEYCEPEEAS DPYATYRRAN LMAGLPLFVV ILVLLNVVFP LPAHPLAWLV PAGFMVLGGG FPLSLPLVAL LVPTCCILAR CPPLSRLLCH PCPNHPMSKN SA // ID Q5F9C7_NEIG1 Unreviewed; 110 AA. AC Q5F9C7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 42. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89210.2}; GN ORFNames=NGO_0472 {ECO:0000313|EMBL:AAW89210.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89210.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89210.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89210; AAW89210; NGO_0472. DR PATRIC; 20333982; VBINeiGon24812_0563. DR HOGENOM; HOG000137689; -. DR BioCyc; NGON242231:GI2G-450-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 12657 MW; 4DD138CFB0EA743B CRC64; MKYYGTAAYG SPDWGMERYY AREDMRQALD GWEAENRILH ESALIGIAKK SAREFVRDAD GEPYSQEDWE TYLTEDASRV GKDTEAAMNY AIDEREWFAL AENIGRLANS // ID Q5F9Y4_NEIG1 Unreviewed; 203 AA. AC Q5F9Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Clp protease ClpB {ECO:0000313|EMBL:AAW89003.1}; GN ORFNames=NGO_0250 {ECO:0000313|EMBL:AAW89003.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89003.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89003.1; -; Genomic_DNA. DR RefSeq; WP_003692687.1; NC_002946.2. DR RefSeq; YP_207415.1; NC_002946.2. DR DNASU; 3281541; -. DR EnsemblBacteria; AAW89003; AAW89003; NGO_0250. DR GeneID; 3281541; -. DR KEGG; ngo:NGO0250; -. DR PATRIC; 20333455; VBINeiGon24812_0308. DR HOGENOM; HOG000218836; -. DR OMA; FCARSSI; -. DR OrthoDB; EOG66F08M; -. DR BioCyc; NGON242231:GI2G-235-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR014861; Uncharacterised_CNP1. DR Pfam; PF08750; CNP1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89003.1}; KW Protease {ECO:0000313|EMBL:AAW89003.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256089. FT DOMAIN 40 188 CNP1. {ECO:0000259|Pfam:PF08750}. SQ SEQUENCE 203 AA; 22551 MW; 757CB6FF38CCFBFE CRC64; MRRAILLILT LTVGTSLAAG FSQKDTPINT RYRETPEEAA AREFKEHTAE LPPLPDAHSD GWFDIYVDEN YGKQPKILLD SLQIMPAPDG SIRYILNIRS DKGYDNLTAE GIFCARSSIG FGNGKLSSYK VFGYGDTVNS RWIQPRNAEW KPIGGTLGRN DALRAVLYQA FCEGGVPADT QGLVQRLKER AGRYAPSMKP HDK // ID Q5F9A0_NEIG1 Unreviewed; 120 AA. AC Q5F9A0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89237.1}; GN ORFNames=NGO_0499 {ECO:0000313|EMBL:AAW89237.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89237.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89237.1; -; Genomic_DNA. DR RefSeq; WP_003689082.1; NC_002946.2. DR RefSeq; YP_207649.1; NC_002946.2. DR EnsemblBacteria; AAW89237; AAW89237; NGO_0499. DR GeneID; 3282950; -. DR KEGG; ngo:NGO0499; -. DR PATRIC; 20334040; VBINeiGon24812_0592. DR OMA; GDFEMTV; -. DR OrthoDB; EOG6CZQWT; -. DR BioCyc; NGON242231:GI2G-477-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 120 AA; 12573 MW; F91F7DA3C549DA37 CRC64; MPSENQTAFS FGDFEMTVKL KAPEGFTDVS FGSQSYAADE NGIVEVPSEA AEFLYQFGFG NVASEPAEGP EKAKRGRKPK TGQPAGQSEP AEAAEPAEAE AEAAEPAEAE AEPAEAEKAE // ID Q5FAJ8_NEIG1 Unreviewed; 116 AA. AC Q5FAJ8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Preprotein translocase subunit SecG {ECO:0000313|EMBL:AAW88785.1}; GN ORFNames=NGO_0016 {ECO:0000313|EMBL:AAW88785.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88785.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88785.1; -; Genomic_DNA. DR RefSeq; WP_003687220.1; NC_002946.2. DR RefSeq; YP_207197.1; NC_002946.2. DR EnsemblBacteria; AAW88785; AAW88785; NGO_0016. DR GeneID; 3283060; -. DR KEGG; ngo:NGO0016; -. DR PATRIC; 20332862; VBINeiGon24812_0016. DR HOGENOM; HOG000071344; -. DR KO; K03075; -. DR OMA; NFMSRAT; -. DR OrthoDB; EOG6CCHB4; -. DR BioCyc; NGON242231:GI2G-13-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 12193 MW; 9F1A41CFB09BA252 CRC64; MEAFKTLIWI INIISALAVI VLVLLQHGKG ADAGATFGSG SGSAQGVFGS AGNANFLSRS TAVAATFFFA TCMAMVYIHT HTTKHGLDFS NIRQTQQAPK PVSNTEPSAP VPQQQK // ID Q5F9J7_NEIG1 Unreviewed; 62 AA. AC Q5F9J7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89140.1}; GN ORFNames=NGO_0396 {ECO:0000313|EMBL:AAW89140.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89140.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89140.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89140; AAW89140; NGO_0396. DR HOGENOM; HOG000137694; -. DR OMA; RNNGAHY; -. DR OrthoDB; EOG6W9XJ8; -. DR BioCyc; NGON242231:GI2G-375-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 6996 MW; 3BFA8D23C19D23A4 CRC64; MRNNGAHYIV KNTVPSDGGY GVYKVYSDCV YFMVKFGFND LTALSRRTGA VRILNRKEAS PF // ID Q5F7M2_NEIG1 Unreviewed; 68 AA. AC Q5F7M2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89815.1}; GN ORFNames=NGO_1148 {ECO:0000313|EMBL:AAW89815.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89815.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89815.1; -; Genomic_DNA. DR RefSeq; WP_003689742.1; NC_002946.2. DR RefSeq; YP_208227.1; NC_002946.2. DR EnsemblBacteria; AAW89815; AAW89815; NGO_1148. DR GeneID; 3282313; -. DR KEGG; ngo:NGO1148; -. DR PATRIC; 20335556; VBINeiGon24812_1343. DR HOGENOM; HOG000219957; -. DR OMA; EMAFTRW; -. DR OrthoDB; EOG6V7BT6; -. DR BioCyc; NGON242231:GI2G-1061-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021249; DUF2788. DR Pfam; PF10981; DUF2788; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 56 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 68 AA; 7519 MW; 0F724AF76FCA2616 CRC64; MDEAVFADWA LKICLTGLII FLGFIVWNLG KESKAGKFGI AVLFLVLGLG VFGFVFKELL IKFLVLPK // ID Q5F8L1_NEIG1 Unreviewed; 102 AA. AC Q5F8L1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89476.1}; GN ORFNames=NGO_0761 {ECO:0000313|EMBL:AAW89476.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89476.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89476.1; -; Genomic_DNA. DR RefSeq; WP_010951118.1; NC_002946.2. DR RefSeq; YP_207888.1; NC_002946.2. DR EnsemblBacteria; AAW89476; AAW89476; NGO_0761. DR GeneID; 3282482; -. DR KEGG; ngo:NGO0761; -. DR PATRIC; 20334670; VBINeiGon24812_0907. DR HOGENOM; HOG000218966; -. DR OMA; LKHISEF; -. DR OrthoDB; EOG6130DH; -. DR BioCyc; NGON242231:GI2G-716-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 102 AA; 11739 MW; F074E06CB4E59ADC CRC64; MTLKTDLLPK INNEDYQRLI LKHSAEFSGG ETRLLNEILE KFNFDVVQAQ ALAQAVMQQV RFDPNAYHID SDDEDTTGIC PHCINPPMPP LHDYLVWRET RG // ID Q5F698_NEIG1 Unreviewed; 58 AA. AC Q5F698; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90289.1}; GN ORFNames=NGO_1664 {ECO:0000313|EMBL:AAW90289.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90289.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90289.1; -; Genomic_DNA. DR RefSeq; WP_003689797.1; NC_002946.2. DR RefSeq; YP_208701.1; NC_002946.2. DR EnsemblBacteria; AAW90289; AAW90289; NGO_1664. DR GeneID; 3281302; -. DR KEGG; ngo:NGO1664; -. DR PATRIC; 20336878; VBINeiGon24812_1984. DR HOGENOM; HOG000071331; -. DR OrthoDB; EOG6QZMWN; -. DR BioCyc; NGON242231:GI2G-1558-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 58 AA; 6581 MW; 36F30C161F58A517 CRC64; MFGRHTEYAI ADNFTKYTAP FHLKNNGLDT ASTEKPAAHL SKPCLQAYLY NLQIQTVH // ID Q5F8S8_NEIG1 Unreviewed; 241 AA. AC Q5F8S8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89409.1}; GN ORFNames=NGO_0682 {ECO:0000313|EMBL:AAW89409.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89409.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89409.1; -; Genomic_DNA. DR RefSeq; WP_010951106.1; NC_002946.2. DR RefSeq; YP_207821.1; NC_002946.2. DR EnsemblBacteria; AAW89409; AAW89409; NGO_0682. DR GeneID; 3281925; -. DR KEGG; ngo:NGO0682; -. DR PATRIC; 20334462; VBINeiGon24812_0803. DR HOGENOM; HOG000011197; -. DR KO; K09765; -. DR OMA; PNIHPYT; -. DR OrthoDB; EOG6S26FS; -. DR BioCyc; NGON242231:GI2G-649-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003828; DUF208. DR Pfam; PF02677; DUF208; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 241 AA; 27813 MW; 33CF56D59ACE8354 CRC64; METQNKPTVT DIDRPILVPP GGHKKVLLHS CCAPCSGEVM EAMLASGIGY TIYFYNPNIH PHKEYMLRKE ENMRFAEKFG IPFIDKDDDY ENDRKEWFAK AKGMEFEPER GIRCTMCFDM RFEKAAQYAH EHGFPVFTSS LGISRWKNMA QINDCGHRAA APYDDVAYWD FNWRKGGGGA RMIEISKREN FYQQEYCGCA YSLRDSNAHR KSQGRIPVKL GVLYYGDEST QYEPAPVRVD K // ID Q5F638_NEIG1 Unreviewed; 228 AA. AC Q5F638; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 60. DE SubName: Full=RlpA {ECO:0000313|EMBL:AAW90349.1}; GN ORFNames=NGO_1728 {ECO:0000313|EMBL:AAW90349.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90349.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the rlpA family. CC {ECO:0000256|RuleBase:RU003495}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90349.1; -; Genomic_DNA. DR RefSeq; WP_003696139.1; NC_002946.2. DR RefSeq; YP_208761.1; NC_002946.2. DR ProteinModelPortal; Q5F638; -. DR EnsemblBacteria; AAW90349; AAW90349; NGO_1728. DR GeneID; 3281107; -. DR KEGG; ngo:NGO1728; -. DR PATRIC; 20337054; VBINeiGon24812_2067. DR HOGENOM; HOG000254768; -. DR KO; K03642; -. DR OMA; QARGMIQ; -. DR OrthoDB; EOG6X3W9K; -. DR BioCyc; NGON242231:GI2G-1624-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256040. FT DOMAIN 149 228 SPOR. {ECO:0000259|PROSITE:PS51724}. SQ SEQUENCE 228 AA; 24694 MW; 39A12BA346DBE38A CRC64; MTLTRKTLFL LTAAFGTHSL QTASADAVVK PEKLHASANR SYKVAEFTQT GNASWYGGRF HGRKTSGGDR YDMNAFTAAH KTLPIPSHVR VTNTKNGKSV IVRVNDRGPF HGNRIIDVSK AAAQKLGFVS QGTAHVKIEQ IVPGQSAPVA ENKDIFIDLK SFGTEHEAQA YLNQAAQNFA ASSSSPNLSV EKRRYEYVVK MGPFASQERA AEAEAQARGM VRAVLTSG // ID Q5F7J3_NEIG1 Unreviewed; 372 AA. AC Q5F7J3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AAW89844.1}; GN ORFNames=NGO_1184 {ECO:0000313|EMBL:AAW89844.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89844.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89844.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F7J3; -. DR DNASU; 3281952; -. DR EnsemblBacteria; AAW89844; AAW89844; NGO_1184. DR PATRIC; 20335665; VBINeiGon24812_1391. DR HOGENOM; HOG000116236; -. DR OMA; WARIGRS; -. DR OrthoDB; EOG6T7N7Q; -. DR BioCyc; NGON242231:GI2G-1096-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001155; OxRdtase_FMN_N. DR Pfam; PF00724; Oxidored_FMN; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 11 312 Oxidored_FMN. {ECO:0000259|Pfam:PF00724}. SQ SEQUENCE 372 AA; 40599 MW; 830B1FBE55E28A92 CRC64; MEEQLAQNDQ PSEKLVRLYG AWAEGGAGVL VTGNVMVAES GKGSINDVLI SDDRALEMLK KWAKARTQND TLLIMQINHA GKQSPAVVNK TPLAPSAVPL VGMNGFINPP RELSADEING LIQQFVQTAK IAEQAGFSGV QIYAVHGYLI SQFLSPHHNR RQDQWGGSLE NRMRFLLETY TAIRAAAGKD FLVGVKLNSA DFQKGGFDES ESVQVVQKLS EMGIDFIEVS GGNYESPQML AAKDSTRKRE AFFIDYAEKA RAASQAPLII TGGFRSQTAM EDALSSGHLD LVGIARPFAL VPDLANKMQN RTYQTVQADR IQTGVAFVDK KAGAMLEMNW YMTQMDLIGQ GKQSNPKIVG VESIAENFAG KR // ID Q5F745_NEIG1 Unreviewed; 284 AA. AC Q5F745; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Dihydropteroate synthase {ECO:0000256|RuleBase:RU361205}; DE Short=DHPS {ECO:0000256|RuleBase:RU361205}; DE EC=2.5.1.15 {ECO:0000256|RuleBase:RU361205}; DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205}; GN ORFNames=NGO_1342 {ECO:0000313|EMBL:AAW89992.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89992.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|RuleBase:RU361205}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361205}; 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 {ECO:0000256|RuleBase:RU361205}. CC -!- SIMILARITY: Belongs to the DHPS family. CC {ECO:0000256|RuleBase:RU361205}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000256|RuleBase:RU361205}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89992.1; -; Genomic_DNA. DR RefSeq; WP_003693788.1; NC_002946.2. DR RefSeq; YP_208404.1; NC_002946.2. DR ProteinModelPortal; Q5F745; -. DR EnsemblBacteria; AAW89992; AAW89992; NGO_1342. DR GeneID; 3282050; -. DR KEGG; ngo:NGO1342; -. DR PATRIC; 20336057; VBINeiGon24812_1578. DR HOGENOM; HOG000217510; -. DR KO; K00796; -. DR OMA; SIDTYHA; -. DR OrthoDB; EOG67T5P5; -. DR BioCyc; NGON242231:GI2G-1256-MONOMER; -. DR UniPathway; UPA00077; UER00156. DR Proteomes; UP000000535; 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; PS00793; DHPS_2; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Folate biosynthesis {ECO:0000256|RuleBase:RU361205}; KW Magnesium {ECO:0000256|RuleBase:RU361205}; KW Metal-binding {ECO:0000256|RuleBase:RU361205}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU361205}. FT DOMAIN 18 275 Pterin-binding. FT {ECO:0000259|PROSITE:PS50972}. SQ SEQUENCE 284 AA; 30380 MW; 1A666DCA6BA73AFC CRC64; MARHVWRAGR FEIGLDKPKI MGIVNLTPDS FSDGGAYSQN AQTALAHAER LLKEGADILD IGGESTRPGA DFVPPEEEEW ARVEPVLAEA AGWGVPVSLD TRRTVVMEKA LALGGIDIIN DVAALTDEGA VELLARQADT GICLMHMRGL PETMQDNPKY QDVVGEVARY LKTRSETCVA AGIAPQRITL DPGFGFGKNL QHNIALMRHL PELMAETGLP LLIGVSRKRM IGELTGEADA AARVHGSVAA ALASVARGAQ IVRVHDVKAT ADALKVWEAL GVNR // ID Q5F5H3_NEIG1 Unreviewed; 86 AA. AC Q5F5H3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90564.1}; GN ORFNames=NGO_1953 {ECO:0000313|EMBL:AAW90564.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90564.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90564.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90564; AAW90564; NGO_1953. DR HOGENOM; HOG000071372; -. DR OMA; ASTEYKN; -. DR OrthoDB; EOG6F29GX; -. DR BioCyc; NGON242231:GI2G-1854-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 9809 MW; 4414012FB62239E3 CRC64; MRRYRLNPSD GIFPHNETKP FPPDRTGFPP PTGRQPADCH LNTRLIPSVC KGNSRLFPLG RKPVLLSKRH FVRLIRAAST EYKNTA // ID Q5F910_NEIG1 Unreviewed; 103 AA. AC Q5F910; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 81. DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|RuleBase:RU004013}; DE EC=2.7.4.6 {ECO:0000256|RuleBase:RU004013}; GN ORFNames=NGO_0597 {ECO:0000313|EMBL:AAW89327.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89327.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. {ECO:0000256|RuleBase:RU004013}. CC -!- SIMILARITY: Belongs to the NDK family. CC {ECO:0000256|RuleBase:RU004011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89327.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F910; -. DR SMR; Q5F910; 1-100. DR EnsemblBacteria; AAW89327; AAW89327; NGO_0597. DR PATRIC; 20334270; VBINeiGon24812_0707. DR HOGENOM; HOG000224565; -. DR OMA; LTQMTQT; -. DR OrthoDB; EOG67DPRV; -. DR BioCyc; NGON242231:GI2G-567-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro. 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 {ECO:0000256|RuleBase:RU004013}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:AAW89327.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004013}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU004013, KW ECO:0000313|EMBL:AAW89327.1}. SQ SEQUENCE 103 AA; 11285 MW; 1560DB56400C128E CRC64; MKQLTLKEAQ EFYAVHKDRP FYAGLVEFMT GGPVMIQVLE GENAVLKNRE LMGATNPTEA AEGTIRADFA TSVSINAVHG SDSVENAALE IAYFFSQTEI CPR // ID Q5F8R5_NEIG1 Unreviewed; 77 AA. AC Q5F8R5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89422.1}; GN ORFNames=NGO_0698 {ECO:0000313|EMBL:AAW89422.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89422.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89422.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89422; AAW89422; NGO_0698. DR PATRIC; 20334508; VBINeiGon24812_0826. DR HOGENOM; HOG000229957; -. DR OMA; MHNNDII; -. DR OrthoDB; EOG6QVRJM; -. DR BioCyc; NGON242231:GI2G-662-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 77 AA; 8911 MW; AA2D316C7F6424C6 CRC64; MHNNDIIIYT TEDGLSEFTL RELDGELWLT QKEIAELYQT SKQNIGKHIK AIFAEQELDD SVVNFQFTTA ADGKNYR // ID Q5F6R1_NEIG1 Unreviewed; 94 AA. AC Q5F6R1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 47. DE SubName: Full=Peptidase propeptide and YPEB domain protein {ECO:0000313|EMBL:AAW90126.1}; GN ORFNames=NGO_1488 {ECO:0000313|EMBL:AAW90126.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90126.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90126.1; -; Genomic_DNA. DR RefSeq; WP_003689372.1; NC_002946.2. DR RefSeq; YP_208538.1; NC_002946.2. DR EnsemblBacteria; AAW90126; AAW90126; NGO_1488. DR GeneID; 3281602; -. DR KEGG; ngo:NGO1488; -. DR PATRIC; 20336427; VBINeiGon24812_1761. DR HOGENOM; HOG000219089; -. DR OMA; AERQIYS; -. DR OrthoDB; EOG6B8XN5; -. DR BioCyc; NGON242231:GI2G-1392-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025711; PepSY. DR Pfam; PF13670; PepSY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256594. FT DOMAIN 4 90 PepSY. {ECO:0000259|Pfam:PF13670}. SQ SEQUENCE 94 AA; 10785 MW; A157A81F78C8D8AC CRC64; MKKLLLAAVV SLNAATAFAG DSAERQIYGD PHFEQNRTKA VKMLEQRGYQ VYDVDADDYW GKPVLEVEAY KDGREYDIVL SYPDLKIIKE QLDR // ID Q5F8Z1_NEIG1 Unreviewed; 146 AA. AC Q5F8Z1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89346.1}; GN ORFNames=NGO_0618 {ECO:0000313|EMBL:AAW89346.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89346.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89346.1; -; Genomic_DNA. DR RefSeq; WP_003688914.1; NC_002946.2. DR RefSeq; YP_207758.1; NC_002946.2. DR EnsemblBacteria; AAW89346; AAW89346; NGO_0618. DR GeneID; 3282901; -. DR KEGG; ngo:NGO0618; -. DR PATRIC; 20334320; VBINeiGon24812_0732. DR HOGENOM; HOG000258661; -. DR OMA; FHAEAWI; -. DR OrthoDB; EOG6MD96X; -. DR BioCyc; NGON242231:GI2G-586-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 15801 MW; F961A89FBDE101D0 CRC64; MMQTFRKISL YAATLWLGMQ IMAGYIAAPV LFKMLPKMQA GEIAGVLFDI LSWSGLAVWG TVLAAAFAAL TRRQTALLLF LLSALAANQF LVTPVIEALK YGHENWLLSV AGGSFGMWHG ISSMTFMATA LLSAVLSWRL SGKEAV // ID Q5FA72_NEIG1 Unreviewed; 867 AA. AC Q5FA72; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:AAW88915.1}; GN Name=pepN {ECO:0000313|EMBL:AAW88915.1}; GN ORFNames=NGO_0158 {ECO:0000313|EMBL:AAW88915.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88915.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88915.1; -; Genomic_DNA. DR RefSeq; WP_003694813.1; NC_002946.2. DR RefSeq; YP_207327.1; NC_002946.2. DR ProteinModelPortal; Q5FA72; -. DR SMR; Q5FA72; 4-866. DR EnsemblBacteria; AAW88915; AAW88915; NGO_0158. DR GeneID; 3281350; -. DR KEGG; ngo:NGO0158; -. DR PATRIC; 20333239; VBINeiGon24812_0202. DR HOGENOM; HOG000257670; -. DR KO; K01256; -. DR OMA; FKRWYSQ; -. DR OrthoDB; EOG693GJ0; -. DR BioCyc; NGON242231:GI2G-145-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Aminopeptidase {ECO:0000313|EMBL:AAW88915.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW88915.1}; KW Protease {ECO:0000313|EMBL:AAW88915.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 86 380 Peptidase_M1. {ECO:0000259|Pfam:PF01433}. FT DOMAIN 454 824 DUF3458. {ECO:0000259|Pfam:PF11940}. SQ SEQUENCE 867 AA; 97516 MW; 40ECD3E5282166A5 CRC64; MSKTVRYLKD YQTPAYRILE TELHFDIAEP QTVVKSRLTV EPQRAGEPLV LDGSAKLLSV KINGAAADYV LEGETLTIAD VPSERFTVEV ETEILPAENK SLMGLYASGG NLFTQCEPEG FRKITFYIDR PDVMSKFTTT IVADKKRYPV LLSNGNKIDG GEFSDGRHWV KWEDPFAKPS YLFALVAGDL AVTEDRFTTM SGRNVKIEFY TTEADKPKVG FAVESLKNAM KWDETRFGLE YDLDIFMVVA VGDFNMGAME NKGLNIFNTK FVLADSRTAT DTDFEGIESV VGHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFSGDR AGRAVRRIEN IRLLRQNQFP EDAGPTAHPV RPVSYEEMNN FYTMTVYEKG AEVVRMYHTL LGEEGFQKGM KLYFQRHDGQ AVTCDDFRAA MADANGINLD QFALWYSQAG TPVLEAEGRL KNNVFELTIK QTVPPTPDMA DKQPMMIPVK VGLLNRNGEA VAFDYQGKRA TEAVLLMTEA EQAFPLEGVT EAVVPSLLRG FSAPVYLNYP YSDDDLLLLL AHDSDAFTCW EAAQTLYRRA VAANLAALSD GIGLPKHEKL LAAVEKVISD DLLDNAFKAL LLGVPSEAEL WDGTENIDPL RYHQAREALL DTLAVRFLPK WHELDRQAAK QENQSYEYSP ETADWRTLRN VCRAFVLRAD PAHIETVAEK YGEMAQNMTH EWGILSAVNG NESDTRNCLL AQFADKFSDD ALVMDKYFAL IGSSRRSDTL QQVQTALQHP KFSLENPNKA RSLIGSFSRN VPHFHAQDGS GYRFIADKVI EIDRFNPQVA ARLVQAFNLC NKLEPHRKNL VKQELQCIRA QEGLSKDVGE IVGKILG // ID Q5F9N8_NEIG1 Unreviewed; 215 AA. AC Q5F9N8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89099.2}; GN ORFNames=NGO_0355 {ECO:0000313|EMBL:AAW89099.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89099.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89099.2; -; Genomic_DNA. DR RefSeq; WP_003687766.1; NC_002946.2. DR RefSeq; YP_207511.2; NC_002946.2. DR DNASU; 3283036; -. DR EnsemblBacteria; AAW89099; AAW89099; NGO_0355. DR GeneID; 3283036; -. DR KEGG; ngo:NGO0355; -. DR HOGENOM; HOG000071241; -. DR OMA; MMNEVEL; -. DR OrthoDB; EOG676Z4R; -. DR BioCyc; NGON242231:GI2G-334-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:InterPro. DR InterPro; IPR003220; InsA_N_dom. DR Pfam; PF03811; Zn_Tnp_IS1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 47 74 Zn_Tnp_IS1. {ECO:0000259|Pfam:PF03811}. SQ SEQUENCE 215 AA; 24532 MW; 40F20A566929775E CRC64; MSGVTKELDI LKQLFENLSD TDKQAFLTSV SSKEQVKKVI EPRKVTKCPH CQSTHFVKNG KDCGNQRFLC RDCKKSFVEQ TGTILYNTQK DIEVWEKYIH CMIEKYPLRK CAEICKINLA TAFTWRHKIL DALQNMMNEV ELDGIVQADE TYSTISYKGH HKNFNLPRPA HKRGTRATKR GISKEQVCVP CGINLDGKSV ARISNLGKPS LKNIN // ID Q5F6W7_NEIG1 Unreviewed; 228 AA. AC Q5F6W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 63. DE SubName: Full=Repressor {ECO:0000313|EMBL:AAW90070.2}; GN ORFNames=NGO_1427 {ECO:0000313|EMBL:AAW90070.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90070.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90070.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6W7; -. DR EnsemblBacteria; AAW90070; AAW90070; NGO_1427. DR PATRIC; 20336273; VBINeiGon24812_1685. DR HOGENOM; HOG000008672; -. DR OMA; VGHEEPV; -. DR OrthoDB; EOG6TBHDR; -. DR BioCyc; NGON242231:GI2G-1335-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 142 207 Peptidase_S24. FT {ECO:0000259|Pfam:PF00717}. SQ SEQUENCE 228 AA; 25712 MW; E1F29B83460A7582 CRC64; METFKDRLVF LWKSEARQAK IASDIEMTIA GFSRIWNEGG LPKSETLKKI KQLKGCSIDW LLTGEGNPFP DEAPKKSLAY DTLGNEVDTD EFVFVPRYDI RAAAGYGQFV GHEEPVFTMA FRRHWIENYV TRDTKNLSVI SVKGDSMEGV LNDGDSILVN HGENTPRDGL YVLRINENLL VKRLQIVPGG IINVISANEA YPAFEINLND LTDDVEIIGR VEWFGRTV // ID Q5F8E5_NEIG1 Unreviewed; 239 AA. AC Q5F8E5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 71. DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:AAW89542.1}; GN ORFNames=NGO_0832 {ECO:0000313|EMBL:AAW89542.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89542.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89542.1; -; Genomic_DNA. DR RefSeq; WP_003688574.1; NC_002946.2. DR RefSeq; YP_207954.1; NC_002946.2. DR ProteinModelPortal; Q5F8E5; -. DR EnsemblBacteria; AAW89542; AAW89542; NGO_0832. DR GeneID; 3282339; -. DR KEGG; ngo:NGO0832; -. DR PATRIC; 20334822; VBINeiGon24812_0981. DR OMA; QAGRIIF; -. DR OrthoDB; EOG6N3CR8; -. DR BioCyc; NGON242231:GI2G-784-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 239 AA; 25980 MW; DE7D31BB911AB78F CRC64; MPTLTDKTIL VTGASQGLGE QVAKAYAAEG ATVILVARHQ KKLEKAYDAI VEAGHPEPFA IRFDLMSAEE KEFERFAATI AEATQGKLDG IVHCAGYFYA LSPLDFQTVA EWVNQYRINT VAPMGLTRAL FPLLKQSPDA SVIFVGESHG ETPKAYWGGF GASKAALNYL CKVAADEWER FGNLRANVLV PGPINSPQRI KSHPGEAGSE RKSYGDVLPA FVWWASAESK GRSGEIVYL // ID Q5F8M2_NEIG1 Unreviewed; 161 AA. AC Q5F8M2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 73. 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 ORFNames=NGO_0748 {ECO:0000313|EMBL:AAW89465.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89465.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89465.1; -; Genomic_DNA. DR RefSeq; WP_003688684.1; NC_002946.2. DR RefSeq; YP_207877.1; NC_002946.2. DR ProteinModelPortal; Q5F8M2; -. DR SMR; Q5F8M2; 4-153. DR EnsemblBacteria; AAW89465; AAW89465; NGO_0748. DR GeneID; 3282594; -. DR KEGG; ngo:NGO0748; -. DR PATRIC; 20334636; VBINeiGon24812_0890. DR HOGENOM; HOG000034140; -. DR KO; K01588; -. DR OMA; SDWATMR; -. DR OrthoDB; EOG6Z0QH2; -. DR BioCyc; NGON242231:GI2G-705-MONOMER; -. DR UniPathway; UPA00074; UER00943. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-HAMAP. 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:UP000000535}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01929}; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01929}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 17182 MW; 8D63C137D9B82B35 CRC64; MIQIGIIMGS NSDWPVMRQA AQFLEEFGVE YEARVVSAHR TPDLMFEYAE TARARGIKAI IAGAGGAAHL PGMVAAKTTV PVLGVPVPSK YLRGEDSLLS IVQMPKGVPV ATFAIGEAGA ANAALFAISM LANENPELAQ KLADFRAKQE QTVLNMELEQ I // ID Q5F5L3_NEIG1 Unreviewed; 716 AA. AC Q5F5L3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 62. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90524.1}; GN ORFNames=NGO_1910 {ECO:0000313|EMBL:AAW90524.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90524.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90524.1; -; Genomic_DNA. DR RefSeq; WP_010951369.1; NC_002946.2. DR RefSeq; YP_208936.1; NC_002946.2. DR EnsemblBacteria; AAW90524; AAW90524; NGO_1910. DR GeneID; 3282136; -. DR KEGG; ngo:NGO1910; -. DR PATRIC; 20337542; VBINeiGon24812_2298. DR HOGENOM; HOG000279479; -. DR OMA; HYNEWAD; -. DR OrthoDB; EOG6MSS1Z; -. DR BioCyc; NGON242231:GI2G-1813-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256190. FT TRANSMEM 86 105 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 136 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 391 420 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 432 452 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; 79870 MW; 177791A4D6696322 CRC64; MKTPLLKPLL ITSLPVFASV FTAASIVWQL GEPKLAMPFV LGIIAGGLVD LDNRLTGRLK NIIATVALFT LSSLTAQSTL GTGLPFILAM TLMTFGFTIL GAVGLKYRTF AFGALAVATY TTLTYTPETY WLTNPFMILC GTVLYSTAII LFQIILPHRP VQESVANAYE ALGGYLEAKA DFFDPDEAAW IGNRHIDLAM SNTGVITAFN QCRSALFYRL RGKHRHPRTA KMLRYYFAAQ DIHERISSAH VDYQEMSEKF KNTDIIFRIR RLLEMQGQAC RNTAQAIRSG KDYVYSKRLG RAIEGCRQSL RLLSDGNDSP DIRHLSRLLD NLGSVDQQFR QLRHSDSPAE NDRMGDTRIA ALETGSFKNT WQAIRPQLNL ESCVFRHAVR LSLVVAAACT IVEALNLNLG YWILLTALFV CQPNYTATKS RVYQRIAGTV LGVIVGSLVP YFTPSVETKL WIVIAGTTLF FMTRTYKYSF STFFITIQAL TSLSLAGLDV YAAMPVRIID TIIGASLAWA AVSYLWPDWK YLTLERTAAL AVCSSGTYLQ KIAERLKTGE TGDDIEYRIT RRRAHEHTAA LSSTLSDMSS EPAKFADSLQ PGFTLLKTGY ALTGYISALG AYRSEMHEEC SPDFTAQFHL AAEHTAHIFQ HLPDMGPDDF QTALDTLRGE LGTLRTRSSG TQSHILLQQL QLIARQLEPY YRAYRQIPHR QPQNAA // ID Q5F684_NEIG1 Unreviewed; 394 AA. AC Q5F684; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE SubName: Full=Ubiquinone biosynthesis protein UbiH {ECO:0000313|EMBL:AAW90303.1}; GN ORFNames=NGO_1678 {ECO:0000313|EMBL:AAW90303.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90303.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90303.1; -; Genomic_DNA. DR RefSeq; WP_010951321.1; NC_002946.2. DR RefSeq; YP_208715.1; NC_002946.2. DR ProteinModelPortal; Q5F684; -. DR DNASU; 3281223; -. DR EnsemblBacteria; AAW90303; AAW90303; NGO_1678. DR GeneID; 3281223; -. DR KEGG; ngo:NGO1678; -. DR PATRIC; 20336912; VBINeiGon24812_2000. DR HOGENOM; HOG000255771; -. DR OMA; NKHMLHA; -. DR OrthoDB; EOG6G20HJ; -. DR BioCyc; NGON242231:GI2G-1573-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Ubiquinone {ECO:0000313|EMBL:AAW90303.1}. FT DOMAIN 6 346 FAD_binding_3. FT {ECO:0000259|Pfam:PF01494}. SQ SEQUENCE 394 AA; 43603 MW; 715F6D35B780E694 CRC64; MSLHSDILVV GAGPAGLSFA AELAGSGLKV TLIERSPLTV LQNPPYDGRE IALTHFSREI MQRLGMWDKI PENEIYPLRD AKVLNGRSDY QLHFPQPTEA RGEPADCLGY LISNHNIRRA AYEVVSQLDN VSILTDTAVK EVKTSDNEAQ VFLENGDILT ARLLLAADSR FSQTRRQLGI SSDMHDYSRT MFVCRMKHTL SNQHTAYECF HYGRTIALLP LEKRLTNTVI TVDTDKINSV QNLSPEELAA SVKEQLKGRL GDMELVSSIH HYPLVGMIAK RFYGKRSALI GDAAVGMHPV TAHGFNLGLS SADILAKLIL EAEQRGQDIG AASLLEKYSS KHMLHAHPLY HGTNMMLKLF TNETAPAKLL RGLVLRAGNN FPPLKKLITK QLTG // ID Q5F7F0_NEIG1 Unreviewed; 371 AA. AC Q5F7F0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Permease {ECO:0000313|EMBL:AAW89887.1}; GN ORFNames=NGO_1228 {ECO:0000313|EMBL:AAW89887.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89887.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89887.1; -; Genomic_DNA. DR RefSeq; WP_003697970.1; NC_002946.2. DR RefSeq; YP_208299.1; NC_002946.2. DR EnsemblBacteria; AAW89887; AAW89887; NGO_1228. DR GeneID; 3281847; -. DR KEGG; ngo:NGO1228; -. DR PATRIC; 20335771; VBINeiGon24812_1444. DR HOGENOM; HOG000263579; -. DR KO; K07091; -. DR OMA; LAWWPIH; -. DR OrthoDB; EOG6TR0CJ; -. DR BioCyc; NGON242231:GI2G-1139-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 41842 MW; CBDFB00E3C65FFD1 CRC64; MIYQRNLIKE LSFTAVGIFV VLLAVLVSTQ AINLLGRAAD GRVAIDAVLA LVGFWVIGMT PLLLVLTAFI STLTVLTRYW RDSEMSVWLS CGLALKQWIR PVMQFAVPFA ILIAVMQLWV IPWAELRSRE YAEILKQKQE LSLVEAGEFN NLGKRNGRVY FVETFDTESG IMKNLFLREQ DKNGGDNIIF AKEGNFSLND NKRTLELRHG YRYSGTPGRA DYNQVSFQKL NLIISTTPKL IDPVSHRRTI STAQLIGSSN PQHQAELMWR ISLTVSVLLL CLLAVPLSYF NPRSGHTYNI LIAIGLFLIY QNGLTLLFEA VEDGKIHFWL GLLPMHIIMF VIAIVLLRVR SMPSQPFWQA VGKSLTLKGG K // ID Q5F7A1_NEIG1 Unreviewed; 112 AA. AC Q5F7A1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89936.2}; GN ORFNames=NGO_1282 {ECO:0000313|EMBL:AAW89936.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89936.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89936.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89936; AAW89936; NGO_1282. DR PATRIC; 20335905; VBINeiGon24812_1507. DR HOGENOM; HOG000027865; -. DR OMA; CFAPLPY; -. DR OrthoDB; EOG6QCDCC; -. DR BioCyc; NGON242231:GI2G-1194-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 112 AA; 12374 MW; 09320FC7CC564CAE CRC64; MIFKCRPNVF QTASAVSAFS GGVLEVVRLC CRRLSVLFNP GVMLFVPDCP VGGAAGFFQY EMLCPLFRQG RLQTGSNFAY DVFMSAGRLN GGRKPPRRLL VFLPCFAPLP YN // ID Q5F8P7_NEIG1 Unreviewed; 67 AA. AC Q5F8P7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89440.1}; GN ORFNames=NGO_0720 {ECO:0000313|EMBL:AAW89440.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89440.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89440.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89440; AAW89440; NGO_0720. DR PATRIC; 20334570; VBINeiGon24812_0857. DR OrthoDB; EOG63JRJJ; -. DR BioCyc; NGON242231:GI2G-680-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7698 MW; 74DB4BB69612CD80 CRC64; MPSERRPFQT AFLSNRKTVG KFAGRVQSRY GGLHKFKHIC SAAMYFKCRS VCGNTQQTVR VWTAKEI // ID Q5F9R3_NEIG1 Unreviewed; 146 AA. AC Q5F9R3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 65. DE SubName: Full=Thiol peroxidase {ECO:0000313|EMBL:AAW89074.2}; GN ORFNames=NGO_0328 {ECO:0000313|EMBL:AAW89074.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89074.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89074.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9R3; -. DR EnsemblBacteria; AAW89074; AAW89074; NGO_0328. DR PATRIC; 20333647; VBINeiGon24812_0401. DR HOGENOM; HOG000022344; -. DR OMA; QPVPDFE; -. DR OrthoDB; EOG6ZH2P1; -. DR BioCyc; NGON242231:GI2G-309-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89074.2}; KW Peroxidase {ECO:0000313|EMBL:AAW89074.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 146 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 146 AA; 16573 MW; E860B779C9A82330 CRC64; MDMKYEFTLP SSSGADFHSA EHLPLVVYFY PKDSTPGCTT EGLDFNARLE QFEALGYTVV GISRDGVKAH QNFCAKQGFR FELLSDKDET VCRLFDVIKL KKLYGKESLG IERSTFVLNK DGEIVREWRK VKVAGHAQEV LETLSR // ID Q5F768_NEIG1 Unreviewed; 209 AA. AC Q5F768; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 55. DE SubName: Full=Heme transporter CcmA {ECO:0000313|EMBL:AAW89969.2}; GN ORFNames=NGO_1318 {ECO:0000313|EMBL:AAW89969.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89969.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89969.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F768; -. DR SMR; Q5F768; 8-206. DR EnsemblBacteria; AAW89969; AAW89969; NGO_1318. DR PATRIC; 20335999; VBINeiGon24812_1550. DR HOGENOM; HOG000219069; -. DR OMA; NQITHEP; -. DR OrthoDB; EOG6R2GZQ; -. DR BioCyc; NGON242231:GI2G-1232-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 209 AA; 23610 MW; 97B3432133A6AE26 CRC64; MSETENQALT FAKRLKADTT AVHDSVDNLV MSVQPFVSKE NYIKFLKLQS VFHKAVDHIY KDPELNKAIS ELEYMARYDA VTQDLKDLGE EPYKFDKELP HETGNKAVGW LYCAEGSNLG AAFLFKHAQK LDYTGEHGAR HLAPHPDGRG KHWRAFVEHL NALNLTPEAE AEAIQGAQEA FAFYKVILRE TFGLPEGTEA PEGMMPHRH // ID Q5F8A9_NEIG1 Unreviewed; 67 AA. AC Q5F8A9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89578.1}; GN ORFNames=NGO_0878 {ECO:0000313|EMBL:AAW89578.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89578.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89578.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89578; AAW89578; NGO_0878. DR PATRIC; 20334931; VBINeiGon24812_1035. DR BioCyc; NGON242231:GI2G-820-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7523 MW; 3EBF4116FFE4368C CRC64; MTIMPSEPPF RRHFTHQNRK PHPKSSSQDT TANRIQNPTP PPKCRLKPSA QPSLSGARLI KGAHNFP // ID Q5FAK8_NEIG1 Unreviewed; 671 AA. AC Q5FAK8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Prolyl endopeptidase {ECO:0000313|EMBL:AAW88795.1}; GN ORFNames=NGO_0026 {ECO:0000313|EMBL:AAW88795.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88795.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88795.1; -; Genomic_DNA. DR RefSeq; WP_003694697.1; NC_002946.2. DR RefSeq; YP_207207.1; NC_002946.2. DR ProteinModelPortal; Q5FAK8; -. DR ESTHER; neime-NMB1877; S9N_PPCE_Peptidase_S9. DR EnsemblBacteria; AAW88795; AAW88795; NGO_0026. DR GeneID; 3283068; -. DR KEGG; ngo:NGO0026; -. DR PATRIC; 20332882; VBINeiGon24812_0026. DR HOGENOM; HOG000238966; -. DR KO; K01322; -. DR OMA; YGPAWHQ; -. DR OrthoDB; EOG6VB6QV; -. DR BioCyc; NGON242231:GI2G-23-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 74558 MW; 8959725973F5F9F7 CRC64; MKSYPDPYRH FENLDSAETQ NFAAEANAET RARFLNNDKA RALSDGILNQ MQDTRQIPFC QEHRARMYHF HQNAEYPKGV YRMCTAATYR SGYPEWKILF SVADFDELLG DDVYLGGVSH LVEQPNRALL TLNKSGGDTA YTLEVDLEAG ELVEGGFHFP AGKNHVSWRD ENSVWVCPAW DERQLTESGY PREVWLVERG KSFEESLPAY QIDKGAMMVN AWRYLDPQGS PIDLIEASDG FYTKTYLQVS SEGGAKPLNL PNDCDVVGYL AGHLLLTLRK DWHRANQSYP SGALVAVKLN RGELGAAQLL FAPDETQALE SVETTKRFVV ASLLENVQGR LKAWRFADSK WQEAELPHLP SGALEMTDQP WGGDVVYLAA SDFTTPLTLF ALDLNVMELT VMRLQPQQFV SDGIEVRQFW AVSSDGERIP YFHVGKNAAP DTPTLVYAYG GFGIPELPHY LGSVGKYWLE EGNAFVLANI RGGGEFGPRW HQAAQGISKH KSVDDLLAVV RDLSERGMSS PKHIGLQGGS NGGLITAAAF VREPQSIGAL VCEVPLTDMI RYPLLSAGSS WTDEYGNPQK YEACKRRLGE LSPYHNLSDG IDYPPALITT SLSDDRVHPA HALKFYAKLR ETSPQSWLYS PDGGGHTGNG TQRESADKLA CVLLFLKEFL G // ID Q5F598_NEIG1 Unreviewed; 267 AA. AC Q5F598; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Cytochrome C {ECO:0000313|EMBL:AAW90639.2}; GN ORFNames=NGO_2031 {ECO:0000313|EMBL:AAW90639.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90639.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90639.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F598; -. DR EnsemblBacteria; AAW90639; AAW90639; NGO_2031. DR PATRIC; 20337845; VBINeiGon24812_2446. DR HOGENOM; HOG000255217; -. DR OMA; ACDQLTI; -. DR OrthoDB; EOG6C5RMW; -. DR BioCyc; NGON242231:GI2G-1932-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 29 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364406. FT TRANSMEM 239 258 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 46 138 Cytochrome c. FT {ECO:0000259|PROSITE:PS51007}. SQ SEQUENCE 267 AA; 30499 MW; 62346A7D9B4FA748 CRC64; MRAVEMKQAM KNWFAALLSA VPMSAAFASG GHAHYEKVDI DLRDQVSLQR GAQIFTNYCL SCHSASGMRF NRLKDIGLTD EEIKKNLMFT TDNVGDVMHS AMNPKDAAKW FGAAPPDLTL IARSKGADYL YAYMRGFYKD PTRPSGWNNT VFDKVGMPHP LWEQQGVQAV ELDAKGQPVM VKDEHGEMKP KLYWESTGLH SRRLPNGKVI QKEYDAYVRD LVNYLVYMGE PAQLQRKRIG YVVMIFLFAV MLPLAYFLKK EYWKDVH // ID Q5F8H9_NEIG1 Unreviewed; 154 AA. AC Q5F8H9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 74. DE RecName: Full=Bacterioferritin {ECO:0000256|RuleBase:RU000623}; GN ORFNames=NGO_0794 {ECO:0000313|EMBL:AAW89508.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89508.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Iron-storage protein. {ECO:0000256|RuleBase:RU000623}. CC -!- SIMILARITY: Belongs to the bacterioferritin family. CC {ECO:0000256|RuleBase:RU000623}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000256|RuleBase:RU003668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89508.1; -; Genomic_DNA. DR RefSeq; WP_003688620.1; NC_002946.2. DR RefSeq; YP_207920.1; NC_002946.2. DR ProteinModelPortal; Q5F8H9; -. DR PRIDE; Q5F8H9; -. DR EnsemblBacteria; AAW89508; AAW89508; NGO_0794. DR GeneID; 3281962; -. DR KEGG; ngo:NGO0794; -. DR PATRIC; 20334736; VBINeiGon24812_0940. DR HOGENOM; HOG000262383; -. DR KO; K03594; -. DR OMA; HEMQDET; -. DR OrthoDB; EOG6WDSKP; -. DR BioCyc; NGON242231:GI2G-748-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Heme {ECO:0000256|RuleBase:RU000623}; KW Iron {ECO:0000256|RuleBase:RU000623}; KW Iron storage {ECO:0000256|RuleBase:RU000623}; KW Metal-binding {ECO:0000256|RuleBase:RU000623}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 145 Ferritin-like diiron. FT {ECO:0000259|PROSITE:PS50905}. SQ SEQUENCE 154 AA; 17977 MW; 0B0C8CEEC245D46A CRC64; MQGNQAVVDY MNELLSGELA ARDQYFIHSR LYSEWGYTKL FERLNHEMEE ETTHAEDFIR RILMLGGTPK MARSELNIGT DVVSCLKADL QTEYEVRDAL KKGIKLCEEA QDYVTRDLMV AQLKDTEEDH AHWLEQQLRL IELIGEGNYY QSQL // ID Q5F943_NEIG1 Unreviewed; 516 AA. AC Q5F943; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89294.1}; GN ORFNames=NGO_0561 {ECO:0000313|EMBL:AAW89294.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89294.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89294.1; -; Genomic_DNA. DR RefSeq; WP_003688997.1; NC_002946.2. DR RefSeq; YP_207706.1; NC_002946.2. DR EnsemblBacteria; AAW89294; AAW89294; NGO_0561. DR GeneID; 3282165; -. DR KEGG; ngo:NGO0561; -. DR PATRIC; 20334184; VBINeiGon24812_0664. DR HOGENOM; HOG000218994; -. DR OMA; PAFDYEE; -. DR OrthoDB; EOG6P8TJH; -. DR BioCyc; NGON242231:GI2G-534-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010352; DUF945. DR Pfam; PF06097; DUF945; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 516 AA; 57091 MW; EF7BB1301A637513 CRC64; MKKPLISVAA VLLGVALGTP YYLGVKAEES LTQQQKILQK TGFLTVESHQ YDRGWFTSTE TTVIRLKPEL LHNAQKYLPD NLKIVLEQPV TLVNHITHGP FAGGFGTQAH IETEFKYAPE TEKVLERFFG KQVPVSLANT VYFNGSGKME VSVPAFDYEE LSGIRLHWEG LTGETVYQKG FKSYRNSYDA PLFKIKLADK GDAAFEKAHF DSETSDGINP LALGSSNLTL EKFSLEWKEG VDYNVKLNEL VNLVTDLQIG AFINPNGSIA PSKIEVGKLA FSTKTGESGA FIDSEGRFRF DTLVYGDEKY GPLDIHIAAE HLDASALTVL KRKFAQISAK KMTEEQIRND LIAAVKGDAS GLFTHDPVLN IKIFRFTLPQ GKIDVGGKIM FKGMKKEDLN QLGLMLKKTE ANIRMSIPQK MLEDLAVSQA GNIFSVNAED EAEARASIAD INETLRLMVD STVQSMAREK YLTLDGNQID TVISLKNNAL KLNGKTLQNE PDPDFDEGDM VSGQPH // ID Q5F6U9_NEIG1 Unreviewed; 161 AA. AC Q5F6U9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Autotransporter adhesin {ECO:0000313|EMBL:AAW90088.1}; GN ORFNames=NGO_1446 {ECO:0000313|EMBL:AAW90088.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90088.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90088.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F6U9; -. DR EnsemblBacteria; AAW90088; AAW90088; NGO_1446. DR PATRIC; 20336311; VBINeiGon24812_1704. DR HOGENOM; HOG000071350; -. DR OMA; MGAVFKP; -. DR OrthoDB; EOG63C0VB; -. DR BioCyc; NGON242231:GI2G-1353-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 20 98 YadA_anchor. {ECO:0000259|Pfam:PF03895}. FT COILED 117 161 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 161 AA; 17439 MW; C2AA30A7CB536D28 CRC64; MSPMARKIYD AVNVRQLNRL SKRTNRVGAS AAALASLKPA QLGKNDKFAF SLGFGSYKNA QAVAMGAVFK PAENVLLNVA GSFAGPDRAF GAGVFWKFGG KPTPAVAAQN AAHPAKVLQL RQEVAALRAR QAETDRKLHK QAEMENELQQ LRRALSELKK H // ID Q5F969_NEIG1 Unreviewed; 517 AA. AC Q5F969; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Long-chain fatty acid--CoA ligase {ECO:0000313|EMBL:AAW89268.1}; GN ORFNames=NGO_0530 {ECO:0000313|EMBL:AAW89268.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89268.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89268.1; -; Genomic_DNA. DR RefSeq; WP_003691393.1; NC_002946.2. DR RefSeq; YP_207680.1; NC_002946.2. DR ProteinModelPortal; Q5F969; -. DR EnsemblBacteria; AAW89268; AAW89268; NGO_0530. DR GeneID; 3282918; -. DR KEGG; ngo:NGO0530; -. DR PATRIC; 20334106; VBINeiGon24812_0625. DR HOGENOM; HOG000229983; -. DR KO; K01897; -. DR OMA; KKEMIIV; -. DR OrthoDB; EOG6MH5BV; -. DR BioCyc; NGON242231:GI2G-508-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW89268.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 57453 MW; 405FC9150C7C307D CRC64; MNRTYANFYE MLAAACRKNG NGTAVFDGKE KTAYRALKQE AEAVAAYLQN IGVKFGDTVA LAVSNSTEFI TAYFAVSAIG AVAVPMNTFL KNSEYAYILN DCKARFLFAS AGLSKELAGL KAQTPVEKII WTDKSRPAGE TAEGDAFFEN VRRFPEKPDL GRQPRINDLA HIIYTSGTTG HPKGALISYA NLFANLNGIE RIFKISKRDR FIVFLPMFHS FTLTAMVLLP IYMACSIILV KSVFPFSNVL KQALLKRATV FLGVPAIYTA MSKAKIPWYF RWFNRIRLFI SGGAPLAEQT ILDFKAKFPR AKLLEGYGLS EASPVVAVNT PERQKARSVG IPLPGLEAKA VDEELVEVPR GEVGELIVRG GSVMRGYLNM PAATDETIVN GWLKTGDFVT IDEDGFIFIV DRKKDLIISK GQNVYPREIE EEIHKLDAVE AAAVIGVKDR YADEEIVAFV QLKEGMDLGE DEIRRHLRTV LANFKIPKQI HFKDGLPRNA TGKVLKRVLK EQFEGNK // ID Q5FAL3_NEIG1 Unreviewed; 725 AA. AC Q5FAL3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAW88790.1}; GN ORFNames=NGO_0021 {ECO:0000313|EMBL:AAW88790.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88790.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88790.1; -; Genomic_DNA. DR RefSeq; WP_010950972.1; NC_002946.2. DR RefSeq; YP_207202.1; NC_002946.2. DR ProteinModelPortal; Q5FAL3; -. DR EnsemblBacteria; AAW88790; AAW88790; NGO_0021. DR GeneID; 3283064; -. DR KEGG; ngo:NGO0021; -. DR PATRIC; 20332872; VBINeiGon24812_0021. DR HOGENOM; HOG000218756; -. DR KO; K16088; -. DR OMA; GETHTDP; -. DR OrthoDB; EOG67DPGD; -. DR BioCyc; NGON242231:GI2G-18-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Receptor {ECO:0000313|EMBL:AAW88790.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256099. FT DOMAIN 68 165 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 480 723 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 725 AA; 80288 MW; C7DE53AD679821CB CRC64; MTRFKYSLLF AALLPVYAQA DVSVSDDPKP QESTELPTIT VTADRTASSN DGYTVSGTHT PFGLPMTLRE IPQSVSVITS QQMRDQNIKT LDRALLQATG TSRQIYGSDR AGYNYLFARG SRIANYQING IPVADALADT GNANTAAYER VEVVRGVAGL PDGTGEPSAT VNLVRKHPTR KPLFEVRAEA GNRKHFGLGA DVSGSLNAEG TLRGRLVSTF GRGDSWRQLE RSRDAELYGI LEYDIAPQTR VHAGMDYQQA KETADAPLSY AVYDSQGYAT AFGPKDNPAT NWSNSRNRAL NLFAGIEHRF NQDWKLKAEY DYTRSRFRQP YGVAGVLSID HSTAATDLIP GYWHADPRTH SASMSLTGKY RLFGREHDLI AGINGYKYAS NKYGERSIIP NAIPNAYEFS RTGAYPQPSS FAQTIPQYDT RRQIGGYLAT RFRAADNLSL ILGGRYSRYR AGSYNSRTQG MTYVSANRFT PYTGIVFDLT GNLSLYGSYS SLFVPQLQKD EHGSYLKPVT GNNLEADIKG EWLEGRLNAS AAVYRARKNN LATAAGRDQS GNTYYRAANQ AKTHGWEIEV GGRITPEWQI QAGYSQSKPR DQDGSRLNPD SVPERSFKLF TAYHLAPEAP SGRTIGAGVR RQGETHTDPA ALRIPNPAAK ARAVANSRQK AYAVADIMAR YRFNPRTELS LNVDNLFNKH YRTQPDRHSY GALRTVNAAF TYRFK // ID Q5F7M5_NEIG1 Unreviewed; 103 AA. AC Q5F7M5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89812.1}; GN ORFNames=NGO_1145 {ECO:0000313|EMBL:AAW89812.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89812.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89812.1; -; Genomic_DNA. DR RefSeq; WP_003689737.1; NC_002946.2. DR RefSeq; YP_208224.1; NC_002946.2. DR EnsemblBacteria; AAW89812; AAW89812; NGO_1145. DR GeneID; 3282134; -. DR KEGG; ngo:NGO1145; -. DR PATRIC; 20335550; VBINeiGon24812_1340. DR HOGENOM; HOG000218819; -. DR OrthoDB; EOG6JDWGV; -. DR BioCyc; NGON242231:GI2G-1058-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 103 AA; 10980 MW; 3B886F4C63D43E3C CRC64; MFETSQVTTY TATLLGAKKF KGEIDGNKID SCTVLVASPM PSNGNAVGFT SESMKFGDSH NFEKLKNLKF PCAVDLTVAM ESTGKGLVQK LLDFQVKGAA PKA // ID Q5F9V4_NEIG1 Unreviewed; 139 AA. AC Q5F9V4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89033.1}; GN ORFNames=NGO_0284 {ECO:0000313|EMBL:AAW89033.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89033.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89033.1; -; Genomic_DNA. DR RefSeq; WP_002217668.1; NC_002946.2. DR RefSeq; YP_207445.1; NC_002946.2. DR EnsemblBacteria; AAW89033; AAW89033; NGO_0284. DR GeneID; 3281629; -. DR KEGG; ngo:NGO0284; -. DR PATRIC; 20333543; VBINeiGon24812_0352. DR HOGENOM; HOG000218848; -. DR OrthoDB; EOG6QG8KT; -. DR BioCyc; NGON242231:GI2G-265-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F7K5_NEIG1 Unreviewed; 98 AA. AC Q5F7K5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89806.1}; GN ORFNames=NGO_1139 {ECO:0000313|EMBL:AAW89806.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89806.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89806.1; -; Genomic_DNA. DR RefSeq; WP_010951200.1; NC_002946.2. DR RefSeq; YP_208218.1; NC_002946.2. DR RefSeq; YP_208244.1; NC_002946.2. DR EnsemblBacteria; AAW89806; AAW89806; NGO_1139. DR GeneID; 3281900; -. DR GeneID; 3282538; -. DR KEGG; ngo:NGO1139; -. DR KEGG; ngo:NGO1166; -. DR PATRIC; 20335538; VBINeiGon24812_1334. DR HOGENOM; HOG000218808; -. DR OrthoDB; EOG6VHZGB; -. DR BioCyc; NGON242231:GI2G-1052-MONOMER; -. DR BioCyc; NGON242231:GI2G-1079-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 81 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 10620 MW; 9878F4A8B3CFCBCE CRC64; MPLLSGLIPL LGILLKMLIV RIILATGLTF VTYAGYLAAL EKFKGYTANA INSMPSDILN LLLISGFGQG LGCLFGAFLV LHWYARIQKT DVCLSGMR // ID Q5F930_NEIG1 Unreviewed; 252 AA. AC Q5F930; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:AAW89307.1}; GN ORFNames=NGO_0574 {ECO:0000313|EMBL:AAW89307.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89307.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89307.1; -; Genomic_DNA. DR RefSeq; WP_003688976.1; NC_002946.2. DR RefSeq; YP_207719.1; NC_002946.2. DR ProteinModelPortal; Q5F930; -. DR SMR; Q5F930; 30-252. DR EnsemblBacteria; AAW89307; AAW89307; NGO_0574. DR GeneID; 3282155; -. DR KEGG; ngo:NGO0574; -. DR PATRIC; 20334214; VBINeiGon24812_0679. DR HOGENOM; HOG000112637; -. DR KO; K01674; -. DR OMA; WRFSGSL; -. DR OrthoDB; EOG65N1DV; -. DR BioCyc; NGON242231:GI2G-547-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR Gene3D; 3.10.200.10; -; 1. DR InterPro; IPR001148; Carbonic_anhydrase_a. DR InterPro; IPR023561; Carbonic_anhydrase_a-class. DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS. DR PANTHER; PTHR18952; PTHR18952; 1. DR Pfam; PF00194; Carb_anhydrase; 1. DR SMART; SM01057; Carb_anhydrase; 1. DR SUPFAM; SSF51069; SSF51069; 1. DR PROSITE; PS00162; ALPHA_CA_1; 1. DR PROSITE; PS51144; ALPHA_CA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256241. FT DOMAIN 31 252 Alpha-carbonic anhydrase. FT {ECO:0000259|PROSITE:PS51144}. SQ SEQUENCE 252 AA; 28085 MW; E4454A145A0F440F CRC64; MPRFPRTLPR LTAVLLLACT AFSAAAHGNH THWGYTGHDS PESWGNLSEE FRLCSTGKNQ SPVNITETVS GKLPAIKVNY KPSMVDVENN GHTIQVNYPE GGNTLTVNGR TYTLKQFHFH VPSENQIKGR TFPMEAHFVH LDENKQPLVL AVLYEAGKTN GRLSSIWNVM PMTAGKVKLN QPFDASTLLP KRLKYYRFAG SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR PVQPLNARVV IE // ID Q5F6E4_NEIG1 Unreviewed; 315 AA. AC Q5F6E4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90243.2}; GN ORFNames=NGO_1615 {ECO:0000313|EMBL:AAW90243.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90243.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90243.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6E4; -. DR EnsemblBacteria; AAW90243; AAW90243; NGO_1615. DR PATRIC; 20336770; VBINeiGon24812_1930. DR HOGENOM; HOG000064546; -. DR OMA; RELYDCK; -. DR OrthoDB; EOG61VZ4C; -. DR BioCyc; NGON242231:GI2G-1512-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 315 AA; 35672 MW; DF19082AA6CC10E0 CRC64; MTFQGHNNRK KAGGYAEYIT GGSLRRLVAA KVRRYCGEHP GVFDGAAGSG QLEQYIEPSD FRAVEIQAEA CKALLQNYPA AKVYNTSLFL YTDGEPQDCT VMNPPFSIKL KDLSEDEKSR IAQEYPWKKS GVADEIFVLK GLENARRFGF FILFPGIAYR KSEQRFREII GNRLAELNRI QNAFEDTPIE VLLLVIDKDK TDGGCIRELY DCKTDTLLAA DTWQIEPDLW QTVQEPAPPK EKEDPVLLEH ECRDAAAKRI ARELRFSKMV NEIEGWPHAE FDGFCDRLCN LIQAEKYGKK HYFPCSLPLF GGAAG // ID Q5F7Z2_NEIG1 Unreviewed; 346 AA. AC Q5F7Z2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89695.2}; GN ORFNames=NGO_1012 {ECO:0000313|EMBL:AAW89695.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89695.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89695.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89695; AAW89695; NGO_1012. DR PATRIC; 20335232; VBINeiGon24812_1184. DR OMA; YKTAGFF; -. DR OrthoDB; EOG62C9F8; -. DR BioCyc; NGON242231:GI2G-938-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009295; C:nucleoid; IEA:InterPro. DR InterPro; IPR007358; Nucleoid_associated_NdpA. DR Pfam; PF04245; NA37; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 346 AA; 39449 MW; 40A291E5AA8B75D5 CRC64; MKKIITHRIY PKNENRERVE PKISTHLIDL PITARRTLET RLTKALGNKS HGIEMSVVNT AENSFFQIAA AIQLKEEAEF IEDSAQFAHM LTDAQLNTNA PGGILLVLKG RVGDTGKPFL CVIKAEPQDG FRTKEEDDFI TIEFLEELLL TDSARLFKIG FLVAETVRPL EQIQSGNYRA FLYDHLMTQT ETRPAASYFY QVFLGMSIAA SSRKLTQDFF EWTRNFIDNS DLSDDAKLDA HEALRVTLKS AEATISVNNF AQNHLPQEKR TAYTEFMVEK DFPQNAVSKD IEYIKTRLRK RRSYGFSNGV VILTPPEHTQ DYMEIAPTED GEYTVVLIKG QLQQQK // ID Q5F637_NEIG1 Unreviewed; 108 AA. AC Q5F637; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW90350.1}; GN ORFNames=NGO_1729 {ECO:0000313|EMBL:AAW90350.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90350.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90350.1; -; Genomic_DNA. DR RefSeq; WP_003689921.1; NC_002946.2. DR RefSeq; YP_208762.1; NC_002946.2. DR EnsemblBacteria; AAW90350; AAW90350; NGO_1729. DR GeneID; 3281258; -. DR KEGG; ngo:NGO1729; -. DR PATRIC; 20337056; VBINeiGon24812_2068. DR HOGENOM; HOG000285676; -. DR OMA; DHGHSKQ; -. DR OrthoDB; EOG6N3D0B; -. DR BioCyc; NGON242231:GI2G-1625-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025711; PepSY. DR Pfam; PF03413; PepSY; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256030. FT DOMAIN 47 104 PepSY. {ECO:0000259|Pfam:PF03413}. SQ SEQUENCE 108 AA; 11752 MW; 38889C37DADDB5EC CRC64; MNIKHLLLTA AATALLGISA PALAHHDGHG DDDHGHAAHQ HGKQDKIISR AQAEKAAWAR VGGKITDIDL EHDDGRPHYD VEIVKNGQEY KVVVDARTGR VISSRRDD // ID Q5F7F2_NEIG1 Unreviewed; 146 AA. AC Q5F7F2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=DNA polymerase III subunit chi {ECO:0000313|EMBL:AAW89885.1}; GN ORFNames=NGO_1226 {ECO:0000313|EMBL:AAW89885.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89885.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89885.1; -; Genomic_DNA. DR RefSeq; WP_003706740.1; NC_002946.2. DR RefSeq; YP_208297.1; NC_002946.2. DR ProteinModelPortal; Q5F7F2; -. DR EnsemblBacteria; AAW89885; AAW89885; NGO_1226. DR GeneID; 3282151; -. DR KEGG; ngo:NGO1226; -. DR PATRIC; 20335765; VBINeiGon24812_1441. DR HOGENOM; HOG000263566; -. DR KO; K02339; -. DR OMA; YGAGQKV; -. DR OrthoDB; EOG68H887; -. DR BioCyc; NGON242231:GI2G-1137-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 146 AA; 16526 MW; F5FAEAE2412A6E47 CRC64; MPKVTFYTHV DQIPLFTCRL IARAIRDGGR ILVWSDSFGR LQELDKMLWQ YEAESFIPHE IWETEEAMPS DTSVLLACDG NLPRIPEGMA VLNLSDGFWN TASVLPARVL EIVGNSLEDL ADARERFTAY RRSGFAIEHH GMEGKA // ID Q5FA81_NEIG1 Unreviewed; 71 AA. AC Q5FA81; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88906.1}; GN ORFNames=NGO_0148 {ECO:0000313|EMBL:AAW88906.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88906.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88906.1; -; Genomic_DNA. DR ProteinModelPortal; Q5FA81; -. DR EnsemblBacteria; AAW88906; AAW88906; NGO_0148. DR PATRIC; 20333215; VBINeiGon24812_0190. DR HOGENOM; HOG000071369; -. DR OMA; SSAKACC; -. DR OrthoDB; EOG6MSSC6; -. DR BioCyc; NGON242231:GI2G-136-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 41 FAD_binding_3. FT {ECO:0000259|Pfam:PF01494}. SQ SEQUENCE 71 AA; 7490 MW; 34D5C0394B09CC91 CRC64; MPTQFDVAVI GAGPAGSAAS ALLRKKGYQV CVLENSTFRA SSSAKACCRT VWKCWKKPVL PMPFAPGPAF S // ID Q5F5H7_NEIG1 Unreviewed; 149 AA. AC Q5F5H7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90560.1}; GN ORFNames=NGO_1948 {ECO:0000313|EMBL:AAW90560.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90560.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90560.1; -; Genomic_DNA. DR RefSeq; WP_003701784.1; NC_002946.2. DR RefSeq; YP_208972.1; NC_002946.2. DR EnsemblBacteria; AAW90560; AAW90560; NGO_1948. DR GeneID; 3282672; -. DR KEGG; ngo:NGO1948; -. DR PATRIC; 20337641; VBINeiGon24812_2347. DR HOGENOM; HOG000198397; -. DR KO; K15977; -. DR OMA; LSMWAEL; -. DR OrthoDB; EOG61GGB6; -. DR BioCyc; NGON242231:GI2G-1850-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 16588 MW; 2BF9B5C400AA2F8D CRC64; MKIGTTWQTA SAMLVLRLFA AYEFLESGLQ KWNGENWFSE INDQFPFPFN LLPDALNWNL AMYAELLLPV LLLLGLATRL SALGLMVVTA VAWAAVHAGS GYNVCDNGYK MALIYIVVLI PLLFQGAGGW SLDTLLKKLF CPKCRLKQD // ID Q5F5Z2_NEIG1 Unreviewed; 343 AA. AC Q5F5Z2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160}; DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160}; GN Name=gapA {ECO:0000313|EMBL:AAW90395.1}; GN ORFNames=NGO_1776 {ECO:0000313|EMBL:AAW90395.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90395.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90395.1; -; Genomic_DNA. DR RefSeq; WP_003690340.1; NC_002946.2. DR RefSeq; YP_208807.1; NC_002946.2. DR ProteinModelPortal; Q5F5Z2; -. DR SMR; Q5F5Z2; 3-330. DR EnsemblBacteria; AAW90395; AAW90395; NGO_1776. DR GeneID; 3282461; -. DR KEGG; ngo:NGO1776; -. DR PATRIC; 20337194; VBINeiGon24812_2133. DR HOGENOM; HOG000071679; -. DR KO; K00134; -. DR OMA; NDQNNID; -. DR OrthoDB; EOG66TG3S; -. DR BioCyc; NGON242231:GI2G-1674-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU361160, KW ECO:0000313|EMBL:AAW90395.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 36965 MW; C7D46581E531F0A4 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 NALMKAVSEA GALKGVLGYN TLPLVSMDFN HTTEASHFDA TLTKVVDGNM VKVFAWYDNE WGFSCQMLNT ARRMFGLEVR PLK // ID Q5F869_NEIG1 Unreviewed; 113 AA. AC Q5F869; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:AAW89618.1}; GN ORFNames=NGO_0922 {ECO:0000313|EMBL:AAW89618.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89618.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89618.1; -; Genomic_DNA. DR RefSeq; WP_003688395.1; NC_002946.2. DR RefSeq; YP_208030.1; NC_002946.2. DR ProteinModelPortal; Q5F869; -. DR EnsemblBacteria; AAW89618; AAW89618; NGO_0922. DR GeneID; 3281726; -. DR KEGG; ngo:NGO0922; -. DR PATRIC; 20335027; VBINeiGon24812_1083. DR HOGENOM; HOG000160364; -. DR KO; K00242; -. DR OMA; QWMKVLT; -. DR OrthoDB; EOG6SV5BS; -. DR BioCyc; NGON242231:GI2G-860-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 69 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; 13113 MW; 6D08D25495857F00 CRC64; MVERKLTGAH YGLRDWVMQR ATAVIMLIYT VALLVVLFAL PKEYPAWQAF FSQAWVKVFT QVSFIAVFLH AWVGIRDLWM DYIKPFGVRL FLQVATIVWL VGCLVYSVKV IWG // ID Q5F989_NEIG1 Unreviewed; 1381 AA. AC Q5F989; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89248.1}; GN ORFNames=NGO_0510 {ECO:0000313|EMBL:AAW89248.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89248.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89248.1; -; Genomic_DNA. DR RefSeq; WP_010951067.1; NC_002946.2. DR RefSeq; YP_207660.1; NC_002946.2. DR EnsemblBacteria; AAW89248; AAW89248; NGO_0510. DR GeneID; 3282939; -. DR KEGG; ngo:NGO0510; -. DR PATRIC; 20334062; VBINeiGon24812_0603. DR HOGENOM; HOG000071313; -. DR OMA; HARSING; -. DR OrthoDB; EOG64FK93; -. DR BioCyc; NGON242231:GI2G-488-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR015406; DUF1983. DR InterPro; IPR032876; J_dom. DR Pfam; PF09327; DUF1983; 1. DR Pfam; PF13550; Phage-tail_3; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 222 406 Phage-tail_3. {ECO:0000259|Pfam:PF13550}. FT DOMAIN 892 951 DUF1983. {ECO:0000259|Pfam:PF09327}. SQ SEQUENCE 1381 AA; 150649 MW; 66AAD139183D3846 CRC64; MGGKSSTVTS AEERILSLQV QRSSQGLTLP VIYGRTRVAG NLIWYGDFVT IEHKAVTRQG GKGGGGVKQV GISYTYEAAV MLALCEGEIQ GVGRVWRDKE KFDSPAQLRL TLMRGGDEQP LWTHLQQAKH QGQALNYSGT AYLCSPNYEL TKSAQIYQHN FEVIGKSGYS GNIPDANPRE IVLDLLTNQR YGCGFPSQNI GDTDRYSNYC RAVGIFLSPA YTEQGEAQRN ISELLEQTNS AAVFSQGRLK IIPYGDGSHS GNGAVYVADN KAAYDLTDDD FIVSGAQDPV KAGRKTNADA FNQIQVEYLD RDNDYNVAIA EAKDQANIEQ YGLRPKDAVR MHGICDAKVA QKVAQQLLQR ALYVRNEYEF KLGWKYCLLE PMDIVTLTDA GLGLNKTPVR ITEIEEDGEG VLSVKAEDCP AGVYTVSEYP TQPSSGYSAD YNVSPGNAHV PVIFEAPLQL TGGEPQIWLA TAGGGMWGGA EVWVSADGDS YTRVGAVNRK ARFGALTADL PDGAVFDRTN TLGVEISAGQ LTGGTEQDSR DLLTLCYVDG EFLAYADAEL KGVGRYTLGN LTRGAYGSAV NAHAAGSRFA RIDEALFKYA VPRNWIGRTV WVKLVSYNVF GGGIQDLAEV PAYSYTIEGA PLGQIQNLRL TSSWAYGKEA VIAWDKLDGA DTYDVEIYAG GSRRRLRAVD GIVDNSYTYT QADMKADGGQ VRGIVFKVRG RAVTGKTGNW AQIAAQNPQL QALQGISIDS GLRQAFFTCQ KPDEEDFAGI IVWVCENAAC PAADANKAYD GAETFITIAK CGGKPLEKGK TYYLRAAGYD SFGKDNLKIS GSISFTVYDV SATDLSESSL NKALRDKINL IDGNGAGSVN ERVEAVRSTA DGNAAAVQTH ARSINGLEAQ YTVKVDANGK VAGFGLATTP KNGTPESKFI VNADRFGIGA AGKADVFPFV VDTQKNRVGI NGELVVNGKA VVDKLNAGDI HGGKIAADTL DANRLKAGSV TAREIGAAAV TADKIGANAV TADKIQVADL SAVSSNLGSI TGGSLNIGGG NFTVSSDGIL TADNAVIRGR IEADSGYFNG TVRASSVEGD VLRAHRLRWT EGNVWVLDLD KDPLPRVLIP NFYVVSETFG NNRVQAKLLL NGGVLAPREV RETENYTNYI WRGRTFGRYE DLPPRARGGG DYTEQSGSRY RTRLEYQIQV IPAGKPVSLK LSLASHESVF SPFVSVSYLA QSDYEYKQLL GRMVWRTFAE SFRYDSKKQI YLGGDRRVHD YQNQMYKHWN AYGGLLQLPD DIYGISFEYR PFTNADWSTM LAFDRSDKFV VVKKYRGHAP QQYSLFQEEF NTAVPKSNLL FFVEHWWQYI ELRNIRVLIP ESRENEVWPS V // ID Q5F9F5_NEIG1 Unreviewed; 327 AA. AC Q5F9F5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 84. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583}; GN ORFNames=NGO_0441 {ECO:0000313|EMBL:AAW89182.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89182.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000256|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; AE004969; AAW89182.1; -; Genomic_DNA. DR RefSeq; WP_003687900.1; NC_002946.2. DR RefSeq; YP_207594.1; NC_002946.2. DR ProteinModelPortal; Q5F9F5; -. DR EnsemblBacteria; AAW89182; AAW89182; NGO_0441. DR GeneID; 3282428; -. DR KEGG; ngo:NGO0441; -. DR PATRIC; 20333908; VBINeiGon24812_0528. DR HOGENOM; HOG000210449; -. DR KO; K00948; -. DR OMA; HENVRGQ; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; NGON242231:GI2G-420-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:AAW89182.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000313|EMBL:AAW89182.1}. FT DOMAIN 7 124 Pribosyltran_N. FT {ECO:0000259|Pfam:PF13793}. FT NP_BIND 40 42 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 99 102 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 196 198 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 223 230 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 310 312 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 132 132 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT METAL 134 134 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT METAL 143 143 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT METAL 147 147 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 108 108 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 134 134 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 139 139 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 173 173 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 327 AA; 35570 MW; 17049546F226A37C CRC64; MAAYDSLMVF TGNANPELAQ RVVRHLDISL GNASVSKFSD GEVAVELLEN VRGRDVFILQ PTCAPTNDNL MEILTMADAL KRASAGRITT AIPYFGYARQ DRRPRSVRVP ISAKLVANML YSAGIDRVLT VDLHADQIQG FFDIPVDNIY ATPILLNDIK QQRIENLTVV SPDIGGVVRA RAVAKSLNAD LAIIDKRRPK ANVAEVMNII GDIQGKTCLI VDDMIDTANT LCKAAVALKE RGAERVLAYA SHAVFSGEAV SRIASSEIDQ VVVTDTIPLS EAAKNCDRIR QVTIAGLLAE TVRRISNEES VSYLFNEEVM TGSMLLP // ID Q5F8Z5_NEIG1 Unreviewed; 384 AA. AC Q5F8Z5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 71. DE SubName: Full=Ribonucleotide-diphosphate reductase subunit beta {ECO:0000313|EMBL:AAW89342.1}; DE EC=1.17.4.1 {ECO:0000313|EMBL:AAW89342.1}; GN ORFNames=NGO_0615 {ECO:0000313|EMBL:AAW89342.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89342.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89342.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F8Z5; -. DR SMR; Q5F8Z5; 9-350. DR EnsemblBacteria; AAW89342; AAW89342; NGO_0615. DR PATRIC; 20334312; VBINeiGon24812_0728. DR HOGENOM; HOG000278087; -. DR OMA; LEPMFLG; -. DR OrthoDB; EOG6J48J7; -. DR BioCyc; NGON242231:GI2G-582-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89342.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 384 AA; 44054 MW; FE45A26E1BAE14F2 CRC64; MSCEHLVMSY STFPKTKNDA LKEPMFFGQP VNVARYDQQK YEVFEKLIEK QLSFFWRPEE IDVSRDRIDY ANLPEHEKHI FISNLKYQTL LDSIQGRSPN VALLPLVSIP ELETWVETWS FSETIHSRSY THIIRNIVND PSVVFDDIVE NEYITARAED IACYYDDLIE YTQYYNLLGE GVHNVGGKPV TVSLRGLKKK LYLCLMCVNV LEAIRFYVSF ACSFAFAERE LMEGNAKIIK LIARDEALHL TGTQHMLNLM RSGVDDPEMA EIAAELQDEC FQLFKKAAEQ EKEWAAYLFK DGSMIGLNKE ILSQYVEYIT NLRMQAVGLP AGFEGANQNP IPWINAWLSS DNVQVAPQEV EISSYLIGQI DSEVNTDDLG DFEL // ID Q5F7I5_NEIG1 Unreviewed; 114 AA. AC Q5F7I5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 57. DE SubName: Full=Murein hydrolase transporter LrgA {ECO:0000313|EMBL:AAW89852.1}; GN ORFNames=NGO_1192 {ECO:0000313|EMBL:AAW89852.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89852.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89852.1; -; Genomic_DNA. DR RefSeq; WP_002219918.1; NC_002946.2. DR RefSeq; YP_208264.1; NC_002946.2. DR EnsemblBacteria; AAW89852; AAW89852; NGO_1192. DR GeneID; 3281957; -. DR KEGG; ngo:NGO1192; -. DR PATRIC; 20335681; VBINeiGon24812_1399. DR HOGENOM; HOG000253615; -. DR KO; K06518; -. DR OMA; GYTTQMM; -. DR OrthoDB; EOG65N1HV; -. DR BioCyc; NGON242231:GI2G-1104-MONOMER; -. DR Proteomes; UP000000535; 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:0016787; F:hydrolase activity; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89852.1}; KW Membrane {ECO:0000256|SAAS:SAAS00459668, KW ECO:0000256|SAAS:SAAS00459673, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 85 104 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 114 AA; 12210 MW; 42D67A9EEF578AE6 CRC64; MNIIRALLII LGCLAAGETA VFLAGIKLPG SIVGMGVLFA LLQAGWVKTS WLQQLTDALM ANLTLFLVPP CVAVISYLDL IADDWFSILV SASASTLCVL LVTGKVHRWI RSII // ID Q5FAA3_NEIG1 Unreviewed; 110 AA. AC Q5FAA3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88884.2}; GN ORFNames=NGO_0124 {ECO:0000313|EMBL:AAW88884.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88884.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88884.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88884; AAW88884; NGO_0124. DR PATRIC; 20333151; VBINeiGon24812_0159. DR BioCyc; NGON242231:GI2G-113-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 10676 MW; DD58D4054410457A CRC64; MNEMTAVFGG TEGTWGHRGR VSGEWVGSKV GGALGSFAGA FTGMAGGALV TGGNPAGIAI GGAGGGWVGA EGGSALGGHI GGFAGAKWGK MIDRRNCQCG EDCHCDPCNC // ID Q5F948_NEIG1 Unreviewed; 497 AA. AC Q5F948; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89289.1}; GN ORFNames=NGO_0555 {ECO:0000313|EMBL:AAW89289.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89289.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89289.1; -; Genomic_DNA. DR RefSeq; WP_010951081.1; NC_002946.2. DR RefSeq; YP_207701.1; NC_002946.2. DR ProteinModelPortal; Q5F948; -. DR EnsemblBacteria; AAW89289; AAW89289; NGO_0555. DR GeneID; 3282453; -. DR KEGG; ngo:NGO0555; -. DR PATRIC; 20334164; VBINeiGon24812_0654. DR HOGENOM; HOG000071304; -. DR OMA; WRINSHA; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NGON242231:GI2G-529-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 497 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256244. FT DOMAIN 112 179 TPR_REGION. FT {ECO:0000259|PROSITE:PS50293}. SQ SEQUENCE 497 AA; 56617 MW; 22A53EB188730058 CRC64; MTHRLCLLFL PLCTVCLAAP SNDAADERRR LLDEGSRQTQ QYRESGWLDT EQARGEVEEN DGYISIGGEI YQVGDTAEEL ESAIYHALNA RQWHKVRQFA ARYAKLPRHK PALIHLADAL QKRDEGDFRA AGNSFQTALE AEPDNPRLLL EAGRFYAEDN QNKESAAAFE KVLKTDIPAE TRPIVENYLS ELGKRRRWHG QISLGYGYNS NVNQGNGINQ CVWEIAGMCL MERTLPAPTD STFSSYSATA EKTVPLKGNH GVQVRGVLYG NRYTEKDKDS AAMPDYGYRN GSLYAGYAYA DARSSFSLLP YFEYDFRNRH THYRAWGADA DWSRTLSPHW RINSHAGAKK TGYGGQSKTY FADFKQYELG AGAEFSITLK SGLLVNFDAA RKAYPEKSSS SKEYTARLGA YRLFSGGTYL NAVLLYRRSL YDAASFVSDN KRRRDKQYIM MAAAGFPQWN IKGVYPELRF RRTIAHSNAV YYRYRQNEWL LGFKYRF // ID Q5F7Z5_NEIG1 Unreviewed; 95 AA. AC Q5F7Z5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89692.1}; GN ORFNames=NGO_1009 {ECO:0000313|EMBL:AAW89692.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89692.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89692.1; -; Genomic_DNA. DR RefSeq; WP_010951160.1; NC_002946.2. DR RefSeq; YP_208104.1; NC_002946.2. DR EnsemblBacteria; AAW89692; AAW89692; NGO_1009. DR GeneID; 3282180; -. DR KEGG; ngo:NGO1009; -. DR PATRIC; 20335226; VBINeiGon24812_1181. DR HOGENOM; HOG000071269; -. DR OMA; WACGYRY; -. DR OrthoDB; EOG676Z61; -. DR BioCyc; NGON242231:GI2G-935-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 95 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005697557. SQ SEQUENCE 95 AA; 11032 MW; B04DCD21AB0F1648 CRC64; MIEFVRAKKR LLWAFVLLLA WACGYRYAAD KVEAEQTALI AAYRHSSMVA AEQYALQLKK AQDERQRWYD FSQKQSTDLA AALSELDKTR NTLQE // ID Q5F8C4_NEIG1 Unreviewed; 82 AA. AC Q5F8C4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89563.1}; GN ORFNames=NGO_0861 {ECO:0000313|EMBL:AAW89563.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89563.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89563.1; -; Genomic_DNA. DR RefSeq; WP_003688538.1; NC_002946.2. DR RefSeq; YP_207975.1; NC_002946.2. DR EnsemblBacteria; AAW89563; AAW89563; NGO_0861. DR GeneID; 3282378; -. DR KEGG; ngo:NGO0861; -. DR PATRIC; 20334890; VBINeiGon24812_1015. DR OrthoDB; EOG68WRG1; -. DR BioCyc; NGON242231:GI2G-805-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 82 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256231. SQ SEQUENCE 82 AA; 9512 MW; AF3D2463962D05BA CRC64; MKMKKLILLS VAAMLVTACT YADRRFVTQE SAAEIQAKSR AIQISERAER AEYRKERREE MMDAARAIKK ANENSPNIYF IR // ID Q5FAB3_NEIG1 Unreviewed; 85 AA. AC Q5FAB3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:AAW88874.1}; GN ORFNames=NGO_0114 {ECO:0000313|EMBL:AAW88874.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88874.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88874.1; -; Genomic_DNA. DR RefSeq; WP_003687379.1; NC_002946.2. DR RefSeq; YP_207286.1; NC_002946.2. DR ProteinModelPortal; Q5FAB3; -. DR EnsemblBacteria; AAW88874; AAW88874; NGO_0114. DR GeneID; 3283078; -. DR KEGG; ngo:NGO0114; -. DR PATRIC; 20333131; VBINeiGon24812_0149. DR HOGENOM; HOG000095203; -. DR KO; K03676; -. DR OMA; MARVVMY; -. DR OrthoDB; EOG6Z3KS6; -. DR BioCyc; NGON242231:GI2G-103-MONOMER; -. DR Proteomes; UP000000535; 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; -; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 85 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. SQ SEQUENCE 85 AA; 9311 MW; FEA7FF550450C395 CRC64; MQTVTMYTGP FCPYCAMAKR LLHAAGVGHI DEIRVDASPE AFAEMQRLSG QRSVPQIFIG ETHVGGFTDL YRLQQEGGLD GLLNP // ID Q5F8J0_NEIG1 Unreviewed; 170 AA. AC Q5F8J0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89497.1}; GN ORFNames=NGO_0783 {ECO:0000313|EMBL:AAW89497.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89497.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89497.1; -; Genomic_DNA. DR RefSeq; WP_003688633.1; NC_002946.2. DR RefSeq; YP_207909.1; NC_002946.2. DR EnsemblBacteria; AAW89497; AAW89497; NGO_0783. DR GeneID; 3281943; -. DR KEGG; ngo:NGO0783; -. DR PATRIC; 20334712; VBINeiGon24812_0928. DR HOGENOM; HOG000218959; -. DR OMA; AATIYKY; -. DR OrthoDB; EOG6GN722; -. DR BioCyc; NGON242231:GI2G-737-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 170 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256063. FT COILED 146 170 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 170 AA; 18471 MW; 42C5102745F58E40 CRC64; MKSKLPLILI NLSLISSPLG ANAAKIYTCT INGETVYTTK PSKSCHSTDL PPIGNYSSER YILPQTPEPA PSPSNGGQAV KYKAPVKTVS KPAKSNTPPQ QAPVNNSRRS ILEAELSNER KALTEAQKML SQARLAKGGN INHQKINALQ SNVLDRQQNI QALQRELGRM // ID Q5F6V4_NEIG1 Unreviewed; 129 AA. AC Q5F6V4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 66. DE SubName: Full=Type IV pilin protein {ECO:0000313|EMBL:AAW90083.1}; GN ORFNames=NGO_1441 {ECO:0000313|EMBL:AAW90083.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90083.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90083.1; -; Genomic_DNA. DR RefSeq; WP_010951266.1; NC_002946.2. DR RefSeq; YP_208495.1; NC_002946.2. DR ProteinModelPortal; Q5F6V4; -. DR EnsemblBacteria; AAW90083; AAW90083; NGO_1441. DR GeneID; 3281720; -. DR KEGG; ngo:NGO1441; -. DR PATRIC; 20336301; VBINeiGon24812_1699. DR HOGENOM; HOG000008197; -. DR KO; K02655; -. DR OMA; TNEGETC; -. DR OrthoDB; EOG6NWBPW; -. DR BioCyc; NGON242231:GI2G-1348-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 14381 MW; B1D65EEAA91FB5C0 CRC64; MKNVQKGFTL LELMIAVAIL GILTLIAYPS YKTYIRRARL SEVKSTLLMN AQNLERYYRQ KGTFEKYDST KLKQNKYFKI TLIKASPDHF TLQAAPDTAT NEGETCTVTL NDGGTIAASG TNQSCPGFD // ID Q5F8Z8_NEIG1 Unreviewed; 255 AA. AC Q5F8Z8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267}; DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267}; GN ORFNames=NGO_0611 {ECO:0000313|EMBL:AAW89339.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89339.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC {ECO:0000256|RuleBase:RU361267}. 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:0000256|RuleBase:RU361267}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {ECO:0000256|RuleBase:RU361267}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89339.1; -; Genomic_DNA. DR RefSeq; WP_003688926.1; NC_002946.2. DR RefSeq; YP_207751.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z8; -. DR EnsemblBacteria; AAW89339; AAW89339; NGO_0611. DR GeneID; 3281750; -. DR KEGG; ngo:NGO0611; -. DR PATRIC; 20334302; VBINeiGon24812_0723. DR HOGENOM; HOG000220746; -. DR KO; K00655; -. DR OMA; EMAPRRQ; -. DR OrthoDB; EOG654P6D; -. DR BioCyc; NGON242231:GI2G-579-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. 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 {ECO:0000256|RuleBase:RU361267, KW ECO:0000313|EMBL:AAW89339.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361267}; KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267}; KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU361267, KW ECO:0000313|EMBL:AAW89339.1}. FT DOMAIN 72 184 PlsC. {ECO:0000259|SMART:SM00563}. SQ SEQUENCE 255 AA; 27758 MW; 833F1A9361A5CC58 CRC64; MSSNKASFFT RLRRLCRLTV WLFKTGKNLR GIDGGCPKSR NRAVIALGKG ALAALDIGLE VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIKVDF VCVADAAESE DRYALKDKIE ESIRAVVAGD ADVAV // ID Q5F547_NEIG1 Unreviewed; 208 AA. AC Q5F547; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90690.1}; GN ORFNames=NGO_2089 {ECO:0000313|EMBL:AAW90690.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90690.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90690.1; -; Genomic_DNA. DR RefSeq; WP_003687047.1; NC_002946.2. DR RefSeq; YP_209102.1; NC_002946.2. DR ProteinModelPortal; Q5F547; -. DR EnsemblBacteria; AAW90690; AAW90690; NGO_2089. DR GeneID; 3282828; -. DR KEGG; ngo:NGO2089; -. DR PATRIC; 20338011; VBINeiGon24812_2528. DR HOGENOM; HOG000146210; -. DR OMA; FRELWQA; -. DR OrthoDB; EOG6C5RS9; -. DR BioCyc; NGON242231:GI2G-1984-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003814; FwdEsu_dom. DR Pfam; PF02663; FmdE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 46 197 FmdE. {ECO:0000259|Pfam:PF02663}. SQ SEQUENCE 208 AA; 22206 MW; 31F30C3F47175EE9 CRC64; MTQERLPEFF DRAPTLTVQD PLAAFLGAAE NGILTYRYAD AVRLCGHSCP TVAGAYLMVI KGLKALYGEE LPERGGIEAA MQGTRDEGTV GVTASVVQLL TGAAPETGFG GIGMQGRFAR RNLLSFGAGE INGTLTLRRK DSGKTVAVSL NAALQPFAPQ MRDIMPKAVG GSASAKELER FGQLWQARVK AFLTESADDP QFVIVREL // ID Q5F6H9_NEIG1 Unreviewed; 244 AA. AC Q5F6H9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAW90208.1}; GN ORFNames=NGO_1579 {ECO:0000313|EMBL:AAW90208.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90208.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90208.1; -; Genomic_DNA. DR RefSeq; WP_010358997.1; NC_002946.2. DR RefSeq; YP_208620.1; NC_002946.2. DR ProteinModelPortal; Q5F6H9; -. DR DNASU; 3281427; -. DR EnsemblBacteria; AAW90208; AAW90208; NGO_1579. DR GeneID; 3281427; -. DR KEGG; ngo:NGO1579; -. DR PATRIC; 20336684; VBINeiGon24812_1888. DR HOGENOM; HOG000186461; -. DR KO; K01420; -. DR OMA; ARCSVCA; -. DR OrthoDB; EOG6RVFWF; -. DR BioCyc; NGON242231:GI2G-1476-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00433748}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 27410 MW; 476CDE0CE52313A3 CRC64; MASHNTTHQM KTLCSSCSLR ELCLPVGLLP NEFSQLDAVI RQSRRLKKGE YLFRAGGAFT SLFAIRSGFF KTTVASQDGR DQVTGFFMSG ELIGMDGICS YVHSCDAVAL ENSEVCELPF THIEELGQNI PSLRTHFFRM ISREIVRDQG VMLLLGNMRA EERIAAFLLN LSQRLYSRGF AANDFILRMS REEIGSYLGL KLETVSRTLS KFHQEGLISV EHKHIKILNL QVLKKMVSGC SHAI // ID Q5FA39_NEIG1 Unreviewed; 321 AA. AC Q5FA39; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 70. DE SubName: Full=Putrescine/spermidine ABC transporter permease {ECO:0000313|EMBL:AAW88948.1}; GN ORFNames=NGO_0195 {ECO:0000313|EMBL:AAW88948.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88948.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88948.1; -; Genomic_DNA. DR RefSeq; WP_003690691.1; NC_002946.2. DR RefSeq; YP_207360.1; NC_002946.2. DR ProteinModelPortal; Q5FA39; -. DR EnsemblBacteria; AAW88948; AAW88948; NGO_0195. DR GeneID; 3281667; -. DR KEGG; ngo:NGO0195; -. DR PATRIC; 20333319; VBINeiGon24812_0242. DR HOGENOM; HOG000263582; -. DR KO; K11075; -. DR OMA; MLNTNFA; -. DR OrthoDB; EOG6HMXBZ; -. DR BioCyc; NGON242231:GI2G-178-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 35924 MW; D37AEFD9E31CBA96 CRC64; MNLNKLKNKL FRRPGQRAVI AVPYIWLLVL FLIPFAIVLK ISFAEQEIAI PPFTPLTTID EDLGRLNIAV SYQNYADIFQ NFWHTLNPFG DSENSNIYLM TYWSSIKTAL TTTVICLLVG YPTAYAISRA NPSVRNGLLL AIMLPFWTSF LLRVYAWMGL LGHNGIINNL LIKMGIIREP LDLFYNAFSL NLVMVYAYLP FMILPLYTQL VKLDSRLLEA ASDLGAGPVK SFLTITLPLS KTGIIAGSML VFVPAVGEFV IPELVGGSEN LMIGKVLWQA FFDQNNWPLA SAVAVVMVAL LVVPIALFQH YENRELEEGA K // ID Q5F9S9_NEIG1 Unreviewed; 135 AA. AC Q5F9S9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89058.1}; GN ORFNames=NGO_0311 {ECO:0000313|EMBL:AAW89058.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89058.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89058.1; -; Genomic_DNA. DR RefSeq; WP_003687699.1; NC_002946.2. DR RefSeq; YP_207470.1; NC_002946.2. DR EnsemblBacteria; AAW89058; AAW89058; NGO_0311. DR GeneID; 3281699; -. DR KEGG; ngo:NGO0311; -. DR OMA; GASHDIY; -. DR OrthoDB; EOG6FBX4C; -. DR BioCyc; NGON242231:GI2G-291-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 135 AA; 15900 MW; 899D1B878CBA6070 CRC64; MNIIEIISRN RFLKQIYPSG IMDISLVSFS TDLSNCILTI RTSTKPSVEI EKWGLWLKDY DTVEIELRNS FIKGMKCQNW SHNNRNICQV EIKNQEDGLK IIRFYDNNSN WLLELEVYGL VFQGCKTYMK EGYES // ID Q5F5K8_NEIG1 Unreviewed; 149 AA. AC Q5F5K8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90529.1}; GN ORFNames=NGO_1916 {ECO:0000313|EMBL:AAW90529.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90529.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90529.1; -; Genomic_DNA. DR RefSeq; WP_003688065.1; NC_002946.2. DR RefSeq; YP_208941.1; NC_002946.2. DR EnsemblBacteria; AAW90529; AAW90529; NGO_1916. DR GeneID; 3282856; -. DR KEGG; ngo:NGO1916; -. DR PATRIC; 20337566; VBINeiGon24812_2311. DR HOGENOM; HOG000218690; -. DR KO; K09943; -. DR OMA; FDMVIFP; -. DR OrthoDB; EOG6N685J; -. DR BioCyc; NGON242231:GI2G-1818-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 16523 MW; E7C66AF6EB5D9330 CRC64; MSIYAVAHII HLYCATAFVG GVFFEVLVLS VLHTGRVSRE ARREVEKAMS YRAVRVMPFA VGLLFASGIV MAANRYLPIS GEPFATSFGT MLTLKILLAF SVLAHFAIAV VKMARSTLTV GWSKYIHAVV FTHMLLIVFL AKAMFYISW // ID Q5F7S7_NEIG1 Unreviewed; 472 AA. AC Q5F7S7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89760.1}; GN ORFNames=NGO_1093 {ECO:0000313|EMBL:AAW89760.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89760.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89760.1; -; Genomic_DNA. DR RefSeq; WP_010951180.1; NC_002946.2. DR RefSeq; YP_208172.1; NC_002946.2. DR EnsemblBacteria; AAW89760; AAW89760; NGO_1093. DR GeneID; 3281081; -. DR KEGG; ngo:NGO1093; -. DR PATRIC; 20335438; VBINeiGon24812_1285. DR BioCyc; NGON242231:GI2G-1005-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 472 AA; 49015 MW; B037E63653B8C89F CRC64; MSDLVRYDPL EHGRLVGGLK EYRGFTQKDA RAAADDTALT RGFKNSMRSA RMGWNALTGD KEELGRLKAE DMDYRKIQEG RKSQARRELG EAWEKGGGVG GGLSNVWGEL KKDWREKGLD GALEDVGEMA GAVLEQAPNA LVPIATATAG GILGALAGGN AAVGAYAGAT LGNTLMEYGG QLDRAAEAAG VDPADKDAVM AFIGRGAPGA LKNAAVKGAV VGAADMAAMK LGGSILNMGK KAAGKAALEK MGVAAADKAA VAAAKGTPEF AALAKESAKG GLGGAARHAA AYATESAGEF AGEYLGTGLA NGEWDEKGAA LEAFSSLGHS AVGFAGTKAY AAVTDPLRPP GRTEGGCAGG YRGQQEGGQA GPGRGAGVAC GGTGGCGRRH RRLRTEARNR AARVSIRRIT ISRIRLCGSL RTVRSRRRRG GFSAALPTAI RRTRRNWRAG RKNSRMFRVS RRRTGRNFWI RA // ID Q5FAB5_NEIG1 Unreviewed; 416 AA. AC Q5FAB5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 80. DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:AAW88872.1}; GN ORFNames=NGO_0112 {ECO:0000313|EMBL:AAW88872.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88872.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88872.1; -; Genomic_DNA. DR RefSeq; WP_010950993.1; NC_002946.2. DR RefSeq; YP_207284.1; NC_002946.2. DR ProteinModelPortal; Q5FAB5; -. DR EnsemblBacteria; AAW88872; AAW88872; NGO_0112. DR GeneID; 3282418; -. DR KEGG; ngo:NGO0112; -. DR PATRIC; 20333125; VBINeiGon24812_0146. DR HOGENOM; HOG000223178; -. DR KO; K07645; -. DR OMA; GIPESEC; -. DR OrthoDB; EOG6G4VQG; -. DR BioCyc; NGON242231:GI2G-101-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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:UP000000535}; KW Kinase {ECO:0000256|SAAS:SAAS00529081, ECO:0000313|EMBL:AAW88872.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00528924}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00529081, KW ECO:0000313|EMBL:AAW88872.1}. FT DOMAIN 200 414 Histidine kinase. FT {ECO:0000259|PROSITE:PS50109}. SQ SEQUENCE 416 AA; 46599 MW; FA28975706F69671 CRC64; MFVPLAMLAG MFSYYETFHE TEALQDDLLR QAALYVGPDS KPETLPEGDG DTRILVQMPQ QEDPVVSLPA HLADGLHTLQ ADGDDDYYRV YIRTTEQGRI AVMQENEYRE DLAEDAARQS VLPLLAALPL MILLTVWITH KAMRPVRKLS QSLEQRRING LSALSVYNIP SKIRGFVTAI NLLLKRVDED IRRRQRFVAD AAHELRTPMT ALSLQAERLN NMPLPPDAGR QSAVLQQSIR RNKHLLEQLL ALARSQSDET PLTKTTFGLQ SRFRQVLQEL MPLALEKRQD IGVAVGGDVE VSADETEIYT LVKTFADNAV RYTPNGGRID LGFTDEGKYL AVWVEDNGNG IPESECPRVL DPFYRILGTE QQGAGLGLSI ADTLAKKYGG YLELTDSRRF GHGLLIRALL DKETLK // ID Q5F7D9_NEIG1 Unreviewed; 295 AA. AC Q5F7D9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Endonuclease {ECO:0000313|EMBL:AAW89898.1}; GN ORFNames=NGO_1239 {ECO:0000313|EMBL:AAW89898.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89898.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89898.1; -; Genomic_DNA. DR RefSeq; WP_003689695.1; NC_002946.2. DR RefSeq; YP_208310.1; NC_002946.2. DR EnsemblBacteria; AAW89898; AAW89898; NGO_1239. DR GeneID; 3282481; -. DR KEGG; ngo:NGO1239; -. DR PATRIC; 20335797; VBINeiGon24812_1458. DR HOGENOM; HOG000219032; -. DR KO; K09968; -. DR OMA; RINEICS; -. DR OrthoDB; EOG6Z6FTR; -. DR BioCyc; NGON242231:GI2G-1151-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR000305; GIY-YIG_SF. DR PROSITE; PS50164; GIY_YIG; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89898.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89898.1}; KW Nuclease {ECO:0000313|EMBL:AAW89898.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 21 115 GIY-YIG. {ECO:0000259|PROSITE:PS50164}. SQ SEQUENCE 295 AA; 33016 MW; 3795B31194B446F6 CRC64; MVAKIKKFSD STLSVLNNGE RRFYVYCLTD LKKDKILYIG KGCGNRIFEH EWVASRSQDP VSGEIIDRKL KAISKCKKLG RYIISYHLTE VEALAAESAL IHFVKSVLGK KLKNKIAGHG PGGISVEELD RRFGFSSLPL SEINPDGLIL AIKIHNAFDL DTDEELDYLF DNQDDANLKS RTLGNWVIGK DVASKVKYVI GVHTGLQNAV VSAYEVDGFE TMTEETKNGR KQTRYRFRTT SRSEEVLAKL GLQQKCLPEL KFGSGGGKAY IRPKTEQETL QTIPSPKITK ENPKS // ID Q5FAB7_NEIG1 Unreviewed; 62 AA. AC Q5FAB7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88870.1}; GN ORFNames=NGO_0109 {ECO:0000313|EMBL:AAW88870.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88870.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88870.1; -; Genomic_DNA. DR RefSeq; WP_003690577.1; NC_002946.2. DR RefSeq; YP_207282.1; NC_002946.2. DR EnsemblBacteria; AAW88870; AAW88870; NGO_0109. DR GeneID; 3282413; -. DR KEGG; ngo:NGO0109; -. DR PATRIC; 20333117; VBINeiGon24812_0142. DR HOGENOM; HOG000071367; -. DR OMA; MIGVFKI; -. DR OrthoDB; EOG6P33G9; -. DR BioCyc; NGON242231:GI2G-99-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 6736 MW; AA35B2A3E5B8637F CRC64; MPNKQTKSKS RKTGSGFAAF LYGPGSVKVC RLPDNARQMI GVFKIPRVRH APRSAMIGGS FV // ID Q5F521_NEIG1 Unreviewed; 164 AA. AC Q5F521; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 51. DE SubName: Full=ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW90716.2}; GN ORFNames=NGO_2118 {ECO:0000313|EMBL:AAW90716.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90716.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90716.2; -; Genomic_DNA. DR DNASU; 3282802; -. DR EnsemblBacteria; AAW90716; AAW90716; NGO_2118. DR PATRIC; 20338083; VBINeiGon24812_2564. DR HOGENOM; HOG000255143; -. DR OMA; EQYIGLE; -. DR OrthoDB; EOG6F296G; -. DR BioCyc; NGON242231:GI2G-2010-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 40 117 MlaD. {ECO:0000259|Pfam:PF02470}. SQ SEQUENCE 164 AA; 16976 MW; 69E08BB671874180 CRC64; MKKNILEFWV GLFVLIGAAA VAFLAFRVAG GAAFGGSDKT YAVYADFGDI GGLKVNAPVK SAGVLVGRVG AIGLDPKSYQ ARVRLDLDGK YQFSSDVSAQ ILTSGLLGEQ YIGLQQGGDT ENLAAGDTIS VTSSAMVLEN LIGKFMTSFA EKNAEGGNAE KAAE // ID Q5F9Q5_NEIG1 Unreviewed; 104 AA. AC Q5F9Q5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 44. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAW89082.1}; GN ORFNames=NGO_0337 {ECO:0000313|EMBL:AAW89082.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89082.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89082.1; -; Genomic_DNA. DR RefSeq; WP_003687735.1; NC_002946.2. DR RefSeq; YP_207494.1; NC_002946.2. DR EnsemblBacteria; AAW89082; AAW89082; NGO_0337. DR GeneID; 3281725; -. DR KEGG; ngo:NGO0337; -. DR PATRIC; 20333665; VBINeiGon24812_0410. DR HOGENOM; HOG000218858; -. DR OMA; ACARNIP; -. DR OrthoDB; EOG69GZPR; -. DR BioCyc; NGON242231:GI2G-317-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000313|EMBL:AAW89082.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 104 AA; 11685 MW; D62123EDD21D0FC5 CRC64; MSRLFLLLFP WATLAACTRN IPASPAVSNC AHLHNRTVLY FDAHGKPADS TAKGGFYRTV EIHDTNRILI QDFNSTGNAL VKPYWSDCRK LSVFPDKHLT MSHP // ID Q5F6C6_NEIG1 Unreviewed; 75 AA. AC Q5F6C6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90261.1}; GN ORFNames=NGO_1633 {ECO:0000313|EMBL:AAW90261.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90261.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90261.1; -; Genomic_DNA. DR RefSeq; WP_003691442.1; NC_002946.2. DR RefSeq; YP_208673.1; NC_002946.2. DR EnsemblBacteria; AAW90261; AAW90261; NGO_1633. DR GeneID; 3281378; -. DR KEGG; ngo:NGO1633; -. DR PATRIC; 20336802; VBINeiGon24812_1946. DR HOGENOM; HOG000071226; -. DR OMA; QPITHYS; -. DR OrthoDB; EOG679TGV; -. DR BioCyc; NGON242231:GI2G-1530-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 75 AA; 8370 MW; DC25D5F71CCA8FE6 CRC64; MNQKQTQCKQ IVDYIRNKGC ITSLEAYQNL KVTQLAARIT DLEGRGFVFA KPRMKAGGRG KPVTHYSIVK NGAEV // ID Q5F6U4_NEIG1 Unreviewed; 165 AA. AC Q5F6U4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90093.1}; GN ORFNames=NGO_1451 {ECO:0000313|EMBL:AAW90093.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90093.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90093.1; -; Genomic_DNA. DR RefSeq; WP_003689329.1; NC_002946.2. DR RefSeq; YP_208505.1; NC_002946.2. DR EnsemblBacteria; AAW90093; AAW90093; NGO_1451. DR GeneID; 3281678; -. DR KEGG; ngo:NGO1451; -. DR PATRIC; 20336321; VBINeiGon24812_1709. DR HOGENOM; HOG000218796; -. DR OMA; FVQLIQN; -. DR OrthoDB; EOG6JX7K2; -. DR BioCyc; NGON242231:GI2G-1358-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025402; DUF4375. DR Pfam; PF14300; DUF4375; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 39 159 DUF4375. {ECO:0000259|Pfam:PF14300}. SQ SEQUENCE 165 AA; 18426 MW; 7A053C273FB861B1 CRC64; MTALTLPEDI RQQEPSVLLY TLVSAYLEHT AQTGDESLSC LSDDQHTLTA FCYLDSQVEE GGFVQLIASG YGEYIFRNPL ADSLRRWKIK AVPKVLDKAK ALYEQHGETI ETLADGGADI ESLRKQFPDF EEWDGAYYEA AEQDLPLLAE HILSNRAAFA HIGQA // ID Q5F7R9_NEIG1 Unreviewed; 104 AA. AC Q5F7R9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Putative phage associated protein {ECO:0000313|EMBL:AAW89768.1}; GN ORFNames=NGO_1101 {ECO:0000313|EMBL:AAW89768.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89768.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89768.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89768; AAW89768; NGO_1101. DR PATRIC; 20335456; VBINeiGon24812_1294. DR HOGENOM; HOG000071254; -. DR OMA; LRNYLEC; -. DR OrthoDB; EOG6W19MM; -. DR BioCyc; NGON242231:GI2G-1013-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 104 AA; 11528 MW; 186A72D93F460F12 CRC64; MSEITKFTKL LVEHGKIYRV TRGIFKPAIG FGETRPVSVS VLDSGMGVLE IGDTVLHLNP QEMRSLGALM SGFGQQFSSI QMGREFSVLR NYLECSAKNG RLDF // ID Q5F5Y4_NEIG1 Unreviewed; 101 AA. AC Q5F5Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Pseudouridine synthase {ECO:0000313|EMBL:AAW90403.1}; GN ORFNames=NGO_1784 {ECO:0000313|EMBL:AAW90403.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90403.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90403.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90403; AAW90403; NGO_1784. DR PATRIC; 20337212; VBINeiGon24812_2142. DR OrthoDB; EOG6GJBWF; -. DR BioCyc; NGON242231:GI2G-1682-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 101 AA; 10931 MW; 7EBD3448F29B8850 CRC64; MKIRRDARSG EPCAEGSDKE GYKDRCGGLP AAFRTLRSEK WAPASSCYRD ACVFGRFAFG AWGSAAVLLP RRNGKINSNL TTFCACRLGT GAGKMLCGVR F // ID Q5F876_NEIG1 Unreviewed; 477 AA. AC Q5F876; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 85. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN ORFNames=NGO_0915 {ECO:0000313|EMBL:AAW89611.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89611.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89611.1; -; Genomic_DNA. DR RefSeq; WP_002217382.1; NC_002946.2. DR RefSeq; YP_208023.1; NC_002946.2. DR ProteinModelPortal; Q5F876; -. DR SMR; Q5F876; 2-476. DR PRIDE; Q5F876; -. DR EnsemblBacteria; AAW89611; AAW89611; NGO_0915. DR GeneID; 3281748; -. DR KEGG; ngo:NGO0915; -. DR PATRIC; 20335013; VBINeiGon24812_1076. DR HOGENOM; HOG000276708; -. DR KO; K00382; -. DR OMA; VYTQPEI; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; NGON242231:GI2G-853-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW89611.1}; KW Redox-active center {ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 50079 MW; 587D727B2E651C1C CRC64; MSQYDVVVIG AGPGGYVAAI RAAQLGFKTA CVDAGVNKAG NAPALGGTCL NVGCIPSKAL LQSSEHFHAA QHDFAEHGIT 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 Q5F8B7_NEIG1 Unreviewed; 214 AA. AC Q5F8B7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89570.1}; GN ORFNames=NGO_0869 {ECO:0000313|EMBL:AAW89570.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89570.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89570.1; -; Genomic_DNA. DR RefSeq; WP_003688528.1; NC_002946.2. DR RefSeq; YP_207982.1; NC_002946.2. DR EnsemblBacteria; AAW89570; AAW89570; NGO_0869. DR GeneID; 3282191; -. DR KEGG; ngo:NGO0869; -. DR PATRIC; 20334910; VBINeiGon24812_1025. DR HOGENOM; HOG000105368; -. DR KO; K03975; -. DR OMA; YLDKTHE; -. DR OrthoDB; EOG6D2KZK; -. DR BioCyc; NGON242231:GI2G-812-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 23469 MW; 91C87775C6FD402D CRC64; MLASVIDFIL HIDQHLLSLS AQYGVWIYAI LFLIVFCETG LIVTPFLPGD SLLFAAGGIA ALGGMDIHLM VALLSLAAIL GDALNFTVGK YFGGRLFANP DSKIFRCEYL GKTRRFYEKH GGKTIIIARF VPIVRTFAPF VAGMGKMHYA KFIRYNIIGG LLWVILFSYA GYFFANFPVV KNNLGLVMGG IIIVSVLPGI IEIARAKLAA KSER // ID Q5F6X8_NEIG1 Unreviewed; 258 AA. AC Q5F6X8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000256|HAMAP-Rule:MF_00427}; DE Short=Na(+)-NQR subunit C {ECO:0000256|HAMAP-Rule:MF_00427}; DE Short=Na(+)-translocating NQR subunit C {ECO:0000256|HAMAP-Rule:MF_00427}; DE EC=1.6.5.8 {ECO:0000256|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR complex subunit C {ECO:0000256|HAMAP-Rule:MF_00427}; DE AltName: Full=NQR-1 subunit C {ECO:0000256|HAMAP-Rule:MF_00427}; GN Name=nqrC {ECO:0000256|HAMAP-Rule:MF_00427}; GN ORFNames=NGO_1415 {ECO:0000313|EMBL:AAW90059.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90059.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00427}. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) + CC ubiquinol + n Na(+)(Out). {ECO:0000256|HAMAP-Rule:MF_00427}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00427}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE CC and NqrF. {ECO:0000256|HAMAP-Rule:MF_00427}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00427}; Single-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00427}. CC -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00427}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90059.1; -; Genomic_DNA. DR RefSeq; WP_003689271.1; NC_002946.2. DR RefSeq; YP_208471.1; NC_002946.2. DR DNASU; 3281782; -. DR EnsemblBacteria; AAW90059; AAW90059; NGO_1415. DR GeneID; 3281782; -. DR KEGG; ngo:NGO1415; -. DR PATRIC; 20336237; VBINeiGon24812_1667. DR HOGENOM; HOG000273678; -. DR KO; K00348; -. DR OMA; IKGITYY; -. DR OrthoDB; EOG6F2981; -. DR BioCyc; NGON242231:GI2G-1324-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00427}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00427}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00427}; KW FMN {ECO:0000256|HAMAP-Rule:MF_00427}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00427}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00427}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00427}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00427}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00427}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Sodium {ECO:0000256|HAMAP-Rule:MF_00427}; KW Sodium transport {ECO:0000256|HAMAP-Rule:MF_00427}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00427}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00427}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00427}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00427}. FT TRANSMEM 14 34 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00427}. FT DOMAIN 146 243 FMN_bind. {ECO:0000259|SMART:SM00900}. FT MOD_RES 226 226 FMN phosphoryl serine. FT {ECO:0000256|HAMAP-Rule:MF_00427}. SQ SEQUENCE 258 AA; 27716 MW; C7FC556F2B8F2451 CRC64; MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY ILSVAGLMDK DTDIGKTFAE RIEQRVVDLA TGEYVKDAPK DFSARIAGKD PAQSIRIKPE DDLAGIKSRA KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV MYGFVAIRPD GNTINGITYY EQGETPGLGG EIGNPLWQQK FVGKKLFDGQ GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF GENGYIPYLN KLKSAGVQ // ID Q5F5D4_NEIG1 Unreviewed; 114 AA. AC Q5F5D4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90603.1}; GN ORFNames=NGO_1995 {ECO:0000313|EMBL:AAW90603.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90603.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90603.1; -; Genomic_DNA. DR RefSeq; WP_003686892.1; NC_002946.2. DR RefSeq; YP_209015.1; NC_002946.2. DR EnsemblBacteria; AAW90603; AAW90603; NGO_1995. DR GeneID; 3282629; -. DR KEGG; ngo:NGO1995; -. DR PATRIC; 20337759; VBINeiGon24812_2406. DR HOGENOM; HOG000218713; -. DR OMA; GWKGWRL; -. DR OrthoDB; EOG6D8BCD; -. DR BioCyc; NGON242231:GI2G-1893-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 85 109 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 114 AA; 12664 MW; 5F8746A150C3DBCF CRC64; MLPNKVLGKY DWNVDGKTGI GAAWVVAAFI LPILVWAVFM LSRMQGWLAP TKANPIWALV WLLICLPCLL IAAKCLGWKG WRRVVNIFVC LTVCAILSVP ASLLIAFTLR DLLK // ID Q5F8T4_NEIG1 Unreviewed; 423 AA. AC Q5F8T4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 69. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_0676 {ECO:0000313|EMBL:AAW89403.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89403.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89403.1; -; Genomic_DNA. DR RefSeq; WP_003688809.1; NC_002946.2. DR RefSeq; YP_207815.1; NC_002946.2. DR ProteinModelPortal; Q5F8T4; -. DR REBASE; 10857; M.NgoAXV. DR EnsemblBacteria; AAW89403; AAW89403; NGO_0676. DR GeneID; 3282000; -. DR KEGG; ngo:NGO0676; -. DR PATRIC; 20334450; VBINeiGon24812_0797. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; FITADNE; -. DR OrthoDB; EOG6PZXGV; -. DR BioCyc; NGON242231:GI2G-643-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW89403.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW89403.1}. FT DOMAIN 4 420 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 423 AA; 47560 MW; 1D2EF5CD27B5CAAC CRC64; MQQIKFIDLF SGMSGIRKGF EQACRKQSVA CECVFTSEIK PAALEVLKQN YPDEVPYGDI TKIETGDIPD FDILLAGFPC QAFSFAGKRL GFEDTRGTLF FDVARILKAK KPKGFILENV EGLVTHDRKD STQKIGRTLT VILETLEALG YYVSWKVLNA KDFGIPQNRK RIYLTGSLKS KPDLSFETSP SPKLKNILES GLPTESSPFI KKLLKKFPPS ELYGKSVKDK RGGKNNIHSW DIELKGAVTE EEKQLLNILL KERRKKKWAS EIGIDWMDGM PLTKAQISTF YKHPDLQNIL DSLTDKGYLV LEHPKQKIGG QRIKDESLPK GYNIVSGKKS FEINKILDPN DVAPTLVAMD MEHLFVVDNG GLRTLTGKEG LRLFGYPDDY SFDIPKKDRC DLLGNTVAVP VIKAVSERLL HTL // ID Q5F613_NEIG1 Unreviewed; 206 AA. AC Q5F613; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90374.1}; GN ORFNames=NGO_1753 {ECO:0000313|EMBL:AAW90374.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90374.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90374.1; -; Genomic_DNA. DR RefSeq; WP_003696151.1; NC_002946.2. DR RefSeq; YP_208786.1; NC_002946.2. DR EnsemblBacteria; AAW90374; AAW90374; NGO_1753. DR GeneID; 3281423; -. DR KEGG; ngo:NGO1753; -. DR PATRIC; 20337112; VBINeiGon24812_2096. DR HOGENOM; HOG000218643; -. DR OMA; LAPYFGN; -. DR OrthoDB; EOG62NX0Q; -. DR BioCyc; NGON242231:GI2G-1649-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 22206 MW; CF4530B11BB5D7B7 CRC64; MNSTASKTLK GLSLVFFASG FCALIYQVSW QRLLFSHIGI DLSSITVIIS VFMVGLGVGA YFGGRIADRF PSSIIPLFCI AEVSIGLFGL VSKGLISGLG HLLVEADLPI IAAANFLLLL LPTFMMGATL PLLTCFFNRK IHNVGESIGT LYFFNTLGAA LGSLAAAEFF YVFFTLSQTI ALTACLNLLI AASVWLRYRK DGYGEH // ID Q5FA35_NEIG1 Unreviewed; 419 AA. AC Q5FA35; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 82. 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:AAW88952.1}; GN ORFNames=NGO_0199 {ECO:0000313|EMBL:AAW88952.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88952.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88952.1; -; Genomic_DNA. DR RefSeq; WP_003687508.1; NC_002946.2. DR RefSeq; YP_207364.1; NC_002946.2. DR ProteinModelPortal; Q5FA35; -. DR SMR; Q5FA35; 1-417. DR EnsemblBacteria; AAW88952; AAW88952; NGO_0199. DR GeneID; 3281719; -. DR KEGG; ngo:NGO0199; -. DR PATRIC; 20333329; VBINeiGon24812_0247. DR HOGENOM; HOG000076952; -. DR KO; K03628; -. DR OMA; FLRAPDY; -. DR OrthoDB; EOG6N681W; -. DR BioCyc; NGON242231:GI2G-182-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 47319 MW; 744CBAE741B4AC23 CRC64; MHVSELQTLH ISKLLELAEE HGIENANRFR KQDLVFAIVR QMMKKGEGFT CSGTLEILPD GFGFLRSADT SYLAGPDDIY VSPTQIRRFN LHTGDTIEGS VRVPKDNERY FALVRLDSIN GDHPEVCRHK ILFENLTPLF PTEQLKLERD LKSEENLTGR AIDLISPIGK GQRALLVAPP KIGKTVMLQN IAHAVTANYP EVELIVLLID ERPEEVTEMS RSVRGEVVSS TFDEPAQRHV QVAEMVLEKA KRMVEHKKDV VILLDSITRL ARAYNTVVPA SGKILTGGVD ANALHRPKRF FGAARNVEEG GSLTIIATAL VETGSRMDDV IYEEFKGTGN MELHLDRRMA EKRLFPAINI NKSGTRREEL LVPNDQLQRM WLLRKFLHPM DEIEATEFLN GKIKASKNND DFFELMRGK // ID Q5F7Q1_NEIG1 Unreviewed; 72 AA. AC Q5F7Q1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89786.1}; GN ORFNames=NGO_1119 {ECO:0000313|EMBL:AAW89786.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89786.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89786.1; -; Genomic_DNA. DR RefSeq; WP_003691731.1; NC_002946.2. DR RefSeq; YP_208198.1; NC_002946.2. DR EnsemblBacteria; AAW89786; AAW89786; NGO_1119. DR GeneID; 3282394; -. DR KEGG; ngo:NGO1119; -. DR PATRIC; 20335492; VBINeiGon24812_1312. DR OrthoDB; EOG6KHG5F; -. DR BioCyc; NGON242231:GI2G-1031-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 72 AA; 7578 MW; 2088BCBDE08A2B4C CRC64; MANSNSGHSK KLRAATAAAA TKAKLASGEY RQFSVQGRAE DVELILAAVE KAGGSRVQAL AKICRRYLEG LS // ID Q5F736_NEIG1 Unreviewed; 418 AA. AC Q5F736; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 61. DE SubName: Full=3-oxoacyl-ACP synthase {ECO:0000313|EMBL:AAW90001.2}; GN ORFNames=NGO_1352 {ECO:0000313|EMBL:AAW90001.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90001.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90001.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F736; -. DR EnsemblBacteria; AAW90001; AAW90001; NGO_1352. DR PATRIC; 20336083; VBINeiGon24812_1591. DR HOGENOM; HOG000071325; -. DR OMA; HTADANI; -. DR OrthoDB; EOG6DG2SR; -. DR BioCyc; NGON242231:GI2G-1265-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF00109; ketoacyl-synt; 1. DR SUPFAM; SSF53901; SSF53901; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 157 Ketoacyl_synth_N. FT {ECO:0000259|Pfam:PF00109}. SQ SEQUENCE 418 AA; 46002 MW; 4200D9EFD68BA2C7 CRC64; MLNTRRVAVT GIGGITAFGR DWQSIQAAFK AEKNAVKYMD WRERFPELEA QLDAPIEDYA PPKHWTRKRL RSMGRVSYLC VDAAEQALMD AGLLGDESIT DGRMGVACGS SGGGTKDIGD VGELLLTGTS RNFGANTYVR MMPHTADANI GIFFGLTRTH HPDIERVFFG QPRHRLCLRG HQIRSDRYDA GGRRRRILPV RSVCFRLALC RQPPQRRTGR DPASIRREPR RAGHRRKGAG IFVLEELEHA KRRGAKIYAE LVGYGANSDG INIGEGAAVF IMTRDADFSG GMQLLGYGAS SDAYHISTPR PDAKAQSSPF RRHCSTPALR PKTSAGLICT APGRTTTTVW KAAPLQRFSA TIRPARPPSR KPDTRWARRA QSKPRSRGAL PTGKAIPKGN FRPGFGTGRT TPTCPPLT // ID Q5F952_NEIG1 Unreviewed; 230 AA. AC Q5F952; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Molecular chaperone DnaJ {ECO:0000313|EMBL:AAW89285.1}; GN ORFNames=NGO_0551 {ECO:0000313|EMBL:AAW89285.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89285.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89285.1; -; Genomic_DNA. DR RefSeq; WP_010357715.1; NC_002946.2. DR RefSeq; YP_207697.1; NC_002946.2. DR ProteinModelPortal; Q5F952; -. DR SMR; Q5F952; 2-67. DR EnsemblBacteria; AAW89285; AAW89285; NGO_0551. DR GeneID; 3282125; -. DR KEGG; ngo:NGO0551; -. DR PATRIC; 20334154; VBINeiGon24812_0649. DR HOGENOM; HOG000218979; -. DR OMA; SKRTQYD; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; NGON242231:GI2G-525-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 156 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 209 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 4 69 J. {ECO:0000259|PROSITE:PS50076}. SQ SEQUENCE 230 AA; 26964 MW; 5D85178A665257D8 CRC64; MDKDLYAVLG VSPQAGADEI KRAYRKLAMK YHPDRNPGNL QAEEKFKEIQ RAYDTLSDLS KRTQYDASFR RHEERGRQEE AFRREQARRE QFYGEQMRRE QAFRREFERQ ASRSRHAYEP SGSGSGRNYI LAAYILFGLG AIIQFMPIVG VILAYMKRNS LDSIVYAAHT EYLIKTFWRT FWLYLLGALT ARFGIGVLVI IATTVWYFYR IIAGFIRFND GRAVAPEKWI // ID Q5F5N3_NEIG1 Unreviewed; 49 AA. AC Q5F5N3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90504.1}; GN ORFNames=NGO_1887 {ECO:0000313|EMBL:AAW90504.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90504.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90504.1; -; Genomic_DNA. DR RefSeq; WP_010951364.1; NC_002946.2. DR RefSeq; YP_208916.1; NC_002946.2. DR EnsemblBacteria; AAW90504; AAW90504; NGO_1887. DR GeneID; 3282332; -. DR KEGG; ngo:NGO1887; -. DR PATRIC; 20337474; VBINeiGon24812_2268. DR HOGENOM; HOG000027830; -. DR OrthoDB; EOG6GR3GF; -. DR BioCyc; NGON242231:GI2G-1788-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5296 MW; 9C2F8C3F4D9D64C8 CRC64; MPSETLLSVS DGILTNTVRR RKTAGFSCVS YADVSTHRTA HKASPYVPS // ID Q5F8W1_NEIG1 Unreviewed; 66 AA. AC Q5F8W1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89376.1}; GN ORFNames=NGO_0649 {ECO:0000313|EMBL:AAW89376.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89376.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89376.1; -; Genomic_DNA. DR RefSeq; WP_003688861.1; NC_002946.2. DR RefSeq; YP_207788.1; NC_002946.2. DR EnsemblBacteria; AAW89376; AAW89376; NGO_0649. DR GeneID; 3281804; -. DR KEGG; ngo:NGO0649; -. DR PATRIC; 20334386; VBINeiGon24812_0765. DR HOGENOM; HOG000027833; -. DR OMA; TAFCFPA; -. DR OrthoDB; EOG66F0C3; -. DR BioCyc; NGON242231:GI2G-616-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 7348 MW; F2000511F1DD2A56 CRC64; MPSEGLSDGI FVFVRGIVML PFDFQTAFCF QAFDVGMAIL IYVRWQGGIV IPPLGFQTAS YRTVKP // ID Q5F6L5_NEIG1 Unreviewed; 126 AA. AC Q5F6L5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Sel1 domain-containing protein repeat-containing protein {ECO:0000313|EMBL:AAW90172.1}; GN ORFNames=NGO_1536 {ECO:0000313|EMBL:AAW90172.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90172.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90172.1; -; Genomic_DNA. DR RefSeq; WP_003689448.1; NC_002946.2. DR RefSeq; YP_208584.1; NC_002946.2. DR ProteinModelPortal; Q5F6L5; -. DR EnsemblBacteria; AAW90172; AAW90172; NGO_1536. DR GeneID; 3281499; -. DR KEGG; ngo:NGO1536; -. DR PATRIC; 20336568; VBINeiGon24812_1832. DR HOGENOM; HOG000003584; -. DR OMA; AMYAEGQ; -. DR OrthoDB; EOG6HJ27Z; -. DR BioCyc; NGON242231:GI2G-1438-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom. DR Pfam; PF08238; Sel1; 2. DR SMART; SM00671; SEL1; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 126 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256033. SQ SEQUENCE 126 AA; 13981 MW; ACFD6CC683D010A6 CRC64; MKQTVKWLAA ALIALGLNQA VWAGDVSDFR ENLQAAEQGN AAAQFNLGVM YENGQGVRQD YVQAVQWYRK ASEQGDAQAQ YNLGLMYYDG RGVRQDLALA QQWLGKACQN GDQNSCDNDQ RLKAGY // ID Q5F8R6_NEIG1 Unreviewed; 1001 AA. AC Q5F8R6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 77. DE SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:AAW89421.2}; GN ORFNames=NGO_0697 {ECO:0000313|EMBL:AAW89421.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89421.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89421.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8R6; -. DR REBASE; 10858; NgoAXVIIP. DR EnsemblBacteria; AAW89421; AAW89421; NGO_0697. DR PATRIC; 20334506; VBINeiGon24812_0825. DR HOGENOM; HOG000249630; -. DR OMA; DEVHRSY; -. DR OrthoDB; EOG60GRR2; -. DR BioCyc; NGON242231:GI2G-661-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. 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 Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89421.2}; KW Hydrolase {ECO:0000313|EMBL:AAW89421.2}; KW Nuclease {ECO:0000313|EMBL:AAW89421.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 287 502 Helicase ATP-binding. FT {ECO:0000259|SMART:SM00487}. FT COILED 697 724 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1001 AA; 115326 MW; 379B654ED08603ED CRC64; MSQTHNENSR VKIPAVLHLM RLGYDYLSLK NANWDRQTNI FPEIFVDSLC RINPDLPPDD ARRLLADIRL ELDNEDLGQK FYERLTNQSG GKKLIDFQNF DNNSFHVVTE LPCINGDEAF RPDIALLVNG MPLVFIEVKK PNNKGGIGEE RERMGKRAKN PKFRRFINIT QFMIFSNNME YDDGATEPAQ GAFYASSACG KPVFNYFREE HKLNLTELLD TLSDDLENNV LQDNNLPVIK HSPEFISNKS PDTPTNRILT SLLCRERLSF LLQHGLTYVK ASQGLVQKHI MRYPQLFATL AIEKHLANGG KKGVIWHTQG SGKTALAYYN TRYLTHYYAK QGIVPKFYFI VDRLDLLKQA QREFTARDLV VHTIDSREAF AADIKSAQTL HNHAGKAEIT VVNIQKFQDD PDVVARNDYD LAIQRVYFLD EVHRSYNPKG SFLANLNQSD VNAVKIGLTG TPLIGVTAGN VNTRELFGDY IHKYYYNASI ADGYTLRLIR EEIGSRYKAQ LQEALAQLEI EKGSFDRKEI YAHPHFVHPM LDYILDDFAK FRKTNQDESL GAMVVCDSAE QARQLFEHFQ TASDHNFTAA LILHDVGTKE ERDQWVKDFK AGKIDILFVY NMLLTGFDAP RLKKLYLGRL IKAHNLLQTL TRVNRTYKSY RYGYVVDFAD IEREFDKTNR AYWDELSNEL GDEIGSYSQL FKTAEEIEQE IADIKNALFD FDTENAEEFC SQISQIEDKK QLLALKKALQ TAKELYNILR LQGSHEFLAH LDFDKLNLLY RETAARLDTL NLAEKLQQGD TAHLLNEALE DVYFQFVKIG EAELKLADDL KDIMRKVREG LAGNFDQDDP EYISLREELE RIFKKKNLAE VGQEEMQANI ATLQTVYTKI KEPNRQNDLL RHKYGGDAKY ARIHKRLMEN AALYGDKLKV FNALSGVKTD ADQKVLDMEQ ILDNQNYFEK QMQGIVLKRF RTEQQFPVQP ADIQAINRLL VREYLKESGR I // ID Q5FA97_NEIG1 Unreviewed; 140 AA. AC Q5FA97; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000313|EMBL:AAW88890.1}; GN ORFNames=NGO_0131 {ECO:0000313|EMBL:AAW88890.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88890.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88890.1; -; Genomic_DNA. DR RefSeq; WP_003704886.1; NC_002946.2. DR RefSeq; YP_207302.1; NC_002946.2. DR ProteinModelPortal; Q5FA97; -. DR EnsemblBacteria; AAW88890; AAW88890; NGO_0131. DR GeneID; 3281264; -. DR KEGG; ngo:NGO0131; -. DR PATRIC; 20333169; VBINeiGon24812_0168. DR HOGENOM; HOG000225068; -. DR KO; K01737; -. DR OMA; MVVWIFE; -. DR OrthoDB; EOG6FFSCJ; -. DR BioCyc; NGON242231:GI2G-119-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 15749 MW; A2DF3917711CF603 CRC64; MKITKIFTFD SSHMLDGHDG KCQNLHGHTY KLEITVSDGI VRGGPKDGMV MDFTDLKAIV KQHITDPFDH AFIYHGGNGR ESQIAALLEG WNMKTLRLPC RTTAENMAVE MYCRLKNAGL NVCRVKLWET PTSCAEYEGE // ID Q5F658_NEIG1 Unreviewed; 716 AA. AC Q5F658; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=ATP-dependent DNA helicase DinG {ECO:0000313|EMBL:AAW90329.1}; GN ORFNames=NGO_1708 {ECO:0000313|EMBL:AAW90329.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90329.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90329.1; -; Genomic_DNA. DR RefSeq; WP_003689889.1; NC_002946.2. DR RefSeq; YP_208741.1; NC_002946.2. DR ProteinModelPortal; Q5F658; -. DR EnsemblBacteria; AAW90329; AAW90329; NGO_1708. DR GeneID; 3281179; -. DR KEGG; ngo:NGO1708; -. DR PATRIC; 20337008; VBINeiGon24812_2044. DR HOGENOM; HOG000242573; -. DR KO; K03722; -. DR OMA; MRALNSF; -. DR OrthoDB; EOG6742WF; -. DR BioCyc; NGON242231:GI2G-1604-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA 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; IPR010614; DEAD_2. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06733; DEAD_2; 1. 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:AAW90329.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000313|EMBL:AAW90329.1}; KW Hydrolase {ECO:0000313|EMBL:AAW90329.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW90329.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 79085 MW; B5298864EC5C5D74 CRC64; MLTDLEKNAI RDHYQNIGKN LPGFRPRASQ REMIAAVANA FSRTLTREEG GEPPKREGES IAVIEGPTGV GKSLAYLLAG GIMAQTRGKR LIVSSATVAL QEQLVDRDLP FLVEKSGLEL TFALAKGRGR YLCPYKLYQL TQSNAQQNLL GFEAPAVLWD SKPKPEELKL LRDIADEFSA RRFNGDRDAW PEKIDDAIWL KVTNDRHGCL KAACPNRPEC PFYLARDMLE TVDVVVANHD LLLADISMGG GVILPAPENS FYCIDEAHHL PKKALSRFAA EHSWNIAVWT LEKLPQLTGK IAALTDKAEL ANLADEAAAS LLDSLHEWQF HLAEEPSLSM GLSENDRRTN SEPTWLWEDG KIPEGLETTV SNTAIAARSL LKHVVGLNDA LSAARREKEQ DGALIDRLTG EFGLFIARIE QISAVWDLLS TVSIEGEEPL AKWIARRADD KNDYIFNASP ISSASHLANS LWRRAAGAVL TSATLQSLGS FNLILRQTGL LWLPETTTLA LKSPFDFEKQ GELYIPSIYA SPKDPEAHTA AVIEWLPKLI SPTEAIGTLV LFSSRKQMQD VALHLPGDYL PLLLVQGELP KAVLLQKHHQ AIEEGKASII FGLDSFAEGL DLPGTACVQV IIAKLPFAMP DNPIEKTQNR WIEQRGGNPF IEITVPEAGI KLIQAVGRLI RTEQDYGRVT ILDNRIKTQR YGQQLLAGLP PFKRIG // ID Q5F9A5_NEIG1 Unreviewed; 149 AA. AC Q5F9A5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89232.1}; GN ORFNames=NGO_0494 {ECO:0000313|EMBL:AAW89232.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89232.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89232.1; -; Genomic_DNA. DR RefSeq; WP_003689093.1; NC_002946.2. DR RefSeq; YP_207644.1; NC_002946.2. DR EnsemblBacteria; AAW89232; AAW89232; NGO_0494. DR GeneID; 3282938; -. DR KEGG; ngo:NGO0494; -. DR PATRIC; 20334028; VBINeiGon24812_0586. DR HOGENOM; HOG000005016; -. DR OMA; KWALARM; -. DR OrthoDB; EOG6RC3QT; -. DR BioCyc; NGON242231:GI2G-472-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 149 AA; 16844 MW; 5F165ABFEE09188A CRC64; MSGTKRKLGR PTDYTKDMAD KICEKIANGR SLRSICAEDG VPPMKTIYRW LEANEEFRHQ YARAREKQAD YFAEEIIEIA DSAQAESAAV SKAKLQIDAR KWAASKIAPK KYGDKSELDV KSGDGSMRAA VRLDAEEYRK IAEDVLRRV // ID Q5FAF6_NEIG1 Unreviewed; 306 AA. AC Q5FAF6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 67. 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 ORFNames=NGO_0068 {ECO:0000313|EMBL:AAW88831.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88831.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88831.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FAF6; -. DR DNASU; 3282316; -. DR EnsemblBacteria; AAW88831; AAW88831; NGO_0068. DR PATRIC; 20332998; VBINeiGon24812_0083. DR HOGENOM; HOG000006845; -. DR OMA; IHITHPH; -. DR OrthoDB; EOG6QP0ZV; -. DR BioCyc; NGON242231:GI2G-60-MONOMER; -. DR UniPathway; UPA00276; UER00406. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000535; 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:UP000000535}; 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:AAW88831.2}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004491}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR004491, KW ECO:0000313|EMBL:AAW88831.2}. FT DOMAIN 184 305 Flavokinase. {ECO:0000259|SMART:SM00904}. SQ SEQUENCE 306 AA; 34122 MW; 1B55CA61C635C470 CRC64; MKIRPGRHNA PDFPHGAAVT IGNFDGVHLG HKHILQKLRL EADARGLPVV AVVFEPQPKE FFALRTGKTP PCRISPLRTK LELLEGTGCV DAAWVLRFDR NFSEISAQAF IDRLLRQTLN TRYLLVGDDF RFGAGREGCF ELLAQQPDMQ TERTPSVIVE DIRTSSTAVR QALSDGNLAY AKKLLGHDYV LGGRVVHGRK LGRTLNAPTA NIRLPGHRYA LGGVFVVEAD GAFGTRRGVA SFGFNPTVDG GCSQKLEVHL FDFQGDLYGQ RLNVRFLHKL RDEEKFDGME ELKRRIEADM EAAKCW // ID Q5F6S4_NEIG1 Unreviewed; 192 AA. AC Q5F6S4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 66. DE SubName: Full=NADPH quinone reductase MdaB {ECO:0000313|EMBL:AAW90113.1}; GN ORFNames=NGO_1473 {ECO:0000313|EMBL:AAW90113.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90113.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90113.1; -; Genomic_DNA. DR RefSeq; WP_003693637.1; NC_002946.2. DR RefSeq; YP_208525.1; NC_002946.2. DR ProteinModelPortal; Q5F6S4; -. DR SMR; Q5F6S4; 1-192. DR EnsemblBacteria; AAW90113; AAW90113; NGO_1473. DR GeneID; 3281639; -. DR KEGG; ngo:NGO1473; -. DR PATRIC; 20336381; VBINeiGon24812_1739. DR HOGENOM; HOG000063966; -. DR KO; K03923; -. DR OMA; PTFICND; -. DR OrthoDB; EOG6ZWJFM; -. DR BioCyc; NGON242231:GI2G-1378-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 187 Flavodoxin_2. {ECO:0000259|Pfam:PF02525}. SQ SEQUENCE 192 AA; 21786 MW; 3E8F12D81A670893 CRC64; MNILLLDGGK AFGHSHGGLN HTLHKKAKEV LTALGHNVQE TVIDAGYDVE AEIEKFVWMD AVIWQMPGWW MHEPWTVKKY MDEVFTGGHG KLYQSDGRHR VNPTEGYGTG GLLQGKKHML SLTWNAPIEA FTREGDFFEG KGVDVLYMHF HKANEFIGLS RLPTFLCNDV VKNPQVEKYL ADYQAHLEKV FG // ID Q5F867_NEIG1 Unreviewed; 69 AA. AC Q5F867; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89620.1}; GN ORFNames=NGO_0924 {ECO:0000313|EMBL:AAW89620.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89620.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89620.1; -; Genomic_DNA. DR RefSeq; WP_003688391.1; NC_002946.2. DR RefSeq; YP_208032.1; NC_002946.2. DR EnsemblBacteria; AAW89620; AAW89620; NGO_0924. DR GeneID; 3282877; -. DR KEGG; ngo:NGO0924; -. DR PATRIC; 20335031; VBINeiGon24812_1085. DR HOGENOM; HOG000027912; -. DR OMA; WGRMLIP; -. DR OrthoDB; EOG69GZRK; -. DR BioCyc; NGON242231:GI2G-862-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 69 AA; 8083 MW; 478211FFDA233840 CRC64; MPPEIFFRRH FIFGDGVGGR MLIPCREGSG KTKNLSFNLL FPRVFVKIYQ FVFKIHCSKW DKTGKLTLM // ID Q5F947_NEIG1 Unreviewed; 465 AA. AC Q5F947; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 64. 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:AAW89290.1}; GN ORFNames=NGO_0556 {ECO:0000313|EMBL:AAW89290.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89290.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89290.1; -; Genomic_DNA. DR RefSeq; WP_010951082.1; NC_002946.2. DR RefSeq; YP_207702.1; NC_002946.2. DR ProteinModelPortal; Q5F947; -. DR SMR; Q5F947; 3-456. DR EnsemblBacteria; AAW89290; AAW89290; NGO_0556. DR GeneID; 3282149; -. DR KEGG; ngo:NGO0556; -. DR PATRIC; 20334166; VBINeiGon24812_0655. DR HOGENOM; HOG000061737; -. DR KO; K01744; -. DR OMA; EICENYV; -. DR OrthoDB; EOG6V1M4M; -. DR BioCyc; NGON242231:GI2G-530-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000256|SAAS:SAAS00429438, KW ECO:0000313|EMBL:AAW89290.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 12 343 Lyase_1. {ECO:0000259|Pfam:PF00206}. FT DOMAIN 409 461 FumaraseC_C. {ECO:0000259|Pfam:PF10415}. SQ SEQUENCE 465 AA; 50692 MW; B8146C281174E07F CRC64; MTVRIEHDLL GDREIPAEVY WGIHTLRAIE NFKISTQKIS DVPQFVRSIV MVKKATAQAN GELGAVKPEI AAAIEKACDE VLLNNRCLDQ FPSDVYQGGA GTSVNMNTNE VIANLALEAL GYEKGRYDIV NPMDHVNASQ STNDAYPTGF RLAVYYSIGE LLDKLTVLKN AFAAKAEAFK DVLKMGRTQL QDAVPMTAGQ EFQSFQVLLE EEILNLDRTR QLLLEVNLGA TAIGTGVNTP KGYAELVVKK LSEVSGLPCK LTENLIEATS DCGAYVMVHG ALKRTAVKLS KICNDLRLLS SGPRAGLKEI NLPELQAGSS IMPAKVNPVI PEVVNQVCFK VIGNDTTITF AAESGQLQLN VMEPVIAQCM FETISLLGNA AVNLSDKCVK GITVNREICE RYVFNSIGLV TYLNPYIGHR NGDLVGKICA QTGKGVREVV LERGLLSEEE INRILSPENL MNPHL // ID Q5F7C8_NEIG1 Unreviewed; 280 AA. AC Q5F7C8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 76. DE SubName: Full=AraC family transcriptional regulator {ECO:0000313|EMBL:AAW89909.1}; GN ORFNames=NGO_1250 {ECO:0000313|EMBL:AAW89909.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89909.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89909.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F7C8; -. DR EnsemblBacteria; AAW89909; AAW89909; NGO_1250. DR PATRIC; 20335833; VBINeiGon24812_1471. DR HOGENOM; HOG000136816; -. DR OMA; EATFHIV; -. DR OrthoDB; EOG690MBW; -. DR BioCyc; NGON242231:GI2G-1167-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 175 276 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 280 AA; 31151 MW; 7E4C6BAF063602B9 CRC64; MCSAFWADND ETLQREGLVH IVTAGSGYLC IDGETSPRPV GTGDIVFFPR GLGHVLSHDG KYGESLQPDI RQNGTFMVKQ CGNGLDMSLF CARFRYDTHA DLMNGLPETV FLNIAHPSLQ YVVSMLQLES EKPLTGTVSV VNALPSVLLV LILRAYLEQD KDVELSGVLK GWQDKRLGHL IQKVIDKPED EWNIDKMVAA ANMSRAQLMR RFKSQVGLSP HAFVNHIRLQ KGALLLKKTP DSVLEVALSV GFQSETHFGK AFKRQYHVSP GQYRKEGGQK // ID Q5F8S5_NEIG1 Unreviewed; 818 AA. AC Q5F8S5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 93. DE SubName: Full=ATPase P {ECO:0000313|EMBL:AAW89412.1}; GN ORFNames=NGO_0685 {ECO:0000313|EMBL:AAW89412.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89412.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89412.1; -; Genomic_DNA. DR RefSeq; WP_010951108.1; NC_002946.2. DR RefSeq; YP_207824.1; NC_002946.2. DR ProteinModelPortal; Q5F8S5; -. DR EnsemblBacteria; AAW89412; AAW89412; NGO_0685. DR GeneID; 3281912; -. DR KEGG; ngo:NGO0685; -. DR PATRIC; 20334468; VBINeiGon24812_0806. DR HOGENOM; HOG000250398; -. DR KO; K01533; -. DR OMA; QMNMDHD; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NGON242231:GI2G-652-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU362081}; KW Membrane {ECO:0000256|RuleBase:RU362081}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 766 782 Helical. {ECO:0000256|RuleBase:RU362081}. FT DOMAIN 92 158 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 818 AA; 88764 MW; DEC46DE6916E4E00 CRC64; MKKTCFHCGL DVPENLHLTV RYEGEDRETC CVGCQAVAQS IIDSGLGSYY KRRTADAKKT ELPPQEILDQ IRLYDLPEVQ SDFVETHNGT HEAVLMLSGI TCAACVWLIE QQLLRTDGIV RIDLNYSTHR CRVVWDDGKI RLSDILLKIR QTGYTAAPYD AQKIEAANQK ERKQYIVRLA VAGLGMMQTM MFALPTYLYG GDIEPDFLQI LHWGGFLMVL PVVFYCAVPF YQGALRDLKN RRAGMDTPIA AAIIMTFIAG IYSLATNAGQ GMYFESIAML LFFLLGGRFM EHIARRKAGD AAERLVKLIP AFCHRMPGYP AVQDVRESAV VKLQAGDIVM VKPGETIPVD GTVLEGNSAV NESMLTGESL PVAKMPSEKV TAGTLNTQSP LIIRTDRTGG GTRLSHIVRL LDRALAQKPR TAELAEQYAS SFIFGELLLA VPVFIGWTLY ADAHTALWIT VALLVITCPC ALSLATPTAL AASTGTLARE GILIGGKQAI ETLSQTTDII FDKTGTLTQG NPAVRRIELL GSMTEAQVLA VAQSLEQQSE HPLARAILNC RISGGSVPEI QVGQRLNRIG EGVGAQLTVN GETQVWALGR ASYVAEISGK EPQTEGGGSA VYLGSQSGFQ AVFYLQDPLK DSAAEAVRQL AGKNLTLHIL SGDREEAVAE TARALGIAHY RAQAMPEDKL EYVEALQKEG KKVLMIGDGI NDAPVLAQAD VSAAAVGGTD IARDGADIVL LNEDLRTVAH LLDQARRTRH IIRQNLIWAG AYNIIAVPLA VLGYVQPWIA ALGMSFSSLA VLGNALRLHK RGEMPSEQ // ID Q5F721_NEIG1 Unreviewed; 522 AA. AC Q5F721; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Aminobenzoyl-glutamate transporter {ECO:0000313|EMBL:AAW90016.1}; GN ORFNames=NGO_1368 {ECO:0000313|EMBL:AAW90016.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90016.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90016.1; -; Genomic_DNA. DR RefSeq; WP_010951251.1; NC_002946.2. DR RefSeq; YP_208428.1; NC_002946.2. DR TCDB; 2.A.68.1.2; the p-aminobenzoyl-glutamate transporter (abgt) family. DR EnsemblBacteria; AAW90016; AAW90016; NGO_1368. DR GeneID; 3281186; -. DR KEGG; ngo:NGO1368; -. DR PATRIC; 20336121; VBINeiGon24812_1609. DR HOGENOM; HOG000285565; -. DR KO; K12942; -. DR OMA; KNDRDVI; -. DR OrthoDB; EOG63586P; -. DR BioCyc; NGON242231:GI2G-1281-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 49 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; 56178 MW; 4475754BFC09AFF8 CRC64; MSQTDARRSG RFLRTVEWLG NMLPHPVTLF IIFIVLLLIA SAVGAYFGLS VPDPRPVGAK GRADDGLIHV VSLLDADGLI KILTHTVKNF TGFAPLGTVL VSLLGVGIAE KSGLISALMR LLLTKSPRKL TTFMVVFTGI LSNTASELGY VVLIPLSAVI FHSLGRHPLA GLAAAFAGVS GGYSANLFLG TIDPLLAGIT QQAAQIIHPD YVVGPEANWF FMAASTFVIA LIGYFVTEKI VEPQLGPYQS DLSQEEKDIR HSNEITPLEY KGLIWAGVVF VALSALLAWS IVPADGILRH PETGLVAGSP FLKSIVVFIF LLFALPGIVY GRITRSLRGE REVVNAMAES MSTLGLYLVI IFFAAQFVAF FNWTNIGQYI AVKGAVFLKE VGLGGSVLFI GFILICAFIN LMIGSASAQW AVTAPIFVPM LMLAGYAPEV IQAAYRIGDS VTNIITPMMS YFGLIMATVI KYKKDAGVGT LISMMLPYSA FFLIAWIALF CIWVFVLGLP VGPGTPTFYP VP // ID Q5F991_NEIG1 Unreviewed; 143 AA. AC Q5F991; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89246.1}; GN ORFNames=NGO_0508 {ECO:0000313|EMBL:AAW89246.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89246.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89246.1; -; Genomic_DNA. DR RefSeq; WP_003689064.1; NC_002946.2. DR RefSeq; YP_207658.1; NC_002946.2. DR ProteinModelPortal; Q5F991; -. DR DNASU; 3282941; -. DR EnsemblBacteria; AAW89246; AAW89246; NGO_0508. DR GeneID; 3282941; -. DR KEGG; ngo:NGO0508; -. DR PATRIC; 20334058; VBINeiGon24812_0601. DR HOGENOM; HOG000061738; -. DR OMA; LGTPYHH; -. DR OrthoDB; EOG6ZH2KH; -. DR BioCyc; NGON242231:GI2G-486-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 20 124 NLPC_P60. {ECO:0000259|Pfam:PF00877}. SQ SEQUENCE 143 AA; 15838 MW; A2D6CBFE2597D1F4 CRC64; MPSETDLRAR IVEEARSWLG TPYHHHAMVK GAGVDCAMLL VAVYGAVGLL PEGFDPRPYP QDWHLHRDCE RYLGFVTQFC RETESPQAGD IAVWRFGRSF SHGGILAGGG KVIHSYIGRG VVSDDIGQAE LIGRGVRFFT FSF // ID Q5F7Q5_NEIG1 Unreviewed; 62 AA. AC Q5F7Q5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89782.1}; GN ORFNames=NGO_1115 {ECO:0000313|EMBL:AAW89782.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89782.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89782.1; -; Genomic_DNA. DR RefSeq; WP_003689136.1; NC_002946.2. DR RefSeq; YP_208194.1; NC_002946.2. DR EnsemblBacteria; AAW89782; AAW89782; NGO_1115. DR GeneID; 3281882; -. DR KEGG; ngo:NGO1115; -. DR PATRIC; 20335484; VBINeiGon24812_1308. DR BioCyc; NGON242231:GI2G-1027-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 7183 MW; 454D79F2EA222D15 CRC64; MDEPRDLVLF LKEKMSSAAI AKEVGCSKEF INKIGNGERK NPRYQIVDSL RSLYRKNQNQ PK // ID Q5F8Y3_NEIG1 Unreviewed; 363 AA. AC Q5F8Y3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Murein transglycosylase {ECO:0000313|EMBL:AAW89354.1}; GN ORFNames=NGO_0626 {ECO:0000313|EMBL:AAW89354.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89354.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89354.1; -; Genomic_DNA. DR RefSeq; WP_003688898.1; NC_002946.2. DR RefSeq; YP_207766.1; NC_002946.2. DR ProteinModelPortal; Q5F8Y3; -. DR EnsemblBacteria; AAW89354; AAW89354; NGO_0626. DR GeneID; 3282893; -. DR KEGG; ngo:NGO0626; -. DR PATRIC; 20334336; VBINeiGon24812_0740. DR HOGENOM; HOG000257828; -. DR KO; K08305; -. DR OMA; NYRVIDA; -. DR OrthoDB; EOG6R87H7; -. DR BioCyc; NGON242231:GI2G-594-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 363 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255549. FT DOMAIN 63 355 SLT_2. {ECO:0000259|Pfam:PF13406}. SQ SEQUENCE 363 AA; 39821 MW; C025335DC2A17F92 CRC64; MEKRKILPLA ICLAALSACT AMEARTPRAN EAQAPRADEM KKESRPAFDA AAVPVSDSGF AANANVRRFV DDEVGKGDFS QAEWQDFFDK AAYKADIVKI MHRPSTSRPW YVFRTGNSGR AKFHGARRFY AENRAVIDDV AQKYGVPAEL IVAIIGIETN YGKNTGSFRV ADALATLGFD YPRRAGFFQK ELVELLKLAK EEGGDVFAFK GSYAGAMGMP QFMPSSYRKW AVDYDGDGHR DIWGNVGDVA ASVANYMKQH GWRTGGKMLV SATLAPGADV QAIIGEKTAL TRTVADLKAY GIIPGETLAD DEKAVLFKLE TAPGVFEYYL GLNNFYTVWQ YNHSRMYVTA VRDIANSLGG PGL // ID Q5F8X6_NEIG1 Unreviewed; 128 AA. AC Q5F8X6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU {ECO:0000256|RuleBase:RU362089}; GN ORFNames=NGO_0633 {ECO:0000313|EMBL:AAW89361.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89361.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89361.1; -; Genomic_DNA. DR RefSeq; WP_002213175.1; NC_002946.2. DR RefSeq; YP_207773.1; NC_002946.2. DR ProteinModelPortal; Q5F8X6; -. DR SMR; Q5F8X6; 1-125. DR EnsemblBacteria; AAW89361; AAW89361; NGO_0633. DR GeneID; 3281368; -. DR KEGG; ngo:NGO0633; -. DR PATRIC; 20334350; VBINeiGon24812_0747. DR HOGENOM; HOG000069228; -. DR KO; K04488; -. DR OMA; VMDHFTN; -. DR OrthoDB; EOG6GFGQT; -. DR BioCyc; NGON242231:GI2G-601-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 126 NifU_N. {ECO:0000259|Pfam:PF01592}. SQ SEQUENCE 128 AA; 13947 MW; 6A923D9C7BA45670 CRC64; MAYSDKVIDH YENPRNVGTF DKNDESVGTG MVGAPACGDV MRLQIKVNDE GIIEDAKFKT YGCGSAIASS SLITEWVKGK SLDDALAIKN SEIAEELELP PVKIHCSILA EDAVKAAVAD YRKRQENR // ID Q5F6K1_NEIG1 Unreviewed; 498 AA. AC Q5F6K1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 84. DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:AAW90186.1}; GN ORFNames=NGO_1550 {ECO:0000313|EMBL:AAW90186.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90186.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90186.1; -; Genomic_DNA. DR RefSeq; WP_003697442.1; NC_002946.2. DR RefSeq; YP_208598.1; NC_002946.2. DR ProteinModelPortal; Q5F6K1; -. DR EnsemblBacteria; AAW90186; AAW90186; NGO_1550. DR GeneID; 3281480; -. DR KEGG; ngo:NGO1550; -. DR PATRIC; 20336602; VBINeiGon24812_1847. DR HOGENOM; HOG000246698; -. DR KO; K07391; -. DR OMA; CRCTPDQ; -. DR OrthoDB; EOG6ZWJFW; -. DR BioCyc; NGON242231:GI2G-1454-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90186.1}; KW Protease {ECO:0000313|EMBL:AAW90186.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 212 393 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 498 AA; 53299 MW; F0D651038DA1F5C7 CRC64; MSLALVYSRA LSGMNAPLVE VEAHLANGLP HFNIVGLPDT EVKESRDRVR AAIIQSGFEF PAKKITVNLA PADLPKESGR FDLPIAIGIL AASGQVAPEK LAEYEFAGEL ALSGLLRPVR GALAMAWQGM QAKRAFVLPE ENAGQAAVMR GITVYGARSL GEVAAHLNGI EPLAQTECSV PQMPSEHGGQ PDLCDVKGQH SARLALEIAA AGGHSLLMMG PPGTGKSMLS QRLPGILPPL AEDELVEVWA LRSLLPNHQQ QLDSNRPFRS PHHGASAAAM VGGGSDPRPG EISLAHHGVL FLDELPEFDR KVLEVLREPL ENGEIHISRA ARQAVYPAKF QLVAAMNPCP CGYLGHPVKP CRCTPESVAR YRSKISGPLL DRIDLTIEVP SLSAAELMQQ EAGESSASVL ERVIAARGKQ YARQGKVNAA LSVSELDSQA CIQKEAQEAL GSLLEKLSLS ARSFHRIMRV ARTLADLAGD EEVGRSHVMK AIGFRRAL // ID Q5F8M4_NEIG1 Unreviewed; 222 AA. AC Q5F8M4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AAW89463.1}; GN ORFNames=NGO_0746 {ECO:0000313|EMBL:AAW89463.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89463.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89463.1; -; Genomic_DNA. DR RefSeq; WP_003688686.1; NC_002946.2. DR RefSeq; YP_207875.1; NC_002946.2. DR ProteinModelPortal; Q5F8M4; -. DR EnsemblBacteria; AAW89463; AAW89463; NGO_0746. DR GeneID; 3282607; -. DR KEGG; ngo:NGO0746; -. DR PATRIC; 20334632; VBINeiGon24812_0888. DR HOGENOM; HOG000016839; -. DR OMA; MVPIADG; -. DR OrthoDB; EOG6ZPT3K; -. DR BioCyc; NGON242231:GI2G-703-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89463.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89463.1}. SQ SEQUENCE 222 AA; 24383 MW; 5EAF54435BE85D32 CRC64; MTTHLSNVAP DLQNYLNAIG EPEHPVLTRL REKAGHHRMG KMAIAREQAA VLVWLAKLIR AEKYLEIGVF TGYSSTALAL ALPEHGRITA CDINVTFTDT ARQVWNEAGV AHKISLHLQP ALLTLDDLIA QGEAGSYDLA LIDADKPPTP QYFERCLKLV RQGGIIAIDN ILLNGRVMRE AAFDAPPSVK ILKDFNQNLP NDTRIVPITL PVGDGLTLLL KK // ID Q5F8S2_NEIG1 Unreviewed; 260 AA. AC Q5F8S2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89415.2}; GN ORFNames=NGO_0688 {ECO:0000313|EMBL:AAW89415.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89415.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89415.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8S2; -. DR EnsemblBacteria; AAW89415; AAW89415; NGO_0688. DR PATRIC; 20334472; VBINeiGon24812_0808. DR HOGENOM; HOG000218975; -. DR OMA; KVWVRKA; -. DR OrthoDB; EOG64XXP5; -. DR BioCyc; NGON242231:GI2G-655-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011009; Kinase-like_dom. DR SUPFAM; SSF56112; SSF56112; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 260 AA; 28799 MW; 4DC3D9DC59F7A3AC CRC64; MQETRFSILL DELAAKQEAT IAPYLLADGT KVWVRKAGRH NARWRYALLG MVARYLKLGV LKPVPSLGGE PAIATESKRL YELRSAGIAV PELLALRKNA LMFGNLEGIP LDTQIRQEAE AGKADAWLAG LEAIARVHKK RQFLSQAFAR NMMWDGKNIS FLDFEDDPSE VLTIAQCQAR DWLCYIHSTA LILKNGGLLE AAAEKWGGVL SDQPAEIQKL IAGTVKPILP IRRLEHPRWG RDALRLAASI SLISLADMPP // ID Q5F7V8_NEIG1 Unreviewed; 518 AA. AC Q5F7V8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 75. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89729.1}; GN ORFNames=NGO_1059 {ECO:0000313|EMBL:AAW89729.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89729.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89729.1; -; Genomic_DNA. DR RefSeq; WP_003706387.1; NC_002946.2. DR RefSeq; YP_208141.1; NC_002946.2. DR ProteinModelPortal; Q5F7V8; -. DR SMR; Q5F7V8; 441-516. DR EnsemblBacteria; AAW89729; AAW89729; NGO_1059. DR GeneID; 3281721; -. DR KEGG; ngo:NGO1059; -. DR PATRIC; 20335350; VBINeiGon24812_1241. DR HOGENOM; HOG000279402; -. DR OMA; MVMRLLL; -. DR OrthoDB; EOG6F297P; -. DR BioCyc; NGON242231:GI2G-974-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00460213, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 57461 MW; 5BA55AFFDD54FEB9 CRC64; MDFSWLAEPH TWIGFATLLV LEVVLGIDNL VFVAILANKV QPARRDRARI TGLGLAVVIR IIMLAFMAHI ITLTEPLFQI GGLAVSGKDM IMLAGGIFLL YKATTELHER LEGHNRFAVA DNQKKHAPFW GVVAQILILD AVFSIDSVIT AVAMVDHIVV AMGAVVVAMA VMISASKLLT EFVDRHPTVV MLCLGFLLMI GFSLIAEAFH FHIPKGYLYA AIGFSILIEL FNQISQRNSR KNDYIGSSWR KRTAENVLGM MGIRESVLAD AGGESVDDAH FEENEKSMIR SVLTLAERPI MGVMIPRRDI ERLDISQSRE EQYAQLQNTP YSRLLVVGKA GVDEPLGYIN KKDLLSQLLE TGGLDIQTAL RQPLVLPDGT TALGALELFR QSSADYALVV DEFGAVLGMV TMKDLLEAIA GEFPEEFERE EEPAVQENPD ESLTVEGALE YVELASQLNL PQQEEDTDFH TVAGLIMEEL QTIPDVGDFA DFHGWRFEVV EKEGQRIERV KITKLPEE // ID Q5F8R7_NEIG1 Unreviewed; 436 AA. AC Q5F8R7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. DE SubName: Full=Recombination factor protein RarA {ECO:0000313|EMBL:AAW89420.1}; GN ORFNames=NGO_0696 {ECO:0000313|EMBL:AAW89420.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89420.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89420.1; -; Genomic_DNA. DR RefSeq; WP_003688780.1; NC_002946.2. DR RefSeq; YP_207832.1; NC_002946.2. DR ProteinModelPortal; Q5F8R7; -. DR EnsemblBacteria; AAW89420; AAW89420; NGO_0696. DR GeneID; 3282887; -. DR KEGG; ngo:NGO0696; -. DR PATRIC; 20334504; VBINeiGon24812_0824. DR HOGENOM; HOG000017623; -. DR KO; K07478; -. DR OMA; YRYDHDE; -. DR OrthoDB; EOG64FKG0; -. DR BioCyc; NGON242231:GI2G-660-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 46 162 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 436 AA; 48378 MW; 8413FD51AA943768 CRC64; MTDLFVREPD APLAERLRPH TLDDVIGQQH LIGEGKPLRV AVEGGKPHSM LLWGPPGVGK TTLARILAQS FNAQFLPVSA VFSGVKDIRG AIDKAEIALQ QGRATILFVD EVHRFNKAQQ DAFLPHVESG LLTFIGATTE NPSFEVNPAL LSRAQVYVLQ SLSSDDLKKL IAKVLALPEY RDFTIEADVQ ELLVNTADGD ARRLLNLLEQ LLRAADTRRL KILTTEFLAD SLGAQIRRFD KGGESFYNQI SALHKSVRGS HPNAALYWFC RMLDGGTDPR YLARRIVRIA WEDIGLADPR AFQIANDAAA TFERLGSPEG ELALAQAVLY LAAAAKSNAG YKAYNQMRRF VKENASDEVP VHLRNAPTKL MKELGYGREY RYAHDEPNAY AAGESYMPDG LDEPDFYQPV PRGLEIKIGE KLAWLKSLDE EALKAK // ID Q5F5Z7_NEIG1 Unreviewed; 290 AA. AC Q5F5Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 58. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90390.2}; GN ORFNames=NGO_1771 {ECO:0000313|EMBL:AAW90390.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90390.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90390.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5Z7; -. DR EnsemblBacteria; AAW90390; AAW90390; NGO_1771. DR PATRIC; 20337172; VBINeiGon24812_2126. DR HOGENOM; HOG000218655; -. DR OMA; GSEPHIH; -. DR OrthoDB; EOG67MF3D; -. DR BioCyc; NGON242231:GI2G-1665-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 77 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 290 AA; 32330 MW; 1AC16FC4E7F00B04 CRC64; MEIWNMLNTW PDAVPIRAEA AESVAAVAAL LLARALLLNI HFRRHPDFGI ESKRRFLVAS RNITLLLVLF SLAFIWSAQI QTLALSMFAV AAAVVVATKE LIMCLSGSIL RSATQQYSVG DYIEINGLRG RVVDINLLNT LMMQVGPNPL VGQLAGTTVS FPNSLLLSHP VRRDNILGDY VIHTVEIPVP IHLDSDEAVC RLKAVLEPLC APYIPAIQRY LENVQAEKLF ITPAARPRVT RVPYDDKAYR IIVRFASPVS KRLEIQQAVM DEFLRVQYRL LNHPAGSETL // ID Q5FAF9_NEIG1 Unreviewed; 79 AA. AC Q5FAF9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88828.1}; GN ORFNames=NGO_0064 {ECO:0000313|EMBL:AAW88828.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88828.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88828.1; -; Genomic_DNA. DR RefSeq; WP_010950985.1; NC_002946.2. DR RefSeq; YP_207240.1; NC_002946.2. DR EnsemblBacteria; AAW88828; AAW88828; NGO_0064. DR GeneID; 3282310; -. DR KEGG; ngo:NGO0064; -. DR PATRIC; 20332980; VBINeiGon24812_0074. DR HOGENOM; HOG000071342; -. DR OMA; PICPPRF; -. DR OrthoDB; EOG68Q0VK; -. DR BioCyc; NGON242231:GI2G-57-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 79 AA; 8961 MW; 6FF04909F6AA34EB CRC64; MPSEAGFGGF RRSHTAGMQP HQNKIPPAFP ICPPRFLQNK LPALPLREAV RYSEYPEPRY KMTFQTAFAQ PAAFQVKTL // ID Q5F7Z1_NEIG1 Unreviewed; 126 AA. AC Q5F7Z1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 55. DE SubName: Full=XRE family transcriptional regulator {ECO:0000313|EMBL:AAW89696.1}; GN ORFNames=NGO_1013 {ECO:0000313|EMBL:AAW89696.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89696.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89696.1; -; Genomic_DNA. DR RefSeq; WP_003688243.1; NC_002946.2. DR RefSeq; YP_208108.1; NC_002946.2. DR ProteinModelPortal; Q5F7Z1; -. DR EnsemblBacteria; AAW89696; AAW89696; NGO_1013. DR GeneID; 3282127; -. DR KEGG; ngo:NGO1013; -. DR PATRIC; 20335234; VBINeiGon24812_1185. DR HOGENOM; HOG000218923; -. DR OMA; KWERGEN; -. DR OrthoDB; EOG62G5W2; -. DR BioCyc; NGON242231:GI2G-939-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 11 64 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 126 AA; 14103 MW; D8DE1A2D3876B04D CRC64; MEKTSLFGKR LKEERIKLGL NQAEAAEKCG FSREMWGKWE RGENRPSSEK LFSFSKIGID IDYVMHGRRG ETAAMPSESL SAEEKELLAL FRQLGSGSRK ELADYAAFKL VVEKKAQTAL GKVSNG // ID Q5F8X0_NEIG1 Unreviewed; 924 AA. AC Q5F8X0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 66. DE SubName: Full=Type III restriction-modification system HindVIP enzyme res {ECO:0000313|EMBL:AAW89367.1}; GN ORFNames=NGO_0640 {ECO:0000313|EMBL:AAW89367.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89367.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89367.1; -; Genomic_DNA. DR RefSeq; WP_010951098.1; NC_002946.2. DR RefSeq; YP_207779.1; NC_002946.2. DR ProteinModelPortal; Q5F8X0; -. DR REBASE; 10854; NgoAXIIP. DR EnsemblBacteria; AAW89367; AAW89367; NGO_0640. DR GeneID; 3281449; -. DR KEGG; ngo:NGO0640; -. DR PATRIC; 20334364; VBINeiGon24812_0754. DR HOGENOM; HOG000219002; -. DR KO; K01156; -. DR OMA; HLANWVK; -. DR OrthoDB; EOG6H7FCV; -. DR BioCyc; NGON242231:GI2G-607-MONOMER; -. DR Proteomes; UP000000535; 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:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 96 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 65 275 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. SQ SEQUENCE 924 AA; 107418 MW; AB9DBDB195D1E59A CRC64; MANNKTLFDW VEDRKSMLEE MEQTDFFALP EFVSNNLKYP FFEWQKSALE NFVIFDRTSK LKDFPDIKNR PTHLLFNMAT GAGKTMMIAA LILYYFEKGY RHFLFFVNKN NIVYKTENNF IDPTHPKFLF TEKILQGDTV IPIRKVETFS QYSDGIEIKF TSIQKLYNDI HTERENQTTL ADLHELNLVI LGDEAHHLNA QTKGKKQGEL DLEKEMNERT SDAEIERKGW EHMVLELLLN KNGNPGQNVL LEFTATLPEN AEVQQKYADK IITKFGLKEF LQKGYTKEIN LVSGTLNKKE RVLHALLFAW YRHQIALKYG IANFKPVMLF RSKTIDESKA DYSAFLNWVE NVQADDFSFL TTFSTSLSDS NNANEQGKTR TEQALKFMQE NKFEFVHLAN WVKQNYQKHN VIITNSETNK TKTEKTDSET EKLLNNLEAA DNPIRAIFTV DRLTEGWDVL NLFDIVRLYE GQNGGGSNKK SGKTAAATVS EKQLIGRGVR YFPFAFEGKQ PNKRKFDNDM QHELRILEEL FYYTHDEQSR YITELKNELR KDGYLPEKDD DKVLTTFKLK SEFADNKDFR ELLIWANKKI PNPNAKSNNA DSLQANPQTL SFQVHGNQLL QETQFTADEN DETARQIGTQ NNFTQTIKMS EMERHIFNKA LHIKGKNSQS LFHFDRLQSK LDIQNRNELQ NKLLKDWQIE FLGLEQDKQV RPDDKLAGCL KILEMVEKHL NESDIPFIGT KEFTPKKLWE IFGTPKQKWV KKDDIKTAIA TQNDWYVMDN FAGTGLEEAL IQFISARLGD LKSQYDVHLI RNEEVFKLNN FADGEGFMPD FVLLLKDKQK SSSDSVDDFL HYQIFIEPKG GHLVENDSWK EAFLKSITVE YGRDKILQKN TPHYRLIGLP FFTDHQKNGQ FTELFPLGAA SLEK // ID Q5F7S1_NEIG1 Unreviewed; 80 AA. AC Q5F7S1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89766.1}; GN ORFNames=NGO_1099 {ECO:0000313|EMBL:AAW89766.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89766.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89766.1; -; Genomic_DNA. DR RefSeq; WP_003687989.1; NC_002946.2. DR RefSeq; YP_208178.1; NC_002946.2. DR EnsemblBacteria; AAW89766; AAW89766; NGO_1099. DR GeneID; 3282523; -. DR KEGG; ngo:NGO1099; -. DR PATRIC; 20335452; VBINeiGon24812_1292. DR BioCyc; NGON242231:GI2G-1011-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 8679 MW; 2BA10466540A710C CRC64; MAENLSKSAE QIVAELYGSP EDTFTKARMF QTVAAGFKVL VEIERKSYGM DTAESKISES AKTAGIRIEF VGPEDDGKDG // ID Q5F872_NEIG1 Unreviewed; 82 AA. AC Q5F872; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89615.1}; GN ORFNames=NGO_0919 {ECO:0000313|EMBL:AAW89615.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89615.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89615.1; -; Genomic_DNA. DR RefSeq; WP_003688400.1; NC_002946.2. DR RefSeq; YP_208027.1; NC_002946.2. DR ProteinModelPortal; Q5F872; -. DR SMR; Q5F872; 1-82. DR EnsemblBacteria; AAW89615; AAW89615; NGO_0919. DR GeneID; 3281227; -. DR KEGG; ngo:NGO0919; -. DR PATRIC; 20335021; VBINeiGon24812_1080. DR HOGENOM; HOG000160701; -. DR KO; K09159; -. DR OMA; FTWIMGH; -. DR OrthoDB; EOG63FW79; -. DR BioCyc; NGON242231:GI2G-857-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 1.10.150.250; -; 1. DR InterPro; IPR005631; SDH. DR Pfam; PF03937; Sdh5; 1. DR SUPFAM; SSF109910; SSF109910; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 9817 MW; 4AB8189272838950 CRC64; MMVFDDIAKR KIRFQTRRGL LELDLIFGRF MEKEFEHLSD KELSEFSEIL EFQDQELLAL IHGHSETDKG HLIPMLEKIR RA // ID Q5F802_NEIG1 Unreviewed; 122 AA. AC Q5F802; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89685.1}; GN ORFNames=NGO_1002 {ECO:0000313|EMBL:AAW89685.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89685.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89685.1; -; Genomic_DNA. DR RefSeq; WP_003688254.1; NC_002946.2. DR RefSeq; YP_208097.1; NC_002946.2. DR EnsemblBacteria; AAW89685; AAW89685; NGO_1002. DR GeneID; 3282605; -. DR KEGG; ngo:NGO1002; -. DR HOGENOM; HOG000086252; -. DR OMA; GCFKSIH; -. DR OrthoDB; EOG6ZH2MK; -. DR BioCyc; NGON242231:GI2G-928-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 122 AA; 14102 MW; 32DC0E9CA5C7D761 CRC64; MKYWLVGASW GGQGHQDQFF VENGYWVLEW ESSQQPDQFA KGEKIQVGDR IAIKRMKGQG SSEIKILHIG IVKGVISETN KIICVVDWIV KNLDRNVESR GCFKSIHDPY DKDEWIEKIF CL // ID Q5F996_NEIG1 Unreviewed; 257 AA. AC Q5F996; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89241.1}; GN ORFNames=NGO_0503 {ECO:0000313|EMBL:AAW89241.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89241.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89241.1; -; Genomic_DNA. DR RefSeq; WP_003691416.1; NC_002946.2. DR RefSeq; YP_207653.1; NC_002946.2. DR EnsemblBacteria; AAW89241; AAW89241; NGO_0503. DR GeneID; 3282946; -. DR KEGG; ngo:NGO0503; -. DR PATRIC; 20334048; VBINeiGon24812_0596. DR HOGENOM; HOG000057664; -. DR OMA; QMITDAY; -. DR OrthoDB; EOG699732; -. DR BioCyc; NGON242231:GI2G-481-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 257 AA; 27789 MW; B76BA14B6F87C782 CRC64; MQLTFGSGEV FAQMITDAYG NRVQNATPVR IMGLQEMSVD LSAELKEFYG QNRYPLAVAQ GKVKVSGKMK GALINGLTLN TLFFGTEYAT GTMKALWAET TGKVLDGDNY SYLQAAAPGG GKFAEDAGVM GQDGTAYIKV ASSPKQGQYT VSESGVYAFN SSDKGKTVYP SFTYTQTMPP AKKIELTNMA TGNTPTFKMR YLTQFKGKKA LLELESVTSG KLGLFSTKND DFSVPEIDFT ASTDEAGFKI GTLWIQE // ID Q5F576_NEIG1 Unreviewed; 90 AA. AC Q5F576; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Spore cortex protein {ECO:0000313|EMBL:AAW90661.1}; GN ORFNames=NGO_2054 {ECO:0000313|EMBL:AAW90661.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90661.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90661.1; -; Genomic_DNA. DR RefSeq; WP_003686997.1; NC_002946.2. DR RefSeq; YP_209073.1; NC_002946.2. DR EnsemblBacteria; AAW90661; AAW90661; NGO_2054. DR GeneID; 3282742; -. DR KEGG; ngo:NGO2054; -. DR PATRIC; 20337909; VBINeiGon24812_2477. DR HOGENOM; HOG000027825; -. DR OMA; MRKTFLF; -. DR OrthoDB; EOG6R87JH; -. DR BioCyc; NGON242231:GI2G-1955-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256029. SQ SEQUENCE 90 AA; 10486 MW; 419F261CF68C65AB CRC64; MRKTFLILTV SAALLSGCAW ETYQDGNGKT AVRQKYPAGT PVYYQDGSYS KNMNYNQYRP ERRAVLPDQT GNNADEEHRQ HWQKPKFQNR // ID Q5F601_NEIG1 Unreviewed; 504 AA. AC Q5F601; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 80. DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498}; DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498}; GN ORFNames=NGO_1767 {ECO:0000313|EMBL:AAW90386.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90386.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90386.1; -; Genomic_DNA. DR RefSeq; WP_010951343.1; NC_002946.2. DR RefSeq; YP_208798.1; NC_002946.2. DR ProteinModelPortal; Q5F601; -. DR SMR; Q5F601; 11-487. DR EnsemblBacteria; AAW90386; AAW90386; NGO_1767. DR GeneID; 3282549; -. DR KEGG; ngo:NGO1767; -. DR PATRIC; 20337154; VBINeiGon24812_2117. DR HOGENOM; HOG000087852; -. DR KO; K03781; -. DR OMA; QVHADFG; -. DR OrthoDB; EOG6P5Z9F; -. DR BioCyc; NGON242231:GI2G-1661-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; 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:UP000000535}. 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; 57313 MW; 734216BB630E95F6 CRC64; MTTSKCPVTH LTMNNGAPVA DNQNSLTAGP RGPLLTQDLW LNEKLADFVR EVIPERRMHA KGSGAFGTFT VTHDITKYTR AKIFSEVGKK TEMFARFTTV AGERGAADAE RDIRGFALKF YTEEGNWDVV GNNTPVFFLR DPRKFPDLNK AVKRDPRTNM RSATNNWDFW TLLPEALHQV TIVMSDRGIP ASYRHMHGFG SHTYSFWNEA GERFWVKFHF RSQQGIKNLT NEEAAKIIAD DRESHQRDLY EAIERGEFPK WTMYIQVMPE ADAEKVPYHP FDLTKVWPKK DYPLIEVGEF ELNRNPENFF ADVEQSAFAP SNLVPGIGAS PDKMLQARLF NYADAQRYRL GVNFRQIPVN RPRCPVHSNQ RDGQGRADGN YGSLPHYEPN SFGQWQQQPD FAEPPLKING DAAHWDYRQD DDDYFSQPRA LFNLMNDAQK QALFDNTAAA MGDAPDFIKY RHIRNCYRCD PAYGEGVAKA LGLTVEDAQA VRATDPALGQ AGLL // ID Q5F8W4_NEIG1 Unreviewed; 397 AA. AC Q5F8W4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 83. DE RecName: Full=Acetylornithine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107}; DE Short=ACOAT {ECO:0000256|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000256|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000256|HAMAP-Rule:MF_01107, GN ECO:0000313|EMBL:AAW89373.1}; GN ORFNames=NGO_0646 {ECO:0000313|EMBL:AAW89373.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89373.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01107}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_01107}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01107}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000256|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; AE004969; AAW89373.1; -; Genomic_DNA. DR RefSeq; WP_003691287.1; NC_002946.2. DR RefSeq; YP_207785.1; NC_002946.2. DR ProteinModelPortal; Q5F8W4; -. DR SMR; Q5F8W4; 2-393. DR EnsemblBacteria; AAW89373; AAW89373; NGO_0646. DR GeneID; 3281412; -. DR KEGG; ngo:NGO0646; -. DR PATRIC; 20334378; VBINeiGon24812_0761. DR HOGENOM; HOG000020206; -. DR KO; K00821; -. DR OMA; GHLFAYM; -. DR OrthoDB; EOG6QVRHN; -. DR BioCyc; NGON242231:GI2G-613-MONOMER; -. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_01107}; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|SAAS:SAAS00461222, ECO:0000313|EMBL:AAW89373.1}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01107}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01107}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS00461208}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01107, KW ECO:0000256|SAAS:SAAS00461222, ECO:0000313|EMBL:AAW89373.1}. FT REGION 214 217 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 129 129 Pyridoxal phosphate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 132 132 N2-acetyl-L-ornithine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 271 271 N2-acetyl-L-ornithine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. FT BINDING 272 272 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_01107}. FT MOD_RES 243 243 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_01107}. SQ SEQUENCE 397 AA; 42684 MW; 135A1D730C872F95 CRC64; MQNYLTPNFA FAPMIPERAS GSRVWDTEGR EYIDFSGGIA VNALGHCHPA LVDALNAQMH KLWHISNIYT TRPAQELAQK LVKHSFADKV FFCNSGAEAN EAALKLARKY ARDRFGGGKS EIVACINSFH GRTLFTVSVG GQPKYSKDYA PLPQGITHVP FNDIAALEAA VGEQTCAVII EPIQGESGIL PATAEYLQAA RRLCDRHNAL LILDEVQTGM GHTGRLFAYE HYGVVPDILS SAKALGCGFP IGTMLATEKI AAAFQPGTHG STFGGNPMAC AVGSRAFDII NAPETLHNVR SQGQKLQTAL LDLGRKTGLF SQVRGMGLLL GCALDTPYRG RSSEIAATSL KHGVMILVAG ADVLRFAPSL LLNDEDIAEG LRRLEHVLTE FAAANRP // ID Q5FA54_NEIG1 Unreviewed; 604 AA. AC Q5FA54; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Polymerase {ECO:0000313|EMBL:AAW88933.1}; GN ORFNames=NGO_0178 {ECO:0000313|EMBL:AAW88933.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88933.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88933.1; -; Genomic_DNA. DR RefSeq; WP_003690624.1; NC_002946.2. DR RefSeq; YP_207345.1; NC_002946.2. DR EnsemblBacteria; AAW88933; AAW88933; NGO_0178. DR GeneID; 3281327; -. DR KEGG; ngo:NGO0178; -. DR PATRIC; 20333283; VBINeiGon24812_0224. DR HOGENOM; HOG000218824; -. DR OMA; LQNIIVY; -. DR OrthoDB; EOG65QWDS; -. DR BioCyc; NGON242231:GI2G-163-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 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 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; 67098 MW; E0334B8CE11F45BB CRC64; MSAETTVSGA RPAAKLPIYI LPCFLWIGII PFTFALRLKP SPDFYHDAAA AAGLIVLLFL TAGKKLFDVK IPAISFLLFA MAAFWWLQAR LMNLIYPGMN DIASWVFILL AVSAWACKSL VAHYGQERIV TLFAWSLLIG SLLQSCIVVI QFAGWENTPL LQNIIVHRGQ GVIGHIGQRN NLGHYLMWGI LASAYLNGQR KIPAALGAIC LIMQTAVLGL VNSRTILTYI AAIALILPFW YFRSDKSNRR TMLGIAAAVF LTALFQFSMN AILETFTGIR YETAVERVAN GGFTDLPRQS EWNKALAAFQ SAPIFGHGWN SFAQQTFLIN AEQHTIHDNF LSTLFTHSHN IILQLLAEMG ISGTLLVAAT LLTGIAGLLK RSLTPASLFL LCALAVSMCH SMLEYPLWYV YFLIPFGLML FLSPAEASDG IAFKKAANLG ILTASAAIFA GLLHLDWTYT RLVNSFSPAA DDSAKTLNRK INELRYISAN SPMLSFYADF SLVNFALPEY PETQTWAEEA TLKALKYRPY SATYRIALYL MRQGKVAEAK QWMRATQSYY PYLMPRYADE IRKLPVWAPL LPELLKDCKA FAAAPGHPET KPCK // ID Q5F7S3_NEIG1 Unreviewed; 750 AA. AC Q5F7S3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89764.1}; GN ORFNames=NGO_1097 {ECO:0000313|EMBL:AAW89764.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89764.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89764.1; -; Genomic_DNA. DR RefSeq; WP_010951184.1; NC_002946.2. DR RefSeq; YP_208176.1; NC_002946.2. DR EnsemblBacteria; AAW89764; AAW89764; NGO_1097. DR GeneID; 3282224; -. DR KEGG; ngo:NGO1097; -. DR PATRIC; 20335448; VBINeiGon24812_1290. DR HOGENOM; HOG000225124; -. DR OMA; VWYIDEK; -. DR OrthoDB; EOG61CKWJ; -. DR BioCyc; NGON242231:GI2G-1009-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 750 AA; 83288 MW; BE3EBFC42BD5F411 CRC64; MGTDVPETGV LPDKNGEPLT IGEYRLFVGE MMNQPAWRAV ADKEMDYADG RQLDNELLQK QRELGLPPAV ENLITPTLLS VQGYEATIRT DWRVTADGET GGRDVADALN FKLNRAERQS RADKACSDAF RGQIACGIGW VEVTRNPNPF EFPYECGVIH RNAIHWDMKS YKYDLSDARW LIRRRWLLPE RLAQFFPEYA GHFKAMGRGG SDWRISGEML DGGGNTGLAD AWGISGRNTV SEEFWFNETT RELAVAEVWY RRWVTADCLR DKKTGRTVEF DGANPNHREM AANGAVLFAA SVPRMRRAFV VGDLVVRDEP TPYPHQKFPY VPFFGFREDN TGIPYGYVRN MKYAQDNLNS TNSKLRWGLS AIRTVRTKGI VDMSDEQFRR NIARVDADIV LNKIEAAQPG ARFDVSRDFE LSAQHWQMLQ DSRATIRQIS GITPSFMGNR GNATSGRQES IQVEQSNQSL GLVMDNFRQS RSLVGELLLA MIIEDLGSDE QTVVIEGDAV TQGRTVVINR PETDPVTGKA YLSNDLQNIR LKVALEDVPS TNSYRSQQLG AMSEAVKSLP PEYQAAVLPF MVSLMDIPFK DKVIEKIKEV RVQETPEQIE ARIAQAVQDA LAKSGNDIKR RELALKEQRT ASEIKEIEAR AVQIGVQAAY AAMQAGGQIA AMPQIAPVAD AVMQGAGYIR PARGDDPGFP VPAMPPETQI PPEGIPEAYG ADTGPMTAVP PKSANHAQTG METPTVSDNL // ID Q5F9E1_NEIG1 Unreviewed; 102 AA. AC Q5F9E1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89196.1}; GN ORFNames=NGO_0457 {ECO:0000313|EMBL:AAW89196.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89196.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89196.1; -; Genomic_DNA. DR RefSeq; WP_010951048.1; NC_002946.2. DR RefSeq; YP_207608.1; NC_002946.2. DR EnsemblBacteria; AAW89196; AAW89196; NGO_0457. DR GeneID; 3282987; -. DR KEGG; ngo:NGO0457; -. DR PATRIC; 20333946; VBINeiGon24812_0547. DR HOGENOM; HOG000122612; -. DR OMA; DKPHELI; -. DR OrthoDB; EOG6X3W8B; -. DR BioCyc; NGON242231:GI2G-434-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR008407; Brnchd-chn_aa_trnsp_AzlD. DR Pfam; PF05437; AzlD; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 91 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 102 AA; 10990 MW; 20348B32A3FDB6A6 CRC64; MKDLLSSPSF LLFSCMLAVT CPTRLIGFFA LRNRTLSRRA QTVMEAAPGC VLISVIAPYF VSDKPHELIA IALTAFAACR FSMLFTVLIG VGSSGISGWL MA // ID Q5F9X8_NEIG1 Unreviewed; 107 AA. AC Q5F9X8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89009.1}; GN ORFNames=NGO_0258 {ECO:0000313|EMBL:AAW89009.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89009.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89009.1; -; Genomic_DNA. DR RefSeq; WP_002238889.1; NC_002946.2. DR RefSeq; YP_207421.1; NC_002946.2. DR EnsemblBacteria; AAW89009; AAW89009; NGO_0258. DR GeneID; 3281085; -. DR KEGG; ngo:NGO0258; -. DR PATRIC; 20333473; VBINeiGon24812_0317. DR HOGENOM; HOG000218842; -. DR OMA; EYMEDSD; -. DR OrthoDB; EOG6K4009; -. DR BioCyc; NGON242231:GI2G-241-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018689; DUF2185. DR Pfam; PF09951; DUF2185; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 15 98 DUF2185. {ECO:0000259|Pfam:PF09951}. SQ SEQUENCE 107 AA; 11827 MW; 54F6D701FED7D1EF CRC64; MNAFAQALSS ALDRCIATNT VAKQNRPVGF LYREAPVFEN DSGWRFFSGD ETDEYTDDPD NFSIVSLADI TKTNPETAAL LSQPEGSAWE LAEDGTFQTV ADWQPQD // ID Q5F8R4_NEIG1 Unreviewed; 400 AA. AC Q5F8R4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Restriction endonuclease subunit S {ECO:0000313|EMBL:AAW89423.1}; GN ORFNames=NGO_0699 {ECO:0000313|EMBL:AAW89423.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89423.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89423.1; -; Genomic_DNA. DR RefSeq; WP_003691244.1; NC_002946.2. DR RefSeq; YP_207835.1; NC_002946.2. DR ProteinModelPortal; Q5F8R4; -. DR REBASE; 10859; S.NgoAXVII. DR EnsemblBacteria; AAW89423; AAW89423; NGO_0699. DR GeneID; 3281876; -. DR KEGG; ngo:NGO0699; -. DR PATRIC; 20334510; VBINeiGon24812_0827. DR HOGENOM; HOG000002669; -. DR KO; K01154; -. DR OMA; GTYRIIK; -. DR OrthoDB; EOG6JDWF1; -. DR BioCyc; NGON242231:GI2G-663-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89423.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89423.1}; KW Nuclease {ECO:0000313|EMBL:AAW89423.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 42 177 Methylase_S. {ECO:0000259|Pfam:PF01420}. SQ SEQUENCE 400 AA; 45584 MW; EA648009BA45CAF8 CRC64; MNHFKKQQIQ NIADFNPREQ LAKGALAKSV PMAMLKEFQR QITGYEIKAF NGGAKFRNGD TLLAKITPCL ENGKTAFVDI LDDGEVAFGS TEFIVLRAKN ETNPEFLYYF AISPDFRKRA IECMEGTSGR QRVNENALKT LELPIPEPQI QQSIAAVLSA LDKKIALNKQ INARLEEMAK TLYDYWFVQF DFPDANGKPY KSSGGDMVFD ETLKREIPKG WGSIELQSCL AKIPNTTKIL NKDIKDFGKY PVVDQSQDFI CGFTNDEKSI LNPQDAHIIF GDHTRIVKLV NFQYARGADG TQVILSNNER MPNYLFYQII NQIDLSSYGY ARHFKFLKEF KIILPSKDIS QKYNEIANTF FVKVRNNLKQ NHHLTQLRDF LLPMLMNGQV SVRCSGARDG // ID Q5F6B3_NEIG1 Unreviewed; 395 AA. AC Q5F6B3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90274.1}; GN ORFNames=NGO_1647 {ECO:0000313|EMBL:AAW90274.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90274.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90274.1; -; Genomic_DNA. DR RefSeq; WP_003689773.1; NC_002946.2. DR RefSeq; YP_208686.1; NC_002946.2. DR ProteinModelPortal; Q5F6B3; -. DR SMR; Q5F6B3; 1-191. DR EnsemblBacteria; AAW90274; AAW90274; NGO_1647. DR GeneID; 3281342; -. DR KEGG; ngo:NGO1647; -. DR PATRIC; 20336834; VBINeiGon24812_1962. DR HOGENOM; HOG000218807; -. DR KO; K10954; -. DR OMA; KSAEVHT; -. DR OrthoDB; EOG6C8MWQ; -. DR BioCyc; NGON242231:GI2G-1543-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 224 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 395 AA; 44049 MW; 71FAAD99DD6AC546 CRC64; MAEICLITGT PGSGKTLKMV SMMANDEMFK PDENGVRRKV FTNIKGLKIP HTHIETDAKK LPKSTDEQLS AHDMYEWIKK PENVGAIVIV DEAQDVWPAR SAGSKIPENV QWLNTHRHQG IDIFVLTQGP KLLDQNLRTL VKRHYHIAAN KMGLRTLLEW KVCADDPVKM ASSAFSSIYT LDKKVYDLYE SAEIHTVNKV KRSKWFYALP VIILLIPLFV GLSYKMLGSY GKKQEEPAAQ ESAATEQQAV LPDKTEGESV NNGNLTADMF VPTLPEKPES KPIYNGVRQV RTFEYIAGCI EGGRTGCTCY SHQGTALKEV TELMCKDYVK NGLPFNPYKE ESQGQEVQQS AQQHSDRAQV ATLGGKPQQN LMYDNWEERG KPFEGIGGGV VGSAN // ID Q5F827_NEIG1 Unreviewed; 436 AA. AC Q5F827; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89660.1}; GN ORFNames=NGO_0974 {ECO:0000313|EMBL:AAW89660.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89660.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89660.1; -; Genomic_DNA. DR RefSeq; WP_010951156.1; NC_002946.2. DR RefSeq; YP_208072.1; NC_002946.2. DR ProteinModelPortal; Q5F827; -. DR EnsemblBacteria; AAW89660; AAW89660; NGO_0974. DR GeneID; 3282874; -. DR KEGG; ngo:NGO0974; -. DR PATRIC; 20335142; VBINeiGon24812_1140. DR HOGENOM; HOG000259439; -. DR OMA; PLYALMQ; -. DR OrthoDB; EOG628F2J; -. DR BioCyc; NGON242231:GI2G-902-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 47265 MW; D12F1498025C0FC9 CRC64; MDAKKGGLGL VKSRRFGPLF ATQFLGAFND NVFKTALFVM IGFYGLGQNG FLPAGQMLNL GALLFILPYF LFSALSGQLG NKFDKAVLAR WVKVLEIIIM AVAAYGFYIR SAPLLLLCLF CMGAQSTLFG PLKYAILPDY LDDNELMMGN SLIESGTFVA ILFGQILGTA VAGAPPYIVG ILVLLVAVGG TAGSLFMPSV PAKAADTQIE WNIVRGTKSL LRETVRHNPV FTAIIGISWF WFVGAVYTTQ LPTFTQIHLG GNDNVFNLML ALFSIGIAAG SVLCAKFGRE RLMLAWVTVG ALGLTVCGLV LVWLTHGHRF EGLNGIFWFL SQGWAYPVMA VMTLIGFFGG FFSVPLYTWL QTASSETFRA RAVAANNIVN GIFMVSAAVL SAVLLFLFDS ISLLYLIVAL GNIPLAVFLI KRERRFLGAA AIRKKP // ID Q5F7J6_NEIG1 Unreviewed; 72 AA. AC Q5F7J6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89841.1}; GN ORFNames=NGO_1179 {ECO:0000313|EMBL:AAW89841.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89841.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89841.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89841; AAW89841; NGO_1179. DR OrthoDB; EOG60KNF7; -. DR BioCyc; NGON242231:GI2G-1093-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 72 AA; 8516 MW; 757E304AFE7BBD62 CRC64; MRGPRHSHLS VICFVKERCE IIKYPFRLSK ISLDISDIPC YTFQFVRRFG SGEEPNYTLK EICGQPFFEK IL // ID Q5F815_NEIG1 Unreviewed; 336 AA. AC Q5F815; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=ADP-heptose--LPS heptosyltransferase {ECO:0000313|EMBL:AAW89672.1}; GN ORFNames=NGO_0987 {ECO:0000313|EMBL:AAW89672.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89672.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89672.1; -; Genomic_DNA. DR RefSeq; WP_003706351.1; NC_002946.2. DR RefSeq; YP_208084.1; NC_002946.2. DR ProteinModelPortal; Q5F815; -. DR CAZy; GT9; Glycosyltransferase Family 9. DR EnsemblBacteria; AAW89672; AAW89672; NGO_0987. DR GeneID; 3281360; -. DR KEGG; ngo:NGO0987; -. DR PATRIC; 20335176; VBINeiGon24812_1157. DR HOGENOM; HOG000237541; -. DR KO; K02843; -. DR OMA; IAFCPGA; -. DR OrthoDB; EOG64N9TX; -. DR BioCyc; NGON242231:GI2G-914-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89672.1}. SQ SEQUENCE 336 AA; 37553 MW; BD6B68A0F2088196 CRC64; MSIKILIISP SWIGDCVMTQ PLFRRLKKLH PGCTIDVFAP KWSMAVFERM PEVNEILENP FGHGALELKR RWRVGRELGR RGYDRVIVLP GSLKSAVIAL ATGIGKRTGY VGESRYFLLN DIRRLDKERL PLMVDRYTAL AHQSQEDFDG HSGFPEFSID ERRREISVET FGLNLGKPVL AFCPGAEFGP AKRWPARHFA ELGKHYSEAG WQVWLFGSQK DNEIAEEINC LSDGMCVNLC GKTDLSQAMD LLSLADTVVC NDSGLMHLAA ALGRKVVAVY GSSSPTHTPP LSDRAKIVSL HLECSPCFKR ECPLGHTDCL NRLYPEKIVQ AVEEAV // ID Q5F5L6_NEIG1 Unreviewed; 228 AA. AC Q5F5L6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:AAW90521.1}; GN ORFNames=NGO_1907 {ECO:0000313|EMBL:AAW90521.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90521.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90521.1; -; Genomic_DNA. DR RefSeq; WP_003690201.1; NC_002946.2. DR RefSeq; YP_208933.1; NC_002946.2. DR ProteinModelPortal; Q5F5L6; -. DR EnsemblBacteria; AAW90521; AAW90521; NGO_1907. DR GeneID; 3282293; -. DR KEGG; ngo:NGO1907; -. DR PATRIC; 20337534; VBINeiGon24812_2294. DR HOGENOM; HOG000048983; -. DR KO; K06997; -. DR OMA; HGSTMVR; -. DR OrthoDB; EOG6G7R84; -. DR BioCyc; NGON242231:GI2G-1810-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR004848-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 24984 MW; 430539473D50BCC3 CRC64; MTVLQERYRE VSDRIGKLVL QAGREPHSVS LIAVSKTFPS DGIREVYAAG QRDFGENYIQ EWYGKTEELA DLTDIVWHVI GDVQSNKTKF VAERAHWVHT VCRLKTAVRL SRQRRSLMPP LQVCVEVNIA GEAAKHGVAP EEAVALAVEV AKLPNLVVRG LMCVAKANSS ETELKTQFQT MQKLLADLNA AGVKADVLSM GMSDDMPAAI ECGATHVRIG SAIFGKRG // ID Q5F5C1_NEIG1 Unreviewed; 366 AA. AC Q5F5C1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Cytochrome C biogenesis protein CcdA {ECO:0000313|EMBL:AAW90616.1}; GN ORFNames=NGO_2008 {ECO:0000313|EMBL:AAW90616.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90616.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90616.1; -; Genomic_DNA. DR RefSeq; WP_003701763.1; NC_002946.2. DR RefSeq; YP_209028.1; NC_002946.2. DR ProteinModelPortal; Q5F5C1; -. DR EnsemblBacteria; AAW90616; AAW90616; NGO_2008. DR GeneID; 3282616; -. DR KEGG; ngo:NGO2008; -. DR PATRIC; 20337797; VBINeiGon24812_2422. DR HOGENOM; HOG000042042; -. DR KO; K03153; -. DR OMA; PRYPIYI; -. DR OrthoDB; EOG622PM9; -. DR BioCyc; NGON242231:GI2G-1909-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 4. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 333 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 366 AA; 40516 MW; 93C60CAB85C64125 CRC64; MTRIAVLGGG LSGRLTALQL AEQGYQIELF DKGTRQGEHA AAYVAAAMLA PAAEAVEATP EVIRLGRQSI PLWRGIRCRL NTLTMMQENG SLIVWHGQDK PLSSEFVRHL KRGGVADDEI VRWRADEIAE REPQLGGRFS DGIYLPTEGQ LDGRQILSAL ADALDELNVP CHWEHECAPQ DLQAQYDWVI DCRGYGAKTA WNQSPEHTST LRGIRGEVAR VYTPEITLNR PVRLLHPRYP LYIAPKENHV FVIGATQIES ESQAPASVRS GLELLSALYA VHPAFGEADI LEIAAGLRPT LNHHNPEIRY SRERRLIEIN GLFRHGFMIS PAVTAAAVRL AVALFDGKDA PERDEESGLA YIGRQD // ID Q5F729_NEIG1 Unreviewed; 259 AA. AC Q5F729; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 66. DE SubName: Full=GntR family transcriptional regulator {ECO:0000313|EMBL:AAW90008.1}; GN ORFNames=NGO_1360 {ECO:0000313|EMBL:AAW90008.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90008.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90008.1; -; Genomic_DNA. DR RefSeq; WP_003691718.1; NC_002946.2. DR RefSeq; YP_208420.1; NC_002946.2. DR ProteinModelPortal; Q5F729; -. DR EnsemblBacteria; AAW90008; AAW90008; NGO_1360. DR GeneID; 3282241; -. DR KEGG; ngo:NGO1360; -. DR PATRIC; 20336105; VBINeiGon24812_1601. DR HOGENOM; HOG000273991; -. DR KO; K05799; -. DR OMA; RLCFEAT; -. DR OrthoDB; EOG6M9DVM; -. DR BioCyc; NGON242231:GI2G-1273-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00452277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 29501 MW; C48650C15380976C CRC64; MKLVRPQKIS DQVLSVLEGR IVEGVYAEGG KIPPERVLAE EFGVSRPSVR SALNILVARQ ILEARQGDGY YVSVKPQQDF LQSWQELLGK HSNWEQDVFD FSCHIEGCMA ALAAERRTDA DLKRIRFWLE KFEEACGSGN LEHQGEADVS FHQTIADAAH NLLFSHLSGG LLKMLYRQTR SSLIYLNQEE DPRPKLMAQH RVLYEAISNR RPGEASEAAK AHLNYVASSI LKDREYQSRN RHADTLAQND LKRVQDWEV // ID Q5F6F4_NEIG1 Unreviewed; 244 AA. AC Q5F6F4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 82. DE SubName: Full=Sugar ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90233.1}; GN ORFNames=NGO_1605 {ECO:0000313|EMBL:AAW90233.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90233.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90233.1; -; Genomic_DNA. DR RefSeq; WP_003689540.1; NC_002946.2. DR RefSeq; YP_208645.1; NC_002946.2. DR ProteinModelPortal; Q5F6F4; -. DR EnsemblBacteria; AAW90233; AAW90233; NGO_1605. DR GeneID; 3281566; -. DR KEGG; ngo:NGO1605; -. DR PATRIC; 20336748; VBINeiGon24812_1919. DR KO; K06861; -. DR OMA; YYLGDNF; -. DR OrthoDB; EOG6VXF80; -. DR BioCyc; NGON242231:GI2G-1502-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90233.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90233.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 240 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 244 AA; 27011 MW; 88B589960AC2CE5D CRC64; MSANNSRLVV QNLQKSFKKR QVVKSFSLEI ESGEVIGLLG PNGAGKTTGF YMIVGLIAAD AGSVMLDGRE LRHLPIHERA RLGVGYLPQE ASIFRKMTVE QNIRAILEIR TKDKNQIDRE IEKLLADLNI GHLRRNPAPS LSGGERRRVE IARVLAMKPR FILLDEPFAG VDPIAVIDIQ KIIGFLKSRG IGVLITDHNV RETLSICDRA YIISDGAVLA SGKPDDLVGN EQVRAVYLGE NFKY // ID Q5F9V7_NEIG1 Unreviewed; 259 AA. AC Q5F9V7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=Laccase domain protein {ECO:0000256|RuleBase:RU361274}; GN ORFNames=NGO_0281 {ECO:0000313|EMBL:AAW89030.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89030.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89030.1; -; Genomic_DNA. DR RefSeq; WP_003690756.1; NC_002946.2. DR RefSeq; YP_207442.1; NC_002946.2. DR ProteinModelPortal; Q5F9V7; -. DR SMR; Q5F9V7; 15-256. DR EnsemblBacteria; AAW89030; AAW89030; NGO_0281. DR GeneID; 3281603; -. DR KEGG; ngo:NGO0281; -. DR PATRIC; 20333537; VBINeiGon24812_0349. DR HOGENOM; HOG000242994; -. DR KO; K05810; -. DR OMA; VVMTADC; -. DR OrthoDB; EOG60GRZN; -. DR BioCyc; NGON242231:GI2G-262-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 259 AA; 27128 MW; E49D4EAE0BDD0295 CRC64; MKTITETLNL APKGKNFLTA DWPAPANVKT LITTRNGGVS QGAYQSLNLG THVGDDPETV RRNREIVQQQ VGLPVAYLNQ IHSTIVVNAA EALDGTPDAD ASVDDTGKAV CAVMTADCLP VLFCDRAGTA VAAAHAGWSG LAGGVLQNTI AAMKVPPVEI MAYLGPAISA DAFEVGQDVF DAFCTSMPEA AAAFEPIGGG KFLADLYALA RLILKREGVG GVYGGTHCTV LERDIFFSYR RDGATGRMAS LIWLDGNAV // ID Q5F985_NEIG1 Unreviewed; 110 AA. AC Q5F985; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89252.1}; GN ORFNames=NGO_0514 {ECO:0000313|EMBL:AAW89252.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89252.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89252.1; -; Genomic_DNA. DR RefSeq; WP_003691408.1; NC_002946.2. DR RefSeq; YP_207664.1; NC_002946.2. DR EnsemblBacteria; AAW89252; AAW89252; NGO_0514. DR GeneID; 3282934; -. DR KEGG; ngo:NGO0514; -. DR PATRIC; 20334070; VBINeiGon24812_0607. DR OMA; WASLQEH; -. DR OrthoDB; EOG6BKJHV; -. DR BioCyc; NGON242231:GI2G-492-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 110 AA; 11150 MW; BCA02571B1EC8FC1 CRC64; MGFLQFGLLF AAAGGVLGAV WASLQERGRP VQAVLEAFIS AIAAAAAAER FVPLDQAWTC AAAGVFAGMM TGHALDTVRA LAPKVLRGYL GGLAEKLTGV KDGGSSDGKD // ID Q5F7U0_NEIG1 Unreviewed; 152 AA. AC Q5F7U0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Cytochrome C {ECO:0000313|EMBL:AAW89747.1}; GN ORFNames=NGO_1080 {ECO:0000313|EMBL:AAW89747.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89747.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89747.1; -; Genomic_DNA. DR RefSeq; WP_003688008.1; NC_002946.2. DR RefSeq; YP_208159.1; NC_002946.2. DR ProteinModelPortal; Q5F7U0; -. DR EnsemblBacteria; AAW89747; AAW89747; NGO_1080. DR GeneID; 3281435; -. DR KEGG; ngo:NGO1080; -. DR PATRIC; 20335404; VBINeiGon24812_1268. DR HOGENOM; HOG000288835; -. DR OMA; SCEACHK; -. DR OrthoDB; EOG64N9ZS; -. DR BioCyc; NGON242231:GI2G-992-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 152 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256054. 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; 16092 MW; 3F9416C37647810E CRC64; MKTQISLAAT ALALFLSACG NGGAPAQPKG EISENRTAAF KSMMPDFSRM GKMVKGEEPY DVEKFKQAAA AFAESSKKPF TLFESDPQGN GRALPAVWSD GAKFEAEKTK FAAAVEKLNA AAQTGKLDEI KAAYGETGAS CKSCHDSFRA PE // ID Q5F855_NEIG1 Unreviewed; 383 AA. AC Q5F855; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89632.1}; GN ORFNames=NGO_0937 {ECO:0000313|EMBL:AAW89632.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89632.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89632.1; -; Genomic_DNA. DR RefSeq; WP_003688367.1; NC_002946.2. DR RefSeq; YP_208044.1; NC_002946.2. DR EnsemblBacteria; AAW89632; AAW89632; NGO_0937. DR GeneID; 3281688; -. DR KEGG; ngo:NGO0937; -. DR PATRIC; 20335059; VBINeiGon24812_1099. DR HOGENOM; HOG000258106; -. DR OMA; FFFPGFT; -. DR OrthoDB; EOG60918W; -. DR BioCyc; NGON242231:GI2G-874-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR016633; UCP015557. DR Pfam; PF10093; DUF2331; 1. DR PIRSF; PIRSF015557; UCP015557; 1. DR TIGRFAMs; TIGR03837; efp_adjacent_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 383 AA; 44212 MW; 76D379BD9DD73439 CRC64; MNTYAFPVCW IFCKVIDNFG DIGVSWRLAR VLHRELGWQV HLWTDDVSAL RALCPDLPDV PFVHQDIHVR TWHSDAADID TAPVPDAVIE TFACDLPENV LNIIRRHKPL WLNWEYLSAE ESNERLHLMP SPQEGVQKYF WFMGFSEKSG GLIRERDYRE AVRFDTEALR RRLVLPEKNA PEWLLFGYRG DVWAKWLDMW QQAGSLMTLL LAGAQIIDSL KQSGVIPQNA LQNDGGVFQT ASVRLVKIPF VPQQDFDKLL HLADCAVIRG EDSFVRTQLA GKPFFWHIYP QDENVHLDKL HAFWDKAYGF YTPETASVHR LLSDDLNGGE ALSATQRLEC WQTLQQHQNG WRQGAEDWSR YLFGQPSASE KLAAFVSKHQ KIR // ID Q5F6F1_NEIG1 Unreviewed; 178 AA. AC Q5F6F1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 67. DE SubName: Full=3-deoxy-D-manno-octulosonate 8-phosphate phosphatase {ECO:0000313|EMBL:AAW90236.2}; GN ORFNames=NGO_1608 {ECO:0000313|EMBL:AAW90236.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90236.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90236.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6F1; -. DR EnsemblBacteria; AAW90236; AAW90236; NGO_1608. DR PATRIC; 20336754; VBINeiGon24812_1922. DR HOGENOM; HOG000264740; -. DR OMA; FDENFHE; -. DR OrthoDB; EOG62C9JR; -. DR BioCyc; NGON242231:GI2G-1505-MONOMER; -. DR Proteomes; UP000000535; 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; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR010023; KDO_8-P_phosphatase. DR PIRSF; PIRSF006118; KDO8-P_Ptase; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01670; KdsC-phosphatas; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|SAAS:SAAS00455242}; KW Magnesium {ECO:0000256|PIRSR:PIRSR006118-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR006118-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 19143 MW; 8752CDD91B5C3EF0 CRC64; MQAISPELQA RAAKIKLLIL DVDGVLTDGR IFIRDDGEEI KSFHTLDGHG LKMLQASGVQ TAIITGRDAP SVGIRVKQLG INYYFKGISD KRAAYEELRA QAGLEEAECA FVGDDVVDLP VMVRCGLPVA VPDAHWFTLQ HAAYIAKRPG GAGAVREVCD LIIRAKGTLG AALNGYIK // ID Q5F4Y3_NEIG1 Unreviewed; 241 AA. AC Q5F4Y3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE RecName: Full=Ribosomal RNA small subunit methyltransferase E {ECO:0000256|PIRNR:PIRNR015601}; DE EC=2.1.1.193 {ECO:0000256|PIRNR:PIRNR015601}; GN ORFNames=NGO_2160 {ECO:0000313|EMBL:AAW90754.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90754.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90754.1; -; Genomic_DNA. DR RefSeq; WP_003692438.1; NC_002946.2. DR RefSeq; YP_209166.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y3; -. DR EnsemblBacteria; AAW90754; AAW90754; NGO_2160. DR GeneID; 3282764; -. DR KEGG; ngo:NGO2160; -. DR PATRIC; 20338174; VBINeiGon24812_2609. DR HOGENOM; HOG000015265; -. DR KO; K09761; -. DR OMA; EKRVAHW; -. DR OrthoDB; EOG6FJNHQ; -. DR BioCyc; NGON242231:GI2G-2048-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR015601}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR015601, KW ECO:0000313|EMBL:AAW90754.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW rRNA processing {ECO:0000256|PIRNR:PIRNR015601}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR015601}; KW Transferase {ECO:0000256|PIRNR:PIRNR015601, KW ECO:0000313|EMBL:AAW90754.1}. SQ SEQUENCE 241 AA; 26779 MW; 934037DEDAF0E47D CRC64; MPRFYLPENL SVGQTVDLPD NIVRHLNVLR VRPNENITLF DGKGKAHTAR LTVLEKHRAE AEILHEDTTD NESPLNITLI QSISSGDRMD FTLQKSVELG VTAIQPVISE RCIVRLDGER AAKRLARWQE IVISACEQSG RNTVPPVLPI IGYREALDKM PSENTKLIMS INRACKLGDI RHPSGAIVFM VGPEGGWTEQ EEQQAFEAGF QAVTLGKRIL RTETAPLAAI AAMQTLWGDF T // ID Q5F6E7_NEIG1 Unreviewed; 319 AA. AC Q5F6E7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 69. 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 ORFNames=NGO_1612 {ECO:0000313|EMBL:AAW90240.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90240.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90240.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6E7; -. DR EnsemblBacteria; AAW90240; AAW90240; NGO_1612. DR PATRIC; 20336764; VBINeiGon24812_1927. DR HOGENOM; HOG000259834; -. DR OMA; IPPLDYD; -. DR OrthoDB; EOG6C8MTR; -. DR BioCyc; NGON242231:GI2G-1509-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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 195 197 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 217 218 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT ACT_SITE 83 83 Proton donor. {ECO:0000256|HAMAP- FT Rule:MF_02041, FT ECO:0000256|PIRSR:PIRSR006621-1}. FT BINDING 53 53 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 122 122 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 155 155 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 80 80 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 167 167 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 170 170 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 285 285 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 288 288 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. SQ SEQUENCE 319 AA; 36134 MW; D05BF1F5F32F5F76 CRC64; MLDWTDRHYR YLARQITRNA WLYSEMVNAG AIVYGDKDRF LMFNEGEQPV ALQLGGSDPS DLAKAAKAAE EYGYNEVNLN CGCPSPRVQK GAFGACLMNE VGLVADCLNA MHDAVGIPVT VKHRIGVDRQ TEYQTVADFV GTLRDKTACK TFIVHARNAW LDGLSPKENR DVPPLKYDYV YRLKQEFPEL EIIINGGITT NEAIAGHLQH VDGVMVGREA YHNPMVMREW DRLFYGDNRA PIEYADLVQR LYTYSQVQIQ AGRGTILRHI VRHSLGLMHG LKGARTWRRM LSDATLLKDN DGGLIFEAWK EVERANTRE // ID Q5F7T5_NEIG1 Unreviewed; 281 AA. AC Q5F7T5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89752.1}; GN ORFNames=NGO_1085 {ECO:0000313|EMBL:AAW89752.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89752.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89752.1; -; Genomic_DNA. DR RefSeq; WP_003701197.1; NC_002946.2. DR RefSeq; YP_208164.1; NC_002946.2. DR DNASU; 3281794; -. DR EnsemblBacteria; AAW89752; AAW89752; NGO_1085. DR GeneID; 3281794; -. DR KEGG; ngo:NGO1085; -. DR PATRIC; 20335420; VBINeiGon24812_1276. DR HOGENOM; HOG000122546; -. DR OMA; EMTYINE; -. DR OrthoDB; EOG644ZVD; -. DR BioCyc; NGON242231:GI2G-997-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003497; BRO_N_domain. DR Pfam; PF02498; Bro-N; 1. DR SMART; SM01040; Bro-N; 1. DR PROSITE; PS51750; BRO_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 106 Bro-N. {ECO:0000259|PROSITE:PS51750}. SQ SEQUENCE 281 AA; 30999 MW; 9E92D45D9611D2F9 CRC64; MNAVQVLNFQ QNSVRTVADN KGELWFLAND VCEILGYTNP RRTVDLHCKS RGVTKRYTPT TSGEQEMTYI NEPNLYRLII KSRKPAAEAF EEWVMETVLP AIRKTGGCQV GPKTTADDRT GLRQAVAALV GRKGIDYSSA YSMIHQRFNV ESIEDLPAGK LPEAVAYVHA LTLHTGLTGE VLDAPPKAEP KLPIDGNSLA DIAAMVYYGT WMIESGKDIS APLKQLGCRQ AVTMWTVWHE TRPILKRSAA ALEVLRGYAD KDASDRIAAC LEGIYGKATV R // ID Q5F8S1_NEIG1 Unreviewed; 469 AA. AC Q5F8S1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:AAW89416.1}; DE EC=4.2.3.1 {ECO:0000313|EMBL:AAW89416.1}; GN ORFNames=NGO_0689 {ECO:0000313|EMBL:AAW89416.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89416.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89416.1; -; Genomic_DNA. DR RefSeq; WP_003688790.1; NC_002946.2. DR RefSeq; YP_207828.1; NC_002946.2. DR ProteinModelPortal; Q5F8S1; -. DR EnsemblBacteria; AAW89416; AAW89416; NGO_0689. DR GeneID; 3281892; -. DR KEGG; ngo:NGO0689; -. DR PATRIC; 20334474; VBINeiGon24812_0809. DR HOGENOM; HOG000230745; -. DR KO; K01733; -. DR OMA; LAFKDYG; -. DR OrthoDB; EOG65BDJX; -. DR BioCyc; NGON242231:GI2G-656-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000313|EMBL:AAW89416.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 79 Thr_synth_N. {ECO:0000259|Pfam:PF14821}. FT DOMAIN 102 335 PALP. {ECO:0000259|Pfam:PF00291}. SQ SEQUENCE 469 AA; 51478 MW; 61CD57008AA2977D CRC64; MRYISTRGET AHKPFSEVLL MGLAPDGGLM LPEHYPQIGR ETLDKWRGLA YPELAFEIMC LFVTDIPEDD LRDILNRTYT EAAFGTKEIT PVRTLSDGIK IQALSNGPTL AFKDMAMQFL GNAFEYVLNK EGKKLNILGA TSGDTGSAAE YALRGKKGVN VFMLSPDGKM SAFQRAQMYS LQDGNIHNIA VKGMFDDCQD IVKAVQNDAA FKEKYHIGTV NSINWGRIVA QVVYYFAGYF NATSSNDETV SFCVPSGNFG NVCAGHIAKQ MGLPVRCLIV ATNENDVLDE FFKTGAYRPR NSAHTYVTSS PSMDISKASN FERFVFDLMD RDPQEINTLW AEVAAGKGFD LRFALDKVGG KYGFTSGKST HADRLATIRQ VYEQDKELID PHTANGVKVA REVREAGETV VCLETALAAK FDATIREAVG DVAIPRPAAL EGLENLPQRV QTVPNSADAV KGIIEQTLA // ID Q5F522_NEIG1 Unreviewed; 258 AA. AC Q5F522; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 54. DE SubName: Full=ABC transporter permease {ECO:0000313|EMBL:AAW90715.1}; GN ORFNames=NGO_2117 {ECO:0000313|EMBL:AAW90715.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90715.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90715.1; -; Genomic_DNA. DR RefSeq; WP_003690418.1; NC_002946.2. DR RefSeq; YP_209127.1; NC_002946.2. DR EnsemblBacteria; AAW90715; AAW90715; NGO_2117. DR GeneID; 3282803; -. DR KEGG; ngo:NGO2117; -. DR PATRIC; 20338081; VBINeiGon24812_2563. DR HOGENOM; HOG000255130; -. DR KO; K02066; -. DR OMA; MQASVDW; -. DR OrthoDB; EOG6RJV8Q; -. DR BioCyc; NGON242231:GI2G-2009-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU362044}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|RuleBase:RU362044}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 12 30 Helical. {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 46 72 Helical. {ECO:0000256|RuleBase:RU362044}. FT TRANSMEM 84 107 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; 27343 MW; F925336AAF82E215 CRC64; MNFIRSVGAK TLGLIQSFGS ITLFLLNILA KSGTAFARPR LSVRQVYFAG VLSVLIVAVS GLFVGMVLGL QGYTQLSKFK SADILGYMVA ASLLRELGPV LAAILFASSA GGAMTSEIGL MKTTGQLEAM NVMAVNPVAR VVAPRFWAGV FSMPLLASIF NVAGIFGAYL VGVSWLGLDS GIFWPQMQNN ITIHYDVING LIKSAAFGVA VTLIAVHQGF HCIPTSEGIL RASTRTVVSS ALTILAVDFI LTAWMFTD // ID Q5F5A0_NEIG1 Unreviewed; 193 AA. AC Q5F5A0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 81. 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 ORFNames=NGO_2029 {ECO:0000313|EMBL:AAW90637.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90637.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90637.1; -; Genomic_DNA. DR RefSeq; WP_010951385.1; NC_002946.2. DR RefSeq; YP_209049.1; NC_002946.2. DR ProteinModelPortal; Q5F5A0; -. DR EnsemblBacteria; AAW90637; AAW90637; NGO_2029. DR GeneID; 3282718; -. DR KEGG; ngo:NGO2029; -. DR PATRIC; 20337841; VBINeiGon24812_2444. DR HOGENOM; HOG000255194; -. DR KO; K00411; -. DR OMA; QPAYAQN; -. DR OrthoDB; EOG6RNQD9; -. DR BioCyc; NGON242231:GI2G-1930-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU004494}. FT TRANSMEM 12 38 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 85 189 Rieske. {ECO:0000259|PROSITE:PS51296}. SQ SEQUENCE 193 AA; 20648 MW; 1A72C02838ACEA3C CRC64; MDNQEINNGR RRFLTLATCG AGGVAALGVA TPFVASFFPS EKAKASGAAV EVDVSKIEAG QLLTAEWQGK PIWVLNRTDQ QLKDLKGLNG ELTDPNSDAE QQPEYAKNET RSIKPNILVA IGICTHLGCS PTFRPDIAPA DLGADWKGGF FCPCHGSKFD LAGRVYKGVP APTNLVVPPY KYLSDTTILV GED // ID Q5F7Z3_NEIG1 Unreviewed; 124 AA. AC Q5F7Z3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89694.1}; GN ORFNames=NGO_1011 {ECO:0000313|EMBL:AAW89694.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89694.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89694.1; -; Genomic_DNA. DR RefSeq; WP_010358353.1; NC_002946.2. DR RefSeq; YP_208106.1; NC_002946.2. DR EnsemblBacteria; AAW89694; AAW89694; NGO_1011. DR GeneID; 3282069; -. DR KEGG; ngo:NGO1011; -. DR PATRIC; 20335230; VBINeiGon24812_1183. DR OrthoDB; EOG635890; -. DR BioCyc; NGON242231:GI2G-937-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro. DR InterPro; IPR007685; RelA_SpoT. DR Pfam; PF04607; RelA_SpoT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 54 120 RelA_SpoT. {ECO:0000259|Pfam:PF04607}. SQ SEQUENCE 124 AA; 13767 MW; 1DD9872D0FD8B36F CRC64; MSDIDDFKSY LESHQAAFSA WGRFVAEEIQ NQLSNVISPV PVANFLKIEA KPGVKEISSA LAKIGRKNYT SPQTQMTDLV GVRFVALLAE HIQIVCEIIE SSSQWNAKVS KDFADEIQQN PKAI // ID Q5F7E4_NEIG1 Unreviewed; 97 AA. AC Q5F7E4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Antibiotic biosynthesis monooxygenase {ECO:0000313|EMBL:AAW89893.1}; GN ORFNames=NGO_1234 {ECO:0000313|EMBL:AAW89893.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89893.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89893.1; -; Genomic_DNA. DR RefSeq; WP_003689684.1; NC_002946.2. DR RefSeq; YP_208305.1; NC_002946.2. DR ProteinModelPortal; Q5F7E4; -. DR EnsemblBacteria; AAW89893; AAW89893; NGO_1234. DR GeneID; 3281870; -. DR KEGG; ngo:NGO1234; -. DR PATRIC; 20335785; VBINeiGon24812_1451. DR HOGENOM; HOG000145619; -. DR OMA; RMVFVEQ; -. DR OrthoDB; EOG6MSS9K; -. DR BioCyc; NGON242231:GI2G-1145-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Monooxygenase {ECO:0000313|EMBL:AAW89893.1}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89893.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 92 ABM. {ECO:0000259|PROSITE:PS51725}. SQ SEQUENCE 97 AA; 10833 MW; C1479FB166B3FD58 CRC64; MSNIKIVALV TVKPEYTETL AAQFKELVKA SRAEEGNISY NLHQEIGKPN RFVFVENWKS QAAIDEHNAS AHFQAFVQSV DGKTEALEIV LMNEVAV // ID Q5F7N9_NEIG1 Unreviewed; 137 AA. AC Q5F7N9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89798.1}; GN ORFNames=NGO_1131 {ECO:0000313|EMBL:AAW89798.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89798.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89798.1; -; Genomic_DNA. DR RefSeq; WP_010951196.1; NC_002946.2. DR RefSeq; YP_208210.1; NC_002946.2. DR EnsemblBacteria; AAW89798; AAW89798; NGO_1131. DR GeneID; 3282195; -. DR KEGG; ngo:NGO1131; -. DR PATRIC; 20335520; VBINeiGon24812_1326. DR OrthoDB; EOG6Q8JBG; -. DR BioCyc; NGON242231:GI2G-1043-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 137 AA; 14712 MW; CDC0B08D1C14CC57 CRC64; MRTHIRTCVY HDSGTKGSNT ASGISGTAAG AAEQAFFSAA KTANRSASAA SANAPPHPDK PKNGRKPMTF QGHNNRKKAG GYAEYITGGE LRLLQQTACR FKAALETAAW KHYVRAIKES EPVPDAEARR KRKKQAA // ID Q5F9Q2_NEIG1 Unreviewed; 310 AA. AC Q5F9Q2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985}; DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985}; GN ORFNames=NGO_0340 {ECO:0000313|EMBL:AAW89085.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89085.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L- CC cysteine + acetate. {ECO:0000256|RuleBase:RU003985}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU003985}; CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- CC synthase family. {ECO:0000256|RuleBase:RU003985}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89085.1; -; Genomic_DNA. DR RefSeq; WP_010951030.1; NC_002946.2. DR RefSeq; YP_207497.1; NC_002946.2. DR ProteinModelPortal; Q5F9Q2; -. DR SMR; Q5F9Q2; 1-307. DR EnsemblBacteria; AAW89085; AAW89085; NGO_0340. DR GeneID; 3281741; -. DR KEGG; ngo:NGO0340; -. DR PATRIC; 20333671; VBINeiGon24812_0413. DR HOGENOM; HOG000217394; -. DR KO; K01738; -. DR OMA; VKCRIGS; -. DR OrthoDB; EOG6Q2SP8; -. DR BioCyc; NGON242231:GI2G-320-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cysteine biosynthesis {ECO:0000256|RuleBase:RU003985}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU003985}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003985}. FT DOMAIN 7 293 PALP. {ECO:0000259|Pfam:PF00291}. SQ SEQUENCE 310 AA; 32727 MW; B89F25E89079C367 CRC64; MKIANSITEL IGNTPLVKLN RLTKGLKAEV AVKLEFFNPG SSVKDRIAEA MIEAAEKAGK INKNTVIVEA TSGNTGIGLA MVCAARGYKL AITMPESMSK ERKMLLRTFG AELILTPAAE GMAGAIAKAQ SLVDAHPDTY FMPRQFDNEA NPEVHRKTTA EEIWNDTDGK VDVFVAGVGT GGTITGVGEV LKKYKPEIEV CAVEAGASPV LSGGEKGPHP IQGIGAGFIP TVLNTKIYDS IAKVPNEAAF ETARAMAEKE GILAGISSGA AVWSALQLAK QPENEGKLIV VLLPSYGERY LSTPLFADLA // ID Q5F834_NEIG1 Unreviewed; 86 AA. AC Q5F834; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89653.1}; GN ORFNames=NGO_0967 {ECO:0000313|EMBL:AAW89653.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89653.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89653.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89653; AAW89653; NGO_0967. DR PATRIC; 20335126; VBINeiGon24812_1132. DR HOGENOM; HOG000071274; -. DR OMA; MPSERTN; -. DR OrthoDB; EOG68SW6P; -. DR BioCyc; NGON242231:GI2G-895-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 9880 MW; B6AF83C99B2AE671 CRC64; MPSERTNSLQ TAFCRQTDLL KPTFFIISDK LLCKNPKIQN HRKLSKKQKP SAVVPAKAGI QTRKPQKFIG KTETRKQRTE FPPAQE // ID Q5F6U0_NEIG1 Unreviewed; 598 AA. AC Q5F6U0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE SubName: Full=Peptidase M24 {ECO:0000313|EMBL:AAW90097.1}; GN ORFNames=NGO_1456 {ECO:0000313|EMBL:AAW90097.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90097.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90097.1; -; Genomic_DNA. DR RefSeq; WP_010951270.1; NC_002946.2. DR RefSeq; YP_208509.1; NC_002946.2. DR ProteinModelPortal; Q5F6U0; -. DR EnsemblBacteria; AAW90097; AAW90097; NGO_1456. DR GeneID; 3281686; -. DR KEGG; ngo:NGO1456; -. DR PATRIC; 20336337; VBINeiGon24812_1717. DR HOGENOM; HOG000255711; -. DR KO; K01262; -. DR OMA; YRPGKWG; -. DR OrthoDB; EOG6QZMPK; -. DR BioCyc; NGON242231:GI2G-1362-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU003652}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 64934 MW; 79C8E7DC2CDBF5FF CRC64; MNTVSNYLSA LREAMKAQGL DALVIPSADP HLSEYLPEHW QARRELSGFT GSVGTFVVTA DEAGVWVDSR YWEQAAKQLS GSGIELQKSG QVPPYNEWLA ANLPENAAVG IPSDMVSLTG KRTLAQSLAA KNIRIQHPDD LLDQVWTSRP AIPAETVFIH DHAYVSETAA EKLARVRAVM AEKGADYHLV SSLDDIAWLT NLRGSDVPFN PVFVSFLLIG KDSAVLFTEQ CRLNAEAAAA LQTAGITVEP YAQVADKLAQ IGGALLIEPN KTAVSTLVRL PESARLIEGI NPSTFFKSVK SEADIARIRE AMEQDGAALC GFFAEFEDII GKGGSLTEID VDTMLYRHRS ARPGFVSLSF DTIAGFNANG ALPHYSATPE SHSTISGNGL LLIDSGAQYK GGTTDITRVV PVGTPTAEQK RDNTLVLKAH IALAEAVFPE NIPSPLIDAI CRKPLWQAQC DYGHGTGHGV SYFLNVHEGP QRIAFAAPAT PETAMKKGMV TSIEPGLYRP GKWGIRIENL AANQAVADPQ ETEFGSFLCF ETLTLCPIDT RLMDTALMTD GEIDWVNRYH AEVRRRLEPL TEGAAKAWLI KRTEPLAR // ID Q5F8K6_NEIG1 Unreviewed; 512 AA. AC Q5F8K6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 57. DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:AAW89481.1}; GN ORFNames=NGO_0766 {ECO:0000313|EMBL:AAW89481.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89481.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89481.1; -; Genomic_DNA. DR RefSeq; WP_003697101.1; NC_002946.2. DR RefSeq; YP_207893.1; NC_002946.2. DR ProteinModelPortal; Q5F8K6; -. DR EnsemblBacteria; AAW89481; AAW89481; NGO_0766. DR GeneID; 3282473; -. DR KEGG; ngo:NGO0766; -. DR PATRIC; 20334682; VBINeiGon24812_0913. DR HOGENOM; HOG000218965; -. DR KO; K03770; -. DR OMA; PEMEKQM; -. DR OrthoDB; EOG6M9DS4; -. DR BioCyc; NGON242231:GI2G-721-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000313|EMBL:AAW89481.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 230 372 PpiC. {ECO:0000259|Pfam:PF13145}. SQ SEQUENCE 512 AA; 56714 MW; 4AF6DB1DA430567F CRC64; MFHSIEKYRT PAQVLLGLIA LTFVGFGVST VSHPGADYIV QVGDEKISEH SINNAMQNEQ ADGGSPWRDA VFQSLLQRAY LKQGAKLMGI SVSSEQIKQM IVDDPNFHDA NGKFSHALLS QYLSQRHMSE DQFVEEIRDQ FALQNLVSLV QNGVLVGDAQ AEQLIRLTQV NRTIRSHTFN PDEFIAQVKA SEADLQKFYN ANKKDYLLPQ AVKLEYVALN LKDFADKQTV SETEVKNAFE ERVARLPAHE AKPSFEQEKA AVENELKMKK AVADFNKAKE KLGDDAFNHP SSLAEAAKNS GLKVETQETW LSRQDAQMSG MPENLINAVF SDDVLKKKHN SEVLTINSET AWVVRAKEVR EEKNLLFEEA KDAVRQAYIR TEAAKLAENK AKEVLTQLNG GKAVDVKWSE VSVLGAQQAR QSMPPEAYAE LLKAKPANGK PAYVRLTGLP APVIVEAQAV TPPEDIAAQL PPAKQALAQQ QSANTFDLLI RYFNGKIKQT KGAQSVDNGD GQ // ID Q5FA80_NEIG1 Unreviewed; 457 AA. AC Q5FA80; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 76. DE SubName: Full=RNA helicase {ECO:0000313|EMBL:AAW88907.1}; GN ORFNames=NGO_0149 {ECO:0000313|EMBL:AAW88907.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88907.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88907.1; -; Genomic_DNA. DR RefSeq; WP_003687439.1; NC_002946.2. DR RefSeq; YP_207319.1; NC_002946.2. DR ProteinModelPortal; Q5FA80; -. DR EnsemblBacteria; AAW88907; AAW88907; NGO_0149. DR GeneID; 3281290; -. DR KEGG; ngo:NGO0149; -. DR PATRIC; 20333219; VBINeiGon24812_0192. DR HOGENOM; HOG000268807; -. DR OMA; YMVPRGW; -. DR OrthoDB; EOG6GBMBM; -. DR BioCyc; NGON242231:GI2G-137-MONOMER; -. DR Proteomes; UP000000535; 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:AAW88907.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000256|RuleBase:RU000492, ECO:0000313|EMBL:AAW88907.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAW88907.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000492, KW ECO:0000313|EMBL:AAW88907.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 50873 MW; D3405C817EE674C9 CRC64; MSNPFSSLGL GTELVSALTA QGYENPTPIQ AAAIPKALAG HDLLAAAQTG TGKTAAFMLP SLERLKRYAT ASTSPAMHPV RMLVLTPTRE LADQIDQNVQ GYIKNLPLRH TVLFGGVNMD KQTADLRAGC EIVVATVGRL LDHVKQKNIS LNKAEIVVLD EADRMLDMGF IDDIRKIMQM LPRQRQTLLF SATFSAPIRK LAQDFMNAPE TVEVAAQNTT NANVEQHIIA VDTFQKRNLL ERLIVDLHMN QVIVFCKTKQ SVDRVTRELV RRNLSAQAIH GDRSQQSRLE TLNAFKDGSL RVLVATDIAA RGLDIAELPF VINYEMPAQP EDYIHRIGRT GRAGADGVAI SLMDESEQKM FEAIKELTGN KLLIERIEGF EPRWWEQEGS KPEKTETSEP RQRNRYESAR AQREKNTRPE TTANDAGAAC GKIAGRSRRS RRGHRTCALL QPRYGVK // ID Q5F800_NEIG1 Unreviewed; 119 AA. AC Q5F800; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89687.1}; GN ORFNames=NGO_1004 {ECO:0000313|EMBL:AAW89687.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89687.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89687.1; -; Genomic_DNA. DR RefSeq; WP_003691015.1; NC_002946.2. DR RefSeq; YP_208099.1; NC_002946.2. DR EnsemblBacteria; AAW89687; AAW89687; NGO_1004. DR GeneID; 3282187; -. DR KEGG; ngo:NGO1004; -. DR PATRIC; 20335210; VBINeiGon24812_1173. DR OrthoDB; EOG63588F; -. DR BioCyc; NGON242231:GI2G-930-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010144; CRISPR-assoc_prot_Csd1-typ. DR Pfam; PF09709; Cas_Csd1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 13480 MW; 7F12959C1924F5EA CRC64; MFTPSDDEQE SAKIFNVLEQ IGKGRPLQEI APELSPNTRF YILGLAPNAA RISVRFWLDT TFGQLAENLA HHWQDLALEP CAWKTPPSIW RLLLQTAVLG KSENIQRLGN RCLPETQNP // ID Q5F977_NEIG1 Unreviewed; 1015 AA. AC Q5F977; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Tail protein {ECO:0000313|EMBL:AAW89260.1}; GN ORFNames=NGO_0522 {ECO:0000313|EMBL:AAW89260.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89260.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89260.1; -; Genomic_DNA. DR RefSeq; WP_010951073.1; NC_002946.2. DR RefSeq; YP_207672.1; NC_002946.2. DR ProteinModelPortal; Q5F977; -. DR EnsemblBacteria; AAW89260; AAW89260; NGO_0522. DR GeneID; 3282926; -. DR KEGG; ngo:NGO0522; -. DR PATRIC; 20334090; VBINeiGon24812_0617. DR HOGENOM; HOG000071308; -. DR OMA; ETEYLAV; -. DR OrthoDB; EOG6CZQG1; -. DR BioCyc; NGON242231:GI2G-500-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR013491; Caudovirus_tape_meas_N. DR TIGRFAMs; TIGR02675; tape_meas_nterm; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 433 456 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 903 924 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 1015 AA; 108310 MW; 7DDD5D64D01777DB CRC64; MSDLEAKVRI TVENHTKQGF DSAAADADKA AEKMRSSGDN AAKGFKAAID SMHETMRNLH ADVKAGFEAA GNQAQQASEK VRAEVGKIGS GLSGLTKLLA GLATADFAKS VLDTADAMQS INSQVRQVTS SETEYLAVQQ QLLDTANRTR ASLESTANLY VSTSRALKDY GYTQQEILKF TEAANNAMTI GGVGAQQQAA ALMQLSQALG SGVLQGDEFK SISEAAPILL DTIAEYMGKS RDEIKKLGSE GKLTADVIFK AISGASEKFG EQAAKMPVTM GQALTVFSNN WQSMVSKLLN DSGTMSGIAA VIKLIADNLN LVVPIVAGFA VAVAAAVAPT LALNLALLAN PFGIIAVAIG TVVGLIAKFG DEIDVFGGGW SNLSDVIRAV WQIITETVGE AVGTVKSWFD GLTGRLNEGA GGWPSLFGRV MSVISSAIGA YVNVYINIFA TGWMLIKEAA NDMPQFFANL GKAIGNVFIS AIERMINKAV GMINSMIDFA NKAASMAGIS GIGKLNKVRM GRMDDGGLGE RIHDSLTKDR AGAMANAVRE RAADIHEADA LKGRGGGGHA KTARKKPGAN QGGGKGGKSR SGGPGAAKDP MQAWEGEIKA RKLAHREMQR ETLAHQEWDL AREAEYWRAK LATVDANGKT GVKIREKILM LEDQLSKQST EAKMNQAAEW EKLDKHKLEM EKDAADQALA DGRISQLERL DLEIEFENRR YRIAYDALQE RIALAEQDPA YSQAAIGKLK AQMGELGRGH ERTQAKNEGK RENQRRKDAP NVMEMLQDGG RNVWQEAQQQ MGQAFTAMLA RAQNFRQAMN GFFKSMGQTF IQEMVTKPLT GLMRRMVQES AIYKMIFGTK ETLETAAAAK TAATKATETT AVVSSNAVQA ASGAAASQAH IPYVGPILAV AAMAAMMSAV MGLMGGGGGS QTTTTTTRIP SAAGGWDIPA GINPLTQLHE NEMVLPAEHA QTIREMADQQ GGGSTVIINS TGGDFIHKND LAKLLKQMKR DFKFV // ID Q5F919_NEIG1 Unreviewed; 90 AA. AC Q5F919; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89318.1}; GN ORFNames=NGO_0587 {ECO:0000313|EMBL:AAW89318.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89318.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89318.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89318; AAW89318; NGO_0587. DR HOGENOM; HOG000071302; -. DR OMA; SAEMPGN; -. DR OrthoDB; EOG6T1WSS; -. DR BioCyc; NGON242231:GI2G-558-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 90 AA; 9935 MW; C0FF4DB3D46C213B CRC64; MQKISFNLLK PTNSLKIGKY RPGLNGAPHI PMPSLRYLPA SAEMPGNNIH PAKSETTHPV AGRVKPPRKA SAIRKTNRLR GLHPKGRIVR // ID Q5F4W5_NEIG1 Unreviewed; 44 AA. AC Q5F4W5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90772.1}; GN ORFNames=NGO_2179 {ECO:0000313|EMBL:AAW90772.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90772.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90772.1; -; Genomic_DNA. DR RefSeq; WP_002214732.1; NC_002946.2. DR RefSeq; YP_209184.1; NC_002946.2. DR EnsemblBacteria; AAW90772; AAW90772; NGO_2179. DR GeneID; 3282746; -. DR KEGG; ngo:NGO2179; -. DR PATRIC; 20338220; VBINeiGon24812_2632. DR OrthoDB; EOG6W19TG; -. DR BioCyc; NGON242231:GI2G-2066-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 44 AA; 4942 MW; EBCCF374C9B906CD CRC64; MPQVACSDRR GIRAGFIPDG RAASPKVQTA LYRNRWEIKG KRAI // ID Q5FAC5_NEIG1 Unreviewed; 207 AA. AC Q5FAC5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Cytochrome C {ECO:0000313|EMBL:AAW88862.1}; GN ORFNames=NGO_0101 {ECO:0000313|EMBL:AAW88862.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88862.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88862.1; -; Genomic_DNA. DR RefSeq; WP_003687359.1; NC_002946.2. DR RefSeq; YP_207274.1; NC_002946.2. DR ProteinModelPortal; Q5FAC5; -. DR EnsemblBacteria; AAW88862; AAW88862; NGO_0101. DR GeneID; 3282451; -. DR KEGG; ngo:NGO0101; -. DR PATRIC; 20333101; VBINeiGon24812_0134. DR HOGENOM; HOG000221626; -. DR OMA; IAACAGC; -. DR OrthoDB; EOG6JDWB3; -. DR BioCyc; NGON242231:GI2G-91-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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_5004256093. 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; 22017 MW; E72AFE7BCB3DCFCD CRC64; MRRLTLLAFV LAAGAVSASP KADVEKGKQV AATVCAACHA ADGNSGIAMY PRLAAQHTAY IYHQTIGIRD GKRTHGSAAV MKPVVMNLSD QDILNVSAFY AKQQPKSGEA NPKENPELGA KIYRGGLSDK KVPACMSCHG PSGAGMPGGG SEIQAYPRLG GQHQAYIVEQ MNAYKSGQRK NTIMEDIANR MSEEDLKAVA NFIQGLR // ID Q5F5L5_NEIG1 Unreviewed; 347 AA. AC Q5F5L5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AAW90522.1}; GN ORFNames=NGO_1908 {ECO:0000313|EMBL:AAW90522.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90522.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90522.1; -; Genomic_DNA. DR RefSeq; WP_010951368.1; NC_002946.2. DR RefSeq; YP_208934.1; NC_002946.2. DR ProteinModelPortal; Q5F5L5; -. DR EnsemblBacteria; AAW90522; AAW90522; NGO_1908. DR GeneID; 3282267; -. DR KEGG; ngo:NGO1908; -. DR PATRIC; 20337536; VBINeiGon24812_2295. DR HOGENOM; HOG000008425; -. DR KO; K02669; -. DR OMA; PIEYVFP; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NGON242231:GI2G-1811-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 193 207 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 347 AA; 37999 MW; 62B15FBAD4450CAD CRC64; MQITDLLAFG AKNKASDLHL SSGISPMIRV HGDMRRINLP EMSAEEVGNM VTSVMNDHQR KIYQQNLEVD FSFELPNVAR FRVNAFNTGR GPAAVFRTIP STVLSLEELK APSIFQKIAE SPRGMVLVTG PTGSGKSTTL AAMINYINET QPAHILTIED PIEFVHQSKK SLINQRELHQ HTLSFANALS SALREDPDVI LVGEMRDPET IGLALTAAET GHLVFGTLHT TGAAKTVDRI VDVFPAGEKE MVRSMLSESL TAVISQNLLK THDGDGRVAS HEILIANPAV RNLIRENKIT QINSVLQTGR ASGMQTMDQS LQSLVRQGLI APEATRRRAQ NSESMSF // ID Q5F9G5_NEIG1 Unreviewed; 45 AA. AC Q5F9G5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89172.1}; GN ORFNames=NGO_0429 {ECO:0000313|EMBL:AAW89172.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89172.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89172.1; -; Genomic_DNA. DR RefSeq; WP_003690878.1; NC_002946.2. DR RefSeq; YP_207584.1; NC_002946.2. DR EnsemblBacteria; AAW89172; AAW89172; NGO_0429. DR GeneID; 3281923; -. DR KEGG; ngo:NGO0429; -. DR PATRIC; 20333873; VBINeiGon24812_0514. DR HOGENOM; HOG000218887; -. DR OrthoDB; EOG6M3PM7; -. DR BioCyc; NGON242231:GI2G-407-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 5391 MW; 2F8C5B2CE8181BF3 CRC64; MELKYCNREA KASVVTFTIY FIILISSKNK IQDYTYRQSF LDCFV // ID Q5F819_NEIG1 Unreviewed; 94 AA. AC Q5F819; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89668.1}; GN ORFNames=NGO_0982 {ECO:0000313|EMBL:AAW89668.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89668.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89668.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89668; AAW89668; NGO_0982. DR BioCyc; NGON242231:GI2G-910-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10987 MW; CB10EC8544441223 CRC64; MQCKFFTTLS KTIPTHLPTS PICLNKSYKI LNYINLYNIY PYRIFNSKTV LQDLSIRPPE NFSFKPFSHL YDIAIPYSMV HNYANSAMNF QPGL // ID Q5F5E7_NEIG1 Unreviewed; 99 AA. AC Q5F5E7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=XRE family transcriptional regulator {ECO:0000313|EMBL:AAW90590.1}; GN ORFNames=NGO_1982 {ECO:0000313|EMBL:AAW90590.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90590.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90590.1; -; Genomic_DNA. DR RefSeq; WP_010951376.1; NC_002946.2. DR RefSeq; YP_209002.1; NC_002946.2. DR ProteinModelPortal; Q5F5E7; -. DR EnsemblBacteria; AAW90590; AAW90590; NGO_1982. DR GeneID; 3282642; -. DR KEGG; ngo:NGO1982; -. DR PATRIC; 20337731; VBINeiGon24812_2392. DR HOGENOM; HOG000218711; -. DR OMA; QIDINKV; -. DR OrthoDB; EOG6FV87D; -. DR BioCyc; NGON242231:GI2G-1880-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 99 AA; 11436 MW; 1FE2C96AFBC4D7B9 CRC64; MKIFENIEDV KAIRKKTGMN QIDFWGKVGV TQSGGSRYET GRKMPKPVRE LLRLVHIECL DLAKVNKKDM EIAALLKKHH PDLYAELSKQ TKSERKKQS // ID Q5F885_NEIG1 Unreviewed; 259 AA. AC Q5F885; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW89602.1}; GN ORFNames=NGO_0904 {ECO:0000313|EMBL:AAW89602.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89602.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89602.1; -; Genomic_DNA. DR RefSeq; WP_003702609.1; NC_002946.2. DR RefSeq; YP_208014.1; NC_002946.2. DR EnsemblBacteria; AAW89602; AAW89602; NGO_0904. DR GeneID; 3281130; -. DR KEGG; ngo:NGO0904; -. DR PATRIC; 20334989; VBINeiGon24812_1064. DR HOGENOM; HOG000262113; -. DR KO; K18928; -. DR OMA; NSCLMHI; -. DR OrthoDB; EOG6GTZM6; -. DR BioCyc; NGON242231:GI2G-844-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR004017; Cys_rich_dom. DR Pfam; PF02754; CCG; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 19 100 CCG. {ECO:0000259|Pfam:PF02754}. FT DOMAIN 146 230 CCG. {ECO:0000259|Pfam:PF02754}. SQ SEQUENCE 259 AA; 28340 MW; 160EFD4AC81E7457 CRC64; MSATIPPKII RYDSNPTDVY FFGTCVLDLF MPEAGMDAIA LIEQQGIRVH FPMAQSCCGQ PAYSSGHPTE AFDVAKVQLD LFPENWPIVV PSGSCGGMMK HHWPTLFKNT EYESKAVDCA NRIIEFTHFL LAIGYKPEDK GEPVKVAVHT SCAARREMNV HLSGWQLIDG MENVERIVHD HESECCGFGG TFSVKQADIS GAMVTDKVAA LKETGATEII SADCGCMMNI GGKIAKDEPD MPRPKHIASF LLERTGGKV // ID Q5F5N9_NEIG1 Unreviewed; 280 AA. AC Q5F5N9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=PhnO {ECO:0000313|EMBL:AAW90498.1}; GN ORFNames=NGO_1878 {ECO:0000313|EMBL:AAW90498.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90498.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90498.1; -; Genomic_DNA. DR RefSeq; WP_003705351.1; NC_002946.2. DR RefSeq; YP_208910.1; NC_002946.2. DR ProteinModelPortal; Q5F5N9; -. DR EnsemblBacteria; AAW90498; AAW90498; NGO_1878. DR GeneID; 3282333; -. DR KEGG; ngo:NGO1878; -. DR PATRIC; 20337452; VBINeiGon24812_2257. DR HOGENOM; HOG000218668; -. DR OMA; QNDPANE; -. DR OrthoDB; EOG6SBT62; -. DR BioCyc; NGON242231:GI2G-1782-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 136 280 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 280 AA; 31610 MW; 577B907CDF12F84A CRC64; MLICNPYEVV IHGTTSSGKI FRPGDWAERL CGILSSFTKD NRLSYSKWVR PMLVDNIRCV AVDKKLETDN PQMFRFLMDF AADNDLRVID CKALLEEREQ GGQNDPANER VLLAQAIEEK HAAEKTQEQT ASGASYVLRE IGADDTATAF AALSVLRSSL TDIGRFTEQI NKIQRPQGYR LLGIFEECKH NAVAVCGFRE ACTLAGGRHI HIDDIVTLPQ SRRKGYASRL LEEVRKIGAE TGVTKIHLNV HVNHDRTDAH RLYFKNGFEI CAYHFRCDPK // ID Q5F516_NEIG1 Unreviewed; 127 AA. AC Q5F516; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Thioesterase {ECO:0000313|EMBL:AAW90721.1}; GN ORFNames=NGO_2123 {ECO:0000313|EMBL:AAW90721.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90721.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90721.1; -; Genomic_DNA. DR RefSeq; WP_003687109.1; NC_002946.2. DR RefSeq; YP_209133.1; NC_002946.2. DR ProteinModelPortal; Q5F516; -. DR EnsemblBacteria; AAW90721; AAW90721; NGO_2123. DR GeneID; 3282797; -. DR KEGG; ngo:NGO2123; -. DR PATRIC; 20338093; VBINeiGon24812_2569. DR HOGENOM; HOG000004132; -. DR KO; K12500; -. DR OMA; ANININY; -. DR OrthoDB; EOG6JQH7N; -. DR BioCyc; NGON242231:GI2G-2015-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 127 AA; 14292 MW; 718D338F923BEBA8 CRC64; MKLTVRNYHL DGYGHVNNAR YLEFLEEARW AFFEKRGLMH ELAGLILIVA RIDIRYSRPA VEGDVLQFSC RLKTPGMRRI VLTQTITLPN GKTAAEADIT LMPVHAATQR TVSLPATLAR ALEALSE // ID Q5F7S6_NEIG1 Unreviewed; 398 AA. AC Q5F7S6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89761.1}; GN ORFNames=NGO_1094 {ECO:0000313|EMBL:AAW89761.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89761.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89761.1; -; Genomic_DNA. DR RefSeq; WP_010951181.1; NC_002946.2. DR RefSeq; YP_208173.1; NC_002946.2. DR EnsemblBacteria; AAW89761; AAW89761; NGO_1094. DR GeneID; 3281126; -. DR KEGG; ngo:NGO1094; -. DR PATRIC; 20335440; VBINeiGon24812_1286. DR HOGENOM; HOG000071255; -. DR OMA; ANYEAGP; -. DR OrthoDB; EOG6S26M3; -. DR BioCyc; NGON242231:GI2G-1006-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 398 AA; 43597 MW; 8136B698E634467D CRC64; MGLFEPSAGD FWEMKEKEEK EKARKGAEER ERAAAQAHRA DAVRRTVANY EAGPARYRNV MDLSRNNIED GARRLRRAGA FERGADAGLG FSGGDKALSP DARAGADFAR RDTRPTDAGG RTPPPLGFDG NVYRGGKPVR DFDAQRPLVS AGPDALSPEE RELYKRATTP YAGALNGQLT AAQLNAARGI VAEHNKNAAV RELGRERLAA AAAENAANRE AVLQKGRFDA AVKANEGALN REMAQRNADR AFDVQQAELG MKRQGFEMKR EADALELEDR KRIADLTRAY GFAKSDGQRG EIARQIDALN GKFERQGEKG FDPNVFKTVS YEVADPDTGL TAKREGIVDL RTGKPLDVEF AGEREKRYAA LGFKPNGQKT AGGKIIYENE KGEKRVEQ // ID Q5F9B4_NEIG1 Unreviewed; 453 AA. AC Q5F9B4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 65. DE SubName: Full=DNA helicase {ECO:0000313|EMBL:AAW89223.1}; GN ORFNames=NGO_0485 {ECO:0000313|EMBL:AAW89223.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89223.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89223.1; -; Genomic_DNA. DR RefSeq; WP_003689132.1; NC_002946.2. DR RefSeq; YP_207635.1; NC_002946.2. DR ProteinModelPortal; Q5F9B4; -. DR EnsemblBacteria; AAW89223; AAW89223; NGO_0485. DR GeneID; 3282962; -. DR KEGG; ngo:NGO0485; -. DR PATRIC; 20334006; VBINeiGon24812_0575. DR HOGENOM; HOG000113196; -. DR OMA; RPHKIIF; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; NGON242231:GI2G-463-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR019889; DNA_helicase_DnaB-like_phg. 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 SUPFAM; SSF48024; SSF48024; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03600; phage_DnaB; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAW89223.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA replication {ECO:0000256|SAAS:SAAS00435671}; KW DNA-binding {ECO:0000256|SAAS:SAAS00435659}; KW Helicase {ECO:0000313|EMBL:AAW89223.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89223.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW89223.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 179 439 SF4 helicase. FT {ECO:0000259|PROSITE:PS51199}. SQ SEQUENCE 453 AA; 49487 MW; 1AC5AC6BEF5475B9 CRC64; MNRIEETEAV QSLASVGAEQ NILGGILIEP TAIARCAILT PEKFYQAQHR IIFRALLDMA AANEPIDIIT LNDKLEARGE AENAGGLAYL IDLNQNTPSA KNISRYVGIV NDRFVERGLL KASAAIEKIA VSKDGGTVAE KLSKAADELA AAGKDAVKRE TKTFGQTVED LIGGLDKRLD GVRFGLPTGL MKLDGMTGGL PDGNLIVIAA RPSMGKTVLA ENIARFALKQ GKAVHFQSYE MSAVELARRG MAAECNIPMQ NLKTGNLTQS DYANMPIYVS QAKEWKFDVN CDLLNVDELC FLAKEKKLTT GLDLLVVDHL HIMPRAGRDE VAELGNISRR LKNLAAELNI PVVLVAQLNR GNTKQADKRP NMADIRGSGA IEQDANIIIM PHRESYYDGN ENPSIAELII AKNRDGETGT VVCGWKGQFM KFEEEPDLAW QAPKHDEYDP YSV // ID Q5F5B6_NEIG1 Unreviewed; 243 AA. AC Q5F5B6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 85. DE SubName: Full=Glutamine ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90621.1}; GN ORFNames=NGO_2013 {ECO:0000313|EMBL:AAW90621.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90621.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90621.1; -; Genomic_DNA. DR RefSeq; WP_003686921.1; NC_002946.2. DR RefSeq; YP_209033.1; NC_002946.2. DR ProteinModelPortal; Q5F5B6; -. DR SMR; Q5F5B6; 1-241. DR EnsemblBacteria; AAW90621; AAW90621; NGO_2013. DR GeneID; 3282699; -. DR KEGG; ngo:NGO2013; -. DR PATRIC; 20337807; VBINeiGon24812_2427. DR KO; K02028; -. DR OMA; TDWRQVR; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1914-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90621.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90621.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 238 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 243 AA; 26784 MW; 2FA20941B49766D3 CRC64; MALLSIRKLH KQYGSVTAIQ SLDLDLEKGE VIVLLGPSGC GKSTLLRCVN GLEPHQGGSI VMDGVGEFGK DVSWQTARQK VGMVFQSYEL FAHMTVIENI LLGPVKVQNR DRAEAEAQAG KLLERVGLLD RKNAYPRELS GGQKQRIAIV RALCLNPEVI LLDEITAALD PEMVREVLEV VLELAREGMS MLIVTHEMGF ARKVADRIVF MDKGGIVESS DPETFFSAPK SERARQFLAG MDY // ID Q5F962_NEIG1 Unreviewed; 170 AA. AC Q5F962; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 67. DE SubName: Full=Protein tyrosine phosphatase {ECO:0000313|EMBL:AAW89275.2}; GN ORFNames=NGO_0541 {ECO:0000313|EMBL:AAW89275.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89275.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89275.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F962; -. DR EnsemblBacteria; AAW89275; AAW89275; NGO_0541. DR PATRIC; 20334132; VBINeiGon24812_0638. DR HOGENOM; HOG000273094; -. DR OMA; YRGCEAL; -. DR OrthoDB; EOG6MH5JB; -. DR BioCyc; NGON242231:GI2G-515-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 167 LMWPc. {ECO:0000259|SMART:SM00226}. SQ SEQUENCE 170 AA; 19068 MW; 600E87D1853C7362 CRC64; MPSERVSASG GIALEQGWDM KKPKILFVCL GNICRSPMAE YILRRRAAEA GIPLETDSAG TSGWHDGEDM HRETAKILKK YGIDASGFTS RKIRQSDATA FDYIIAMDGK NLSELEKTFG RRPEKIFKLT DLIPESGYDH VPDPWYMGDF EETYRLADAG CRALLEKISK // ID Q5F7X5_NEIG1 Unreviewed; 242 AA. AC Q5F7X5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89712.1}; GN ORFNames=NGO_1040 {ECO:0000313|EMBL:AAW89712.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89712.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89712.1; -; Genomic_DNA. DR RefSeq; WP_003690990.1; NC_002946.2. DR RefSeq; YP_208124.1; NC_002946.2. DR EnsemblBacteria; AAW89712; AAW89712; NGO_1040. DR GeneID; 3282439; -. DR KEGG; ngo:NGO1040; -. DR PATRIC; 20335302; VBINeiGon24812_1217. DR HOGENOM; HOG000220756; -. DR OMA; ARYGSHM; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NGON242231:GI2G-957-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 242 AA; 27809 MW; 9E16F09AC95FCD0B CRC64; MSREINAGGH HFLYGGISRG VHYWDNKDFS EQSLRLSFGH QNRSVTRSFG TVPFVGQNLL GGSRYNFAGG FNADFSRRLG ERWRLTLNAG NMWKHYQEDR TAARYGSHMP LAGATLMYSA PKDRLLYGGA DWPHDMTKEA EQASVRKGLR VGAVKTFDGG LGLRANLRYT RRTFDAPGTI VYRFPRKDHE YQANLSLRHD KISWKGFTPQ LNFRYLKIGS NMKSFYTRKN TQIFMSVEKD FK // ID Q5F940_NEIG1 Unreviewed; 529 AA. AC Q5F940; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137}; DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137}; GN ORFNames=NGO_0564 {ECO:0000313|EMBL:AAW89297.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89297.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89297.1; -; Genomic_DNA. DR RefSeq; WP_010357738.1; NC_002946.2. DR RefSeq; YP_207709.1; NC_002946.2. DR ProteinModelPortal; Q5F940; -. DR SMR; Q5F940; 2-82, 103-183, 290-529. DR EnsemblBacteria; AAW89297; AAW89297; NGO_0564. DR GeneID; 3282469; -. DR KEGG; ngo:NGO0564; -. DR PATRIC; 20334190; VBINeiGon24812_0667. DR HOGENOM; HOG000281562; -. DR KO; K00627; -. DR OMA; GKEFEPR; -. DR OrthoDB; EOG610413; -. DR BioCyc; NGON242231:GI2G-537-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Glycolysis {ECO:0000256|RuleBase:RU361137}; KW Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU361137}. FT DOMAIN 3 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. FT DOMAIN 104 178 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 529 AA; 54693 MW; 7BE68DD1B79450BF CRC64; MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA DAAGVVKEVK VKVGDKISEG GVILTVETGA AAAEAAPAAA AEAQPAPAAA GGATVQVAVP DIGGHTDVDV IAVEIKVGDT VAEDDTLITL ETDKATMDVP CTAAGVVKAV FLKVGDKVSE GSAIIEVETA GSAAAAPAPA AQAAAPAAVP TSAAPAAVPT SASPAAAKID EAAFAKAHAG PSARKLAREL GVDLGQVKGS GLKGRIMGDD IKAFVKSVMQ GGAAKPAAAG ASLGGGLDLL PWPKVDFSKF GNVEVKELSR IKKISGQNLS RNWVVIPHVT VHEEADMTEL EEFRKQLNKE WEREGVKLSP LAFIIKASVS ALKAFPEFNA SLDGDNLVLK NYFNIGFAAD TPNGLVVPVI KDVDQKGLKQ ISQELTELSK KAREGKLKPQ EMQGACFTIS SLGGIGGTGF TPIVNAPEVA ILGVCKSQIK PVWNGKEFAP RLMCPLSLSF DHRVIDGAAG MRFTVFLANL LKDFRRITL // ID Q5F5P9_NEIG1 Unreviewed; 199 AA. AC Q5F5P9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90488.1}; GN ORFNames=NGO_1868 {ECO:0000313|EMBL:AAW90488.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90488.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90488.1; -; Genomic_DNA. DR RefSeq; WP_003690128.1; NC_002946.2. DR RefSeq; YP_208900.1; NC_002946.2. DR EnsemblBacteria; AAW90488; AAW90488; NGO_1868. DR GeneID; 3282358; -. DR KEGG; ngo:NGO1868; -. DR PATRIC; 20337430; VBINeiGon24812_2246. DR HOGENOM; HOG000266169; -. DR OMA; WKRFTFT; -. DR OrthoDB; EOG65XN25; -. DR BioCyc; NGON242231:GI2G-1772-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025500; DUF4390. DR Pfam; PF14334; DUF4390; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 199 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256578. SQ SEQUENCE 199 AA; 21912 MW; A53A189E3FDE8095 CRC64; MAFITRLFKS IKQWLVLLPI LSVLPDAAAE GIAATRAEAR ITDGGRLSIS SRFQTELPDQ LQQALRRGVP LNFTLSWQLS APTIASYRFK LGQLIGDDDN IDYKLSFHPL TNRYRVTVGA FSTDYDTLDA ALRATGAVAN WKVLNKGALS GAEAGETKAE IRLTLSTSKL PKPFQINALT SQNWHLDSGW KPLNIIGNK // ID Q5F7S2_NEIG1 Unreviewed; 424 AA. AC Q5F7S2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Terminase {ECO:0000313|EMBL:AAW89765.1}; GN ORFNames=NGO_1098 {ECO:0000313|EMBL:AAW89765.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89765.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89765.1; -; Genomic_DNA. DR RefSeq; WP_010951185.1; NC_002946.2. DR RefSeq; YP_208177.1; NC_002946.2. DR DNASU; 3281337; -. DR EnsemblBacteria; AAW89765; AAW89765; NGO_1098. DR GeneID; 3281337; -. DR KEGG; ngo:NGO1098; -. DR PATRIC; 20335450; VBINeiGon24812_1291. DR HOGENOM; HOG000226549; -. DR KO; K06909; -. DR OMA; ALGWYHE; -. DR OrthoDB; EOG62RS86; -. DR BioCyc; NGON242231:GI2G-1010-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0006323; P:DNA packaging; IEA:InterPro. DR InterPro; IPR006437; Phage_terminase_lsu. DR Pfam; PF04466; Terminase_3; 1. DR TIGRFAMs; TIGR01547; phage_term_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 424 AA; 48377 MW; 4B7FA08B7CCEA952 CRC64; MTGKTVDLKL PAKLDGLFKP CRYKVMYGGR GGGKSHGAAS ALLALGAQRP LRILCAREIQ KSMRDSVHRL LKDKVAQLGL GHFYEITDFE IRGANGTLFV FSGLQSHTVD SIKSFEGIDI VWVEEGHGVS KKSWDVLTPT IRKEGSEIWI TLNPDMETDE TYRRFIAMPS EDTWLCEINW RDNPWFPEAL NRERLKAQRS MNKEDYGNIW EGRPRMVSEG AVYRHEIQDA FHSGRVTLVP YDSSLPVHTV WDLGWNDAMT IGLVQRDLTS VRIIGYIEDT HRTLDWYVAE LEKLPYRWGT DFLPHDGRTR NFQTGKSTME ILTGLGRKSV FVQNATGIEE GIRAARMLFP KVYFDKDKTA RLLECLKRYG RQIHAKTGVA MGPLHDEYSH GADMFRYLAQ AVDLMDTGSN TGYTETPVSD WRLY // ID Q5F715_NEIG1 Unreviewed; 481 AA. AC Q5F715; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. DE SubName: Full=Cbb3-type cytochrome c oxidase subunit I {ECO:0000313|EMBL:AAW90022.1}; GN ORFNames=NGO_1374 {ECO:0000313|EMBL:AAW90022.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90022.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90022.1; -; Genomic_DNA. DR RefSeq; WP_003693745.1; NC_002946.2. DR RefSeq; YP_208434.1; NC_002946.2. DR ProteinModelPortal; Q5F715; -. DR EnsemblBacteria; AAW90022; AAW90022; NGO_1374. DR GeneID; 3281484; -. DR KEGG; ngo:NGO1374; -. DR PATRIC; 20336137; VBINeiGon24812_1617. DR HOGENOM; HOG000277908; -. DR KO; K00404; -. DR OMA; NLNYIAG; -. DR OrthoDB; EOG6G7QZX; -. DR BioCyc; NGON242231:GI2G-1287-MONOMER; -. DR Proteomes; UP000000535; 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: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 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:UP000000535}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 53947 MW; F2F431143E3AC19C CRC64; METLMDTQTY NYKVVRQFAI MTVVWGIVGM LVGVIVAAQL FAPALDLSNI GPWFHFGRLR PLHTNAVIFA FGGCGLIGTS YYVVQRTCNT RLFGGWLPAF TFWGWQAVIV AAVVSFPMGW TQGKEYAELE WPIDILITLV WVAYAIVFFG TIAKRKVKHI 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 KRTMPYYMIR FAGGLLYLSG MCIMAYNVYR TAIGGKAVDA EIPAVSQTQH H // ID Q5F7V4_NEIG1 Unreviewed; 126 AA. AC Q5F7V4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Membrane-bound lysozyme-inhibitor of c-type lysozyme family protein {ECO:0000313|EMBL:AAW89733.1}; GN ORFNames=NGO_1063 {ECO:0000313|EMBL:AAW89733.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89733.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89733.1; -; Genomic_DNA. DR RefSeq; WP_003688168.1; NC_002946.2. DR RefSeq; YP_208145.1; NC_002946.2. DR ProteinModelPortal; Q5F7V4; -. DR EnsemblBacteria; AAW89733; AAW89733; NGO_1063. DR GeneID; 3281787; -. DR KEGG; ngo:NGO1063; -. DR PATRIC; 20335358; VBINeiGon24812_1245. DR HOGENOM; HOG000219019; -. DR OMA; DCENGLA; -. DR OrthoDB; EOG6BW518; -. DR BioCyc; NGON242231:GI2G-978-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018660; C-type_lysozyme_inhibitor. DR Pfam; PF09864; MliC; 1. DR SUPFAM; SSF141488; SSF141488; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 126 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256224. SQ SEQUENCE 126 AA; 13484 MW; 79342D447A82A6DC CRC64; MNIRFFALTV SVLSLAACAV PEAYDGGGRG YMPPVQNQAG PDDFRAFSCE NGLSVRVRNL DGGKIALRLD GRRAVLSSDV AASGERYTAE HGLFGNGTEW HQKGGEAFFG FTDAYGNSVE TSCRAR // ID Q5FA14_NEIG1 Unreviewed; 289 AA. AC Q5FA14; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. 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 ORFNames=NGO_0220 {ECO:0000313|EMBL:AAW88973.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88973.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88973.1; -; Genomic_DNA. DR RefSeq; WP_003687550.1; NC_002946.2. DR RefSeq; YP_207385.1; NC_002946.2. DR ProteinModelPortal; Q5FA14; -. DR EnsemblBacteria; AAW88973; AAW88973; NGO_0220. DR GeneID; 3281452; -. DR KEGG; ngo:NGO0220; -. DR PATRIC; 20333379; VBINeiGon24812_0272. DR HOGENOM; HOG000283477; -. DR KO; K00963; -. DR OMA; KGWLEAN; -. DR OrthoDB; EOG6Z9B3V; -. DR BioCyc; NGON242231:GI2G-203-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU361259, KW ECO:0000313|EMBL:AAW88973.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU361259, KW ECO:0000313|EMBL:AAW88973.1}. FT DOMAIN 11 265 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 289 AA; 31997 MW; 1B4F23EC8F3E5360 CRC64; MKPIKKAVFP VAGMGTRFLP ATKANPKEML PIVDKPLIQY AVEEAVEAGC TEMVFVTGRN KRSIEDHFDK AYELETKLEM RHKDKLLEHV RNILPPNITC LYIRQAEALG LGHAVLCARA AIGDEPFAVI LADDLIDAPK GALKQMVEVY GRSGNSILGV ETVEPSQTGS YGIVETEQLK QFQRITGIVE KPKPEDAPSN LAVVGRYILT PRIFDLLTGL PRGAGNEIQL TDGIAKLLDH EFVLAHPFEG TRYDCGSKLG YLEATVAYGL KHPETGEPFR RLLEKYRTE // ID Q5F557_NEIG1 Unreviewed; 199 AA. AC Q5F557; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. 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 ORFNames=NGO_2079 {ECO:0000313|EMBL:AAW90680.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90680.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90680.1; -; Genomic_DNA. DR RefSeq; WP_003690382.1; NC_002946.2. DR RefSeq; YP_209092.1; NC_002946.2. DR ProteinModelPortal; Q5F557; -. DR EnsemblBacteria; AAW90680; AAW90680; NGO_2079. DR GeneID; 3282838; -. DR KEGG; ngo:NGO2079; -. DR PATRIC; 20337991; VBINeiGon24812_2518. DR HOGENOM; HOG000021986; -. DR KO; K01673; -. DR OMA; FLEPAMG; -. DR OrthoDB; EOG6WMJ50; -. DR BioCyc; NGON242231:GI2G-1974-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|RuleBase:RU003956}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Zinc {ECO:0000256|RuleBase:RU003956}. SQ SEQUENCE 199 AA; 22086 MW; 7206265FFDD2C778 CRC64; MSELSEILSY NQKFVESGEY EKYFTDKYPE RGLAVLSCMD ARIIGLLPDA LGLKNGDAKL IKNAGALVTH PWGSVMRSLL VAVFELKVRE IMVIAHHDCG MQGLNAEEFL GRVRESRIPE DRIETLRYAG VDLDGWLTGF DNVEDSVRHT VDLIRNHPLM PRHIAVHGLV IHPVTGKLTL VVDGSVSDGM DLSEGMETS // ID Q5F6N6_NEIG1 Unreviewed; 235 AA. AC Q5F6N6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Opacity protein opA54 {ECO:0000313|EMBL:AAW90151.2}; GN ORFNames=NGO_1513 {ECO:0000313|EMBL:AAW90151.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90151.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90151.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6N6; -. DR EnsemblBacteria; AAW90151; AAW90151; NGO_1513. DR PATRIC; 20336506; VBINeiGon24812_1801. DR HOGENOM; HOG000218831; -. DR OMA; PSKGATE; -. DR OrthoDB; EOG69KTWT; -. DR BioCyc; NGON242231:GI2G-1417-MONOMER; -. DR Proteomes; UP000000535; 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; -; 3. DR InterPro; IPR011250; OMP/PagP_b-brl. DR InterPro; IPR003394; Porin_opacity. DR Pfam; PF02462; Opacity; 1. DR SUPFAM; SSF56925; SSF56925; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 235 Opacity. {ECO:0000259|Pfam:PF02462}. SQ SEQUENCE 235 AA; 26645 MW; A907A5C1EFA7ECAA CRC64; MQADLAYAAE RITHDYPEPT APGKNKISTV SDYFRNIRTH SIHPRVSVGY DFGGWRIAAD YARYRKWHNN KYSVNIKELE RKNNKTFGGN QLNIKYQKTE HQENGTFHAV SSLGLSAVYD FKLNDKFKPY IGARVAYGHV RHSIDSTKKI TGTLTAYPSD ADAAVTVYPD GHPQKNTYQK SNSSRRLGFG AMAGVGIDVA PGLTLDAGYR YHNWGRLENT RFKTHEASLG MRYRF // ID Q5F514_NEIG1 Unreviewed; 171 AA. AC Q5F514; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AAW90723.2}; GN ORFNames=NGO_2125 {ECO:0000313|EMBL:AAW90723.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90723.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90723.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F514; -. DR EnsemblBacteria; AAW90723; AAW90723; NGO_2125. DR PATRIC; 20338099; VBINeiGon24812_2572. DR HOGENOM; HOG000049435; -. DR OMA; WPGRRVI; -. DR OrthoDB; EOG6PZXGR; -. DR BioCyc; NGON242231:GI2G-2017-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90723.2}. SQ SEQUENCE 171 AA; 18508 MW; A43B020B39932908 CRC64; MESKFFFLLL RFAGSVLPPS YMRGIGIVGR RVRGFLARRV SPHIGRGVNI ERGAYVFPDT VLGDGSGIGA NCEICRGLVV GKNVMMGPEC LLYSTNHKFD RENKRFEGYT EIRPITLEDD VWPGRRVIVM AGVTVGRGSV VGAGAVVTKD IPPYSLAAGN PAVVKKNLPE G // ID Q5F6A0_NEIG1 Unreviewed; 389 AA. AC Q5F6A0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994}; GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994}; GN ORFNames=NGO_1662 {ECO:0000313|EMBL:AAW90287.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90287.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90287.1; -; Genomic_DNA. DR RefSeq; WP_003689796.1; NC_002946.2. DR RefSeq; YP_208699.1; NC_002946.2. DR ProteinModelPortal; Q5F6A0; -. DR DNASU; 3281303; -. DR EnsemblBacteria; AAW90287; AAW90287; NGO_1662. DR GeneID; 3281303; -. DR KEGG; ngo:NGO1662; -. DR PATRIC; 20336874; VBINeiGon24812_1982. DR HOGENOM; HOG000257805; -. DR KO; K19804; -. DR OMA; RYRCAAC; -. DR OrthoDB; EOG68SVV7; -. DR BioCyc; NGON242231:GI2G-1556-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 44503 MW; C917FFDAD6DB9E0A CRC64; MDNELWIILL PIILLPVFFT MGWFAARVDM KTVLKQAKSI PSGFYKSLDA LVDRNSGRAA RELAEVVDGR PQSYDLNLTL GKLYRQRGEN DKAINIHRTM LDSPDTVGEK RARVLFELAQ NYQSAGLVDR AEQIFLGLQD GEMAREARQH LLNIYQQDRD WEKAVETAQL LSHDEQTYQF EIAQFYCELA QAALFKSNFD AARFNVGKAL EANKKCTRAN MILGDIEHRQ GNFPAAVEAY AAIEQQNHAY LSMVGEKLYE AYAAQGKPEE GLNRLTGYMQ TFPELDLINV VYEKSLLLKG EKEAAQTAVE LVRRKPDLNG VYRLLGLKLS DLDPAWKADA DMMRSVIGRQ LQRSVMYRCR NCHFKSQVFF WHCPACNKWQ TFTPNKIEV // ID Q5F661_NEIG1 Unreviewed; 132 AA. AC Q5F661; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90326.1}; GN ORFNames=NGO_1705 {ECO:0000313|EMBL:AAW90326.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90326.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90326.1; -; Genomic_DNA. DR RefSeq; WP_002216361.1; NC_002946.2. DR RefSeq; YP_208738.1; NC_002946.2. DR DNASU; 3281173; -. DR EnsemblBacteria; AAW90326; AAW90326; NGO_1705. DR GeneID; 3281173; -. DR KEGG; ngo:NGO1705; -. DR PATRIC; 20337002; VBINeiGon24812_2041. DR HOGENOM; HOG000198397; -. DR KO; K15977; -. DR OMA; GFPASQM; -. DR OrthoDB; EOG69SKFR; -. DR BioCyc; NGON242231:GI2G-1601-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F8R8_NEIG1 Unreviewed; 872 AA. AC Q5F8R8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Autotransporter {ECO:0000313|EMBL:AAW89419.1}; GN ORFNames=NGO_0694 {ECO:0000313|EMBL:AAW89419.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89419.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89419.1; -; Genomic_DNA. DR RefSeq; WP_010951109.1; NC_002946.2. DR RefSeq; YP_207831.1; NC_002946.2. DR ProteinModelPortal; Q5F8R8; -. DR EnsemblBacteria; AAW89419; AAW89419; NGO_0694. DR GeneID; 3281816; -. DR KEGG; ngo:NGO0694; -. DR PATRIC; 20334498; VBINeiGon24812_0821. DR OMA; WIRLTHT; -. DR OrthoDB; EOG60KN07; -. DR BioCyc; NGON242231:GI2G-659-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR Gene3D; 2.160.20.20; -; 1. 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; IPR004899; Pertactin_central. DR Pfam; PF03797; Autotransporter; 1. DR Pfam; PF03212; Pertactin; 1. DR SMART; SM00869; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR SUPFAM; SSF51126; SSF51126; 1. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 647 872 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. SQ SEQUENCE 872 AA; 96812 MW; 451E24AE978E7A37 CRC64; MNQEGITAHG NATITLKAKE NNKITVENAA YSSDGISTLI NRTGARPGTR DDGNKIILEA GGDNIVTMKS GDADADYVNN SKVLTETPYY KSKRGSNGIF AYGDKSLVKL IGENNIVKSE ISEKSKALNG GFRHIGIYSW QNAKVELSAK SDNIVQGGIW GLYSNNSSIS LKGKNNVISN PKYNVFAYKK AKVDLTVENK NTLSDAEFGV YALNTSMVNL SSKDNNEVKS TQVGLYSQDG GSINVDRKDN IIEGDAVALV GKGGSQNIRA SRTNLISSKS LGIHAEQAAK IAITGASNTI HASNAAIRSL DKSEVKIDGQ ITIDSNVANL ARQDGSIHLN YKDDTRITGA TVSDKGLVAI KPLNNTNIVA DTIHYKGDVL AVNKGKVELD FTPNILLAGR LDNFSGLTDS KHKNLFENYV ANLDSKSAGE INFNLAKDAL WTMTGQSWLD KLEGQGTIDF NNDAKTSGRA LHIGELAGAN KFLMHLNKDG IHSDMLYVKK GTSTPQEVVV KNLSEVLDSM NYGERLRFAT VTNSKNEFVN GKKYIDDTHL MEDALTVEYS AHNGDKNNKD DYNKSFNGSE MTAEKAGDDY VNKTYTDNRQ NVYLVKQATG NPSRNVKNIN DMFDSTAHYA FTLDTYAKRE GERAFSTLDK KEGDWIRLTH TRVIQSNAFR FHNNDFEIGY DRFSLNEQEK KRKWGISLDY GHGRTSLWNT FGKDKIRKYE LALYNTTQYI DKEGDETGYI DNVLKIGKLR NRVIARNHMG QLWGKGKYSN TLFSISTEYG RRKFLDDDKL WRITPQVQLQ YSYLRGTGYR IDNGINVNLS HANSLIGRLG LDVVRKFDGG KKLFYIKGNI FHEFLGSRSF KAFEGKSHYA QK // ID Q5F5B1_NEIG1 Unreviewed; 64 AA. AC Q5F5B1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90626.1}; GN ORFNames=NGO_2018 {ECO:0000313|EMBL:AAW90626.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90626.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90626.1; -; Genomic_DNA. DR RefSeq; WP_003686931.1; NC_002946.2. DR RefSeq; YP_209038.1; NC_002946.2. DR EnsemblBacteria; AAW90626; AAW90626; NGO_2018. DR GeneID; 3282729; -. DR KEGG; ngo:NGO2018; -. DR OrthoDB; EOG674358; -. DR BioCyc; NGON242231:GI2G-1919-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 7100 MW; 36D2CDF68565C16B CRC64; MKPVLVRTAM SGFPRCKQIK PTGYSNTAKK SRPNPKGTDG QTHYGENVLL NESAKQTLLK QLQL // ID Q5F844_NEIG1 Unreviewed; 71 AA. AC Q5F844; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89643.1}; GN ORFNames=NGO_0953 {ECO:0000313|EMBL:AAW89643.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89643.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89643.1; -; Genomic_DNA. DR RefSeq; WP_003691062.1; NC_002946.2. DR RefSeq; YP_208055.1; NC_002946.2. DR EnsemblBacteria; AAW89643; AAW89643; NGO_0953. DR GeneID; 3282086; -. DR KEGG; ngo:NGO0953; -. DR PATRIC; 20335091; VBINeiGon24812_1115. DR HOGENOM; HOG000027854; -. DR OMA; RESRHSM; -. DR OrthoDB; EOG6M0T9H; -. DR BioCyc; NGON242231:GI2G-885-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 71 AA; 8290 MW; 20870CCEB8331AA5 CRC64; MPSESPSDGI CFPKRIILPQ AYANPFYRIG NSKKNPFHSH AGKPVFDFGY FWLFRVIYES SFPQKRESVF L // ID Q5FA98_NEIG1 Unreviewed; 171 AA. AC Q5FA98; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88889.1}; GN ORFNames=NGO_0130 {ECO:0000313|EMBL:AAW88889.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88889.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88889.1; -; Genomic_DNA. DR RefSeq; WP_003687408.1; NC_002946.2. DR RefSeq; YP_207301.1; NC_002946.2. DR ProteinModelPortal; Q5FA98; -. DR EnsemblBacteria; AAW88889; AAW88889; NGO_0130. DR GeneID; 3281252; -. DR KEGG; ngo:NGO0130; -. DR PATRIC; 20333167; VBINeiGon24812_0167. DR HOGENOM; HOG000063012; -. DR OMA; KPDWFGY; -. DR OrthoDB; EOG6T7N9G; -. DR BioCyc; NGON242231:GI2G-118-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011440; DUF1543. DR Pfam; PF07566; DUF1543; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 66 DUF1543. {ECO:0000259|Pfam:PF07566}. FT DOMAIN 96 140 DUF1543. {ECO:0000259|Pfam:PF07566}. SQ SEQUENCE 171 AA; 18983 MW; B1009C1810B85D35 CRC64; MPKLHMFYLG GNAGRSNIEV HDIQFAVCDD YREAVPALKA AWFGDTDKIH IDGWQVVEWA DGYDIAVSET PKTKMPPENA PRLYFANVGG YRAGQLAEAH AFGLFAAATP AEAKQKALQT LLTDYVRQHK DNLKDVDNLL ALEHIGNFHI RLTPNPHGKP AEIGFQGYLP I // ID Q5F5K4_NEIG1 Unreviewed; 82 AA. AC Q5F5K4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=BolA family transcriptional regulator {ECO:0000313|EMBL:AAW90533.1}; GN ORFNames=NGO_1920 {ECO:0000313|EMBL:AAW90533.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90533.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90533.1; -; Genomic_DNA. DR RefSeq; WP_010951370.1; NC_002946.2. DR RefSeq; YP_208945.1; NC_002946.2. DR ProteinModelPortal; Q5F5K4; -. DR EnsemblBacteria; AAW90533; AAW90533; NGO_1920. DR GeneID; 3282853; -. DR KEGG; ngo:NGO1920; -. DR PATRIC; 20337576; VBINeiGon24812_2315. DR HOGENOM; HOG000255170; -. DR OMA; PAEWQAG; -. DR OrthoDB; EOG6VMTQ7; -. DR BioCyc; NGON242231:GI2G-1823-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 8898 MW; 922709391A952E5C CRC64; MLTPEQVKAL IAGVAKCEHI EVEGDGHHFF AVIVSLEFEG KARLARHRLI KDGLKAQLES NELHALSISV AATPAEWAAK AQ // ID Q5F693_NEIG1 Unreviewed; 410 AA. AC Q5F693; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 70. DE SubName: Full=Type II secretion system protein F {ECO:0000313|EMBL:AAW90294.1}; GN ORFNames=NGO_1669 {ECO:0000313|EMBL:AAW90294.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90294.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90294.1; -; Genomic_DNA. DR RefSeq; WP_003689811.1; NC_002946.2. DR RefSeq; YP_208706.1; NC_002946.2. DR EnsemblBacteria; AAW90294; AAW90294; NGO_1669. DR GeneID; 3281254; -. DR KEGG; ngo:NGO1669; -. DR PATRIC; 20336890; VBINeiGon24812_1990. DR HOGENOM; HOG000253740; -. DR KO; K02653; -. DR OMA; TRQMATM; -. DR OrthoDB; EOG6Z6FTM; -. DR BioCyc; NGON242231:GI2G-1563-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 45332 MW; E7A9BD26F09EF0A3 CRC64; MAKNGGFSLF AKKEKRFIFE GRHSASDKLV NGEVSAFTEE EARKKLAKRG IRPLQITRVK TSSKRKITQE DITVFTRQLS TMIKAGLPLM QAFEIVARGH GNPSMTEMLM EIRGQVEQGS SLSRAFSNHP KYFDRFYCNL VAAGETGGVL ESLLDKLAIY KEKTQAIRKK VKTALTYPVS VIAVAIGLVF VMMIFVLPAF KEVYANMGAE LPPLTQTVMD MSDFFVSYGW MVLIALGFAI YGFLKLKARS IKIQRRMDAI LLRMPIFGDI VRKGTIARWG RTTATLFAAG VPLVDVLDST AGAAGNLIYE EATREIRTRV IQGLSMTSGM RATELFPNMM LQMSSIGEES GSLDDMLNKA AEFYEDEVDN AVGRLSAMME PIIIVILGLV IGTLLVAMYL PLFNLGNVVA // ID Q5FA38_NEIG1 Unreviewed; 295 AA. AC Q5FA38; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 69. DE SubName: Full=Polyamine ABC transporter permease {ECO:0000313|EMBL:AAW88949.1}; GN ORFNames=NGO_0196 {ECO:0000313|EMBL:AAW88949.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88949.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88949.1; -; Genomic_DNA. DR RefSeq; WP_003687503.1; NC_002946.2. DR RefSeq; YP_207361.1; NC_002946.2. DR ProteinModelPortal; Q5FA38; -. DR EnsemblBacteria; AAW88949; AAW88949; NGO_0196. DR GeneID; 3281651; -. DR KEGG; ngo:NGO0196; -. DR PATRIC; 20333321; VBINeiGon24812_0243. DR HOGENOM; HOG000263700; -. DR KO; K11074; -. DR OMA; KPWKVFF; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NGON242231:GI2G-179-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 32618 MW; 08C32E0BAE1F8A77 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 RQATKRNREA AEAYRQEKLA AEKAN // ID Q5F7W7_NEIG1 Unreviewed; 69 AA. AC Q5F7W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 63. DE RecName: Full=Tautomerase {ECO:0000256|RuleBase:RU362032}; DE EC=5.3.2.- {ECO:0000256|RuleBase:RU362032}; GN ORFNames=NGO_1048 {ECO:0000313|EMBL:AAW89720.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89720.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89720.1; -; Genomic_DNA. DR RefSeq; WP_003688192.1; NC_002946.2. DR RefSeq; YP_208132.1; NC_002946.2. DR ProteinModelPortal; Q5F7W7; -. DR EnsemblBacteria; AAW89720; AAW89720; NGO_1048. DR GeneID; 3282572; -. DR KEGG; ngo:NGO1048; -. DR PATRIC; 20335320; VBINeiGon24812_1226. DR HOGENOM; HOG000077848; -. DR KO; K01821; -. DR OMA; WGIGGET; -. DR OrthoDB; EOG62ZHW8; -. DR BioCyc; NGON242231:GI2G-965-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU362032}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 64 4-oxalocrotonate_tautomerase. FT {ECO:0000259|Pfam:PF01361}. SQ SEQUENCE 69 AA; 7420 MW; 5C3C244DDC737AE3 CRC64; MPYVNIKVTG GKEAPTAAQK AELIGGVIEL LARVLGKNPE TTVVVIDEVD TDNWDIGGKS VSERRKEGR // ID Q5F8X5_NEIG1 Unreviewed; 103 AA. AC Q5F8X5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89362.2}; GN ORFNames=NGO_0635 {ECO:0000313|EMBL:AAW89362.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89362.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89362.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89362; AAW89362; NGO_0635. DR PATRIC; 20334354; VBINeiGon24812_0749. DR HOGENOM; HOG000071299; -. DR OMA; YNRSIFK; -. DR OrthoDB; EOG6NWBTM; -. DR BioCyc; NGON242231:GI2G-602-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 103 AA; 12086 MW; 739FE7AAB446FBBE CRC64; MGGALRLMSN KGCLRKNTMK VKIINLPNGY KRIIYGKYFE QFDLDYEQDL DVLKKDIEFA LSVIEYNRSI FKKFSSLFEN KIIFVYQGGH HLDIIDRDKG SLK // ID Q5F853_NEIG1 Unreviewed; 103 AA. AC Q5F853; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89634.1}; GN ORFNames=NGO_0939 {ECO:0000313|EMBL:AAW89634.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89634.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89634.1; -; Genomic_DNA. DR RefSeq; WP_003699853.1; NC_002946.2. DR RefSeq; YP_208046.1; NC_002946.2. DR EnsemblBacteria; AAW89634; AAW89634; NGO_0939. DR GeneID; 3281627; -. DR KEGG; ngo:NGO0939; -. DR PATRIC; 20335063; VBINeiGon24812_1101. DR HOGENOM; HOG000071280; -. DR OMA; FCFAEAR; -. DR OrthoDB; EOG64JFXN; -. DR BioCyc; NGON242231:GI2G-876-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 103 AA; 11724 MW; 3B841763AE9D29FF CRC64; MFQVWKNADY SGKRAALIFC FAEARRRQGA GLPYAFIKCV QTDASGFQYA RARCRLVRRH RRQRPISRGT PVPGIFKGSV VRRFPAARLQ TASPARPLDK VRS // ID Q5F7N7_NEIG1 Unreviewed; 224 AA. AC Q5F7N7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89800.1}; GN ORFNames=NGO_1133 {ECO:0000313|EMBL:AAW89800.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89800.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89800.1; -; Genomic_DNA. DR RefSeq; WP_003689160.1; NC_002946.2. DR RefSeq; YP_208212.1; NC_002946.2. DR EnsemblBacteria; AAW89800; AAW89800; NGO_1133. DR GeneID; 3282248; -. DR KEGG; ngo:NGO1133; -. DR PATRIC; 20335526; VBINeiGon24812_1328. DR HOGENOM; HOG000218969; -. DR OMA; GWMNIAS; -. DR OrthoDB; EOG6NGVQR; -. DR BioCyc; NGON242231:GI2G-1046-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 224 AA; 24193 MW; 8298FA9D0090EA79 CRC64; MPAALIKDFL LTQGLKLPLD EVRAAYLTAQ TVMDMGMASI DRSVLWCNDE GWKLADYLPC DDVREDALKR LFMALDSVFS RSTGVRSAAV YALMPSENAA LRLVCLSQQG EGLENIWEQD GNITDVSLAC RSAQSGWMNV ASDVRRWLNL GELSGERNHA SAAQISIPVC TESGGVLGVV HVEFECAECA DTAAQAEWVA LALALSEPLK QLLGITAAEG DENV // ID Q5F8X1_NEIG1 Unreviewed; 390 AA. AC Q5F8X1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:AAW89366.1}; DE EC=1.1.2.3 {ECO:0000313|EMBL:AAW89366.1}; GN Name=lldD {ECO:0000313|EMBL:AAW89366.1}; GN ORFNames=NGO_0639 {ECO:0000313|EMBL:AAW89366.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89366.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89366.1; -; Genomic_DNA. DR RefSeq; WP_010951097.1; NC_002946.2. DR RefSeq; YP_207778.1; NC_002946.2. DR ProteinModelPortal; Q5F8X1; -. DR EnsemblBacteria; AAW89366; AAW89366; NGO_0639. DR GeneID; 3281775; -. DR KEGG; ngo:NGO0639; -. DR PATRIC; 20334362; VBINeiGon24812_0753. DR HOGENOM; HOG000217464; -. DR KO; K00101; -. DR OMA; AWIKEQW; -. DR OrthoDB; EOG6HMXBG; -. DR BioCyc; NGON242231:GI2G-606-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89366.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 43397 MW; 11A9E0E4BAB48076 CRC64; MKRDLSKMTC IEDLHRVAKR KMPRMFYDYI DSGSWTETTY RENTSDFKDI RFRQKVLVNM EGRSLETKMI GGDVKMPVAI APTGFTGMAH ADGEILAARA AEKFGIPFTL STMSICSIED VAENTSAPFW FQLYVMRDRE FMENLIKRAK DAKCSALVLT ADLQVLGQRH KDIKNGLSAP PKPTIANLIN LATKPEWCMK MLNTERRTFR NIVGHAKNVG DLSSLSSWTA EQFDPRLSWD DVARIKDLWG GKLIIKGIME PEDAEKAAKS GADALVVSNH GGRQLDDTVS AIKALPDIVS AVGSDIEVWM DSGIRSGQDI LKAWALGAKG TMIGRAFLYG LGAYGEEGVT RALEILYKEM DVSMAFTGHR DIQDVDASIL RSKDWGRETV // ID Q5F635_NEIG1 Unreviewed; 45 AA. AC Q5F635; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90352.1}; GN ORFNames=NGO_1731 {ECO:0000313|EMBL:AAW90352.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90352.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90352.1; -; Genomic_DNA. DR RefSeq; WP_002235413.1; NC_002946.2. DR RefSeq; YP_208764.1; NC_002946.2. DR EnsemblBacteria; AAW90352; AAW90352; NGO_1731. DR GeneID; 3281105; -. DR KEGG; ngo:NGO1731; -. DR PATRIC; 20337060; VBINeiGon24812_2070. DR HOGENOM; HOG000027897; -. DR OrthoDB; EOG66TGC9; -. DR BioCyc; NGON242231:GI2G-1627-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 4674 MW; 792F093BB10DD61F CRC64; MPSEGGAAFA LTKPCVSAPR CLPDGFSRKM ALLSFLSDGI VFDAV // ID Q5F999_NEIG1 Unreviewed; 176 AA. AC Q5F999; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Phage gp6-like head-tail connector family protein {ECO:0000313|EMBL:AAW89238.1}; GN ORFNames=NGO_0500 {ECO:0000313|EMBL:AAW89238.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89238.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89238.1; -; Genomic_DNA. DR RefSeq; WP_003689080.1; NC_002946.2. DR RefSeq; YP_207650.1; NC_002946.2. DR EnsemblBacteria; AAW89238; AAW89238; NGO_0500. DR GeneID; 3282949; -. DR KEGG; ngo:NGO0500; -. DR PATRIC; 20334042; VBINeiGon24812_0593. DR OMA; LAYKERT; -. DR OrthoDB; EOG62K1W9; -. DR BioCyc; NGON242231:GI2G-478-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR021146; Phafe_gp6_head-tail. DR Pfam; PF05135; Phage_connect_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 176 AA; 19256 MW; 3A0A8A78700FDCFD CRC64; MAAPVSLEEF KQRIGVEHDR RDDFFLSVID GVSAAAEAYI GRSLLAADYV GRYDGNGKDR IVLDNYPVLS VSSVKINGAD AGGWEFDNWL LMRPEGFARG LKNVEVSYRA GYERMPADIR EAVMIIAVQR VNEIEGKGVR SKTLAGETVA FSTFGNSGGM PPSAFAILNE YKRKGV // ID Q5F833_NEIG1 Unreviewed; 248 AA. AC Q5F833; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 76. DE SubName: Full=Amino acid ABC transporter permease {ECO:0000313|EMBL:AAW89654.1}; GN ORFNames=NGO_0968 {ECO:0000313|EMBL:AAW89654.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89654.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89654.1; -; Genomic_DNA. DR RefSeq; WP_003688329.1; NC_002946.2. DR RefSeq; YP_208066.1; NC_002946.2. DR ProteinModelPortal; Q5F833; -. DR EnsemblBacteria; AAW89654; AAW89654; NGO_0968. DR GeneID; 3281136; -. DR KEGG; ngo:NGO0968; -. DR PATRIC; 20335128; VBINeiGon24812_1133. DR HOGENOM; HOG000267552; -. DR KO; K02029; -. DR OMA; YKAEETQ; -. DR OrthoDB; EOG6MM1R5; -. DR BioCyc; NGON242231:GI2G-896-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 27739 MW; 2A57FC06CECC4808 CRC64; MDFRFDIIYE YRWMFLYGAL TTLGLTVVAT AGGSVLGLLL ALARLIHLEK AGAPMRVLAW ALRKVSLLYV TLFRGTPLFV QIVIWAYVWF PFFVHPSDGI LVSGEAAIAL RRGYGPLIAG SLALIANSGA YICEIFRAGI QSIDKGQMEA ACSLGLTYPQ AMRYVILPQA LRRMLPPLAS EFITLLKDSS LLSVIAVAEL AYVQNTITGR YSVYEEPLYT AALIYLLMTT FLGWIFLRLE KRYNPQHR // ID Q5F5H6_NEIG1 Unreviewed; 300 AA. AC Q5F5H6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Esterase {ECO:0000313|EMBL:AAW90561.1}; GN ORFNames=NGO_1949 {ECO:0000313|EMBL:AAW90561.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90561.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90561.1; -; Genomic_DNA. DR RefSeq; WP_003688125.1; NC_002946.2. DR RefSeq; YP_208973.1; NC_002946.2. DR ProteinModelPortal; Q5F5H6; -. DR EnsemblBacteria; AAW90561; AAW90561; NGO_1949. DR GeneID; 3282671; -. DR KEGG; ngo:NGO1949; -. DR PATRIC; 20337643; VBINeiGon24812_2348. DR HOGENOM; HOG000261884; -. DR KO; K07001; -. DR OMA; ILFRRGN; -. DR OrthoDB; EOG6KDKSZ; -. DR BioCyc; NGON242231:GI2G-1851-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 300 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256187. FT DOMAIN 48 205 Patatin. {ECO:0000259|Pfam:PF01734}. SQ SEQUENCE 300 AA; 31354 MW; D99286A5729755DE CRC64; MENMVTFSKI RSFLAIAAAA LLAACGTAGN NAARKPVQTA KPAAVVALAL GGGASKGFAH IGIVKVLKEN GIPVKVVTGT SAGSIVGSLL ASGMSPDRLE LEAEILGKTD LVDLTLSTSG FIKGEKLQNY INRKVGGRQI QQFPIKFAAV ATDFETGKAV AFNQGNAGQA VRASAAIPNV FQPVIIGRHK YVDGGLSQPV PVSAARRQGA NFVIAVDISA RPSKNVGQGF FSYLDQTLNV MSVSVLQNEL GQADVVIKPQ VLDLGAVGGF DQKKRAIRLG EEAARAALPE IKRKLAAYRY // ID Q5F8G1_NEIG1 Unreviewed; 50 AA. AC Q5F8G1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89526.1}; GN ORFNames=NGO_0814 {ECO:0000313|EMBL:AAW89526.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89526.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89526.1; -; Genomic_DNA. DR RefSeq; WP_010360202.1; NC_002946.2. DR RefSeq; YP_207938.1; NC_002946.2. DR EnsemblBacteria; AAW89526; AAW89526; NGO_0814. DR GeneID; 3281941; -. DR KEGG; ngo:NGO0814; -. DR BioCyc; NGON242231:GI2G-768-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 50 AA; 5522 MW; 6ED392B2AE3D4D2D CRC64; MPGCAAQRRK NRLPRIFKRV TLAAAVFSHL ITRNRRHCAG GLPVSVIAPL // ID Q5F8U0_NEIG1 Unreviewed; 271 AA. AC Q5F8U0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 62. DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AAW89397.1}; GN ORFNames=NGO_0670 {ECO:0000313|EMBL:AAW89397.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89397.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3IC6} RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-220. RA Chang C., Marshall N., Cobb G., Joachimiak A.; RT "Crystal structure of putative methylase family protein from Neisseria RT gonorrhoeae."; RL Submitted (JUL-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; AE004969; AAW89397.1; -; Genomic_DNA. DR RefSeq; WP_003688817.1; NC_002946.2. DR RefSeq; YP_207809.1; NC_002946.2. DR PDB; 3IC6; X-ray; 2.59 A; A=1-220. DR PDBsum; 3IC6; -. DR ProteinModelPortal; Q5F8U0; -. DR EnsemblBacteria; AAW89397; AAW89397; NGO_0670. DR GeneID; 3282065; -. DR KEGG; ngo:NGO0670; -. DR PATRIC; 20334436; VBINeiGon24812_0790. DR HOGENOM; HOG000229628; -. DR KO; K02533; -. DR OMA; ELQRCHF; -. DR OrthoDB; EOG6XSZTC; -. DR BioCyc; NGON242231:GI2G-637-MONOMER; -. DR EvolutionaryTrace; Q5F8U0; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3IC6}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAW89397.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAW89397.1}. FT DOMAIN 15 50 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. FT DOMAIN 74 185 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. SQ SEQUENCE 271 AA; 30099 MW; 762DA47BFAEFC7F0 CRC64; MTALKPALPD YLGNIRIILT RTSHPANIGS AARAMKTMGL HRLTIVTPNL MATPMTENPP VFNPDDVQSF ALPEESFILA SGAADVLHNA EIVATLDEAL ADTTIACALT SRRREITAPL QTPRDLVPEL LQAANRGEKV ALVFGNETFG LSIEEVRACN RLMTINGNPD YFSLNLAQAV QVVCYEIFSQ TDSPMTHLQQ EDHAATHEQI KGMLAHMESV MDDIGFFNRR NGERLMRRMQ SLFGRANTQT EDIDILRGFF NTVSHRIHKK D // ID Q5F8F9_NEIG1 Unreviewed; 101 AA. AC Q5F8F9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89528.1}; GN ORFNames=NGO_0816 {ECO:0000313|EMBL:AAW89528.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89528.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89528.1; -; Genomic_DNA. DR RefSeq; WP_003688593.1; NC_002946.2. DR RefSeq; YP_207940.1; NC_002946.2. DR EnsemblBacteria; AAW89528; AAW89528; NGO_0816. DR GeneID; 3281946; -. DR KEGG; ngo:NGO0816; -. DR PATRIC; 20334786; VBINeiGon24812_0963. DR HOGENOM; HOG000218955; -. DR OMA; FSANVYE; -. DR OrthoDB; EOG64FKHK; -. DR BioCyc; NGON242231:GI2G-770-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025392; DUF4124. DR Pfam; PF13511; DUF4124; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 101 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255538. FT DOMAIN 12 65 DUF4124. {ECO:0000259|Pfam:PF13511}. SQ SEQUENCE 101 AA; 10814 MW; 4C85124A3A6A27D2 CRC64; MRVSKMIGSI LLVAAVQTVF SANVYECRHN GKTSYSQTPG KDCTNAGLGR DRVYSSVRPA VKDRAEDAGV GDYSDTVRDE AVQNPKGNAQ KDGSDAGIRP H // ID Q5F7W2_NEIG1 Unreviewed; 53 AA. AC Q5F7W2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89725.1}; GN ORFNames=NGO_1054 {ECO:0000313|EMBL:AAW89725.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89725.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89725.1; -; Genomic_DNA. DR RefSeq; WP_010358395.1; NC_002946.2. DR RefSeq; YP_208137.1; NC_002946.2. DR EnsemblBacteria; AAW89725; AAW89725; NGO_1054. DR GeneID; 3281526; -. DR KEGG; ngo:NGO1054; -. DR PATRIC; 20335340; VBINeiGon24812_1236. DR HOGENOM; HOG000027847; -. DR OMA; HHASPIE; -. DR OrthoDB; EOG6TJ84P; -. DR BioCyc; NGON242231:GI2G-970-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 6136 MW; 83792F3E0705C3CA CRC64; MSEQPEKHHA SPIEDERKNP VYRMGRAVAG FMLAVWAGVL ALVFFLVFRF WLS // ID Q5F5D5_NEIG1 Unreviewed; 259 AA. AC Q5F5D5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 63. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AAW90602.1}; GN ORFNames=NGO_1994 {ECO:0000313|EMBL:AAW90602.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90602.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90602.1; -; Genomic_DNA. DR RefSeq; WP_003686889.1; NC_002946.2. DR RefSeq; YP_209014.1; NC_002946.2. DR ProteinModelPortal; Q5F5D5; -. DR SMR; Q5F5D5; 1-259. DR EnsemblBacteria; AAW90602; AAW90602; NGO_1994. DR GeneID; 3282630; -. DR KEGG; ngo:NGO1994; -. DR PATRIC; 20337757; VBINeiGon24812_2405. DR HOGENOM; HOG000034586; -. DR KO; K01142; -. DR OMA; PDQYTWW; -. DR OrthoDB; EOG6TBHJS; -. DR BioCyc; NGON242231:GI2G-1892-MONOMER; -. DR Proteomes; UP000000535; 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: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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 247 Endo/exonuclease/phosphatase. FT {ECO:0000259|Pfam:PF03372}. SQ SEQUENCE 259 AA; 29628 MW; 1A68440D43507A0D CRC64; MLKIISANVN GIRSAYKKGF YEYIAASGAD IVCVQELKAQ EADLSADMKN PHGMHGYWHC AEKRGYSGVA VYSKRKPDNV QIGMGIEEFD REGRFVRCDF GRLGVISLYL PSGSSAEERQ QVKYRFLDAF YPMLEAMKNE GRDIVVCGDW NIAHQNIDLK NWKGNQKNSG FLPEEREWIG KVIHTLGWTD MWRTLYPDVP GYTWWSNRGQ AYAKDVGWRI DYQMVTPELA AKAVSAHVYK DEKFSDHAPL VVEYDYAAE // ID Q5F8D9_NEIG1 Unreviewed; 95 AA. AC Q5F8D9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89548.1}; GN ORFNames=NGO_0843 {ECO:0000313|EMBL:AAW89548.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89548.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89548.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89548; AAW89548; NGO_0843. DR PATRIC; 20334854; VBINeiGon24812_0997. DR BioCyc; NGON242231:GI2G-790-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 95 AA; 11106 MW; 364BE98588398513 CRC64; MPALAENLFV RFLFLGFRAI SKLLFPSKQK PQQKPKIRHS RREFGFFEIR LFWINSPALI FCFSDNAITL KFRHSHAGGN PDLSARKLIG KKRFL // ID Q5F9K0_NEIG1 Unreviewed; 216 AA. AC Q5F9K0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 73. DE SubName: Full=TetR family transcriptional regulator {ECO:0000313|EMBL:AAW89137.1}; GN ORFNames=NGO_0393 {ECO:0000313|EMBL:AAW89137.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89137.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89137.1; -; Genomic_DNA. DR RefSeq; WP_003692786.1; NC_002946.2. DR RefSeq; YP_207549.1; NC_002946.2. DR ProteinModelPortal; Q5F9K0; -. DR EnsemblBacteria; AAW89137; AAW89137; NGO_0393. DR GeneID; 3283016; -. DR KEGG; ngo:NGO0393; -. DR PATRIC; 20333793; VBINeiGon24812_0474. DR HOGENOM; HOG000262674; -. DR OMA; HYPAKDE; -. DR OrthoDB; EOG62ZJ03; -. DR BioCyc; NGON242231:GI2G-372-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 24752 MW; 0420DD87B91DD396 CRC64; MPVTRIAKTN TYTRIIDASL ALFNEEGERN ISTNHIAAHL GISPGNLYYH FRNKDEIIVQ LFKRYSEALL AYLNEAVLPS DVEDSINYMA GIYDVMWEYR FLFSDVNTLL ARSAELLGEH NTFTQAKVSP LLVKLLTQLN GLNVINADQT AMNDLAVNMW MVTKYWFDFD SSLRGRTKLT EDSKARGVRR TLSLLRPYLL PEHRAEYDRK IGNGNP // ID Q5F6C5_NEIG1 Unreviewed; 183 AA. AC Q5F6C5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90262.1}; GN ORFNames=NGO_1634 {ECO:0000313|EMBL:AAW90262.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90262.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90262.1; -; Genomic_DNA. DR RefSeq; WP_010951309.1; NC_002946.2. DR RefSeq; YP_208674.1; NC_002946.2. DR ProteinModelPortal; Q5F6C5; -. DR EnsemblBacteria; AAW90262; AAW90262; NGO_1634. DR GeneID; 3281353; -. DR KEGG; ngo:NGO1634; -. DR PATRIC; 20336804; VBINeiGon24812_1947. DR HOGENOM; HOG000071227; -. DR OMA; DYEPSDF; -. DR OrthoDB; EOG6HF5WB; -. DR BioCyc; NGON242231:GI2G-1531-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 183 AA; 21112 MW; FE92560A528F11F1 CRC64; MSARLMGMAF KTGIPRGQRF VLVKLCDCAN DDGLCYPSQE TLAEDTGFAE TAVRQHIKWL KDNNFIKSAR RQRGRERKSD IYRINVALLE KCYAEAAKRK AARQAKMWEE PLDYEPSDFE PSDYEPSDFE PSDYEPSDFD AKNHQILSDE PSDFALRTIR FCAKNHQILS GEPSDFALRT IRF // ID Q5F594_NEIG1 Unreviewed; 187 AA. AC Q5F594; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Hypoxanthine phosphoribosyltransferase {ECO:0000313|EMBL:AAW90643.1}; GN ORFNames=NGO_2035 {ECO:0000313|EMBL:AAW90643.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90643.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90643.1; -; Genomic_DNA. DR RefSeq; WP_003694420.1; NC_002946.2. DR RefSeq; YP_209055.1; NC_002946.2. DR ProteinModelPortal; Q5F594; -. DR EnsemblBacteria; AAW90643; AAW90643; NGO_2035. DR GeneID; 3282712; -. DR KEGG; ngo:NGO2035; -. DR PATRIC; 20337853; VBINeiGon24812_2450. DR HOGENOM; HOG000236519; -. DR KO; K00760; -. DR OMA; TMDWMAV; -. DR OrthoDB; EOG693GNP; -. DR BioCyc; NGON242231:GI2G-1936-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Glycosyltransferase {ECO:0000313|EMBL:AAW90643.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90643.1}. FT DOMAIN 19 169 Pribosyltran. {ECO:0000259|Pfam:PF00156}. SQ SEQUENCE 187 AA; 20753 MW; 0217BCFBE63CBE65 CRC64; MTDLETKRLE TQAMLENADL LFDQGQCRAA LQKVADEITR DLGDKYPLLL PVMGGAVVFT GQLLPLLRFP LDFDYVHVSR YGDKLEGGAF NWKRMPDAEQ IRGRHVVVLD DILDEGHTMS AIQAKLLEMG AASCRAAVFA NKLIDKEKPV KADYVGLDVP NRYVFGYGMD AAGCWRNLGE IYALGGK // ID Q5F9V5_NEIG1 Unreviewed; 332 AA. AC Q5F9V5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 65. DE SubName: Full=DNA polymerase III subunit delta {ECO:0000313|EMBL:AAW89032.1}; GN ORFNames=NGO_0283 {ECO:0000313|EMBL:AAW89032.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89032.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89032.1; -; Genomic_DNA. DR RefSeq; WP_003687654.1; NC_002946.2. DR RefSeq; YP_207444.1; NC_002946.2. DR ProteinModelPortal; Q5F9V5; -. DR EnsemblBacteria; AAW89032; AAW89032; NGO_0283. DR GeneID; 3281638; -. DR KEGG; ngo:NGO0283; -. DR PATRIC; 20333541; VBINeiGon24812_0351. DR HOGENOM; HOG000256203; -. DR KO; K02340; -. DR OMA; RQQGFDE; -. DR OrthoDB; EOG6BCSPJ; -. DR BioCyc; NGON242231:GI2G-264-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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; IPR010372; DNA_pol3_delta_N. DR InterPro; IPR005790; DNA_polIII_delta. DR InterPro; IPR027417; P-loop_NTPase. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 18 187 DNA_pol3_delta. FT {ECO:0000259|Pfam:PF06144}. SQ SEQUENCE 332 AA; 36238 MW; 08F8F65D5EE3F892 CRC64; MAAHIGRIDT DAPLKPLYVI HGEEELLRIE AVDALRAAAK KQGYLNREAY TADASFDWNE LLQTAGNAGL FADLKLLELH IPNGKPGKNG GEALQDFAAR LPEDTVTLVL LPKLEKTRLQ SKWFAALAAK GEVWEAKPVG AAALPQWIRG RLDKIGLGIE ADALALFAER VEGNLLAARQ EIDKLALLYP KGHAVNIDEA QTAVANVARF DAFQLAGAWM KGDVPRVCRL LDGLEEEGEE PVLLLWAVAE DVRTLIRLAA ALKQGQSIQS VRNSLRLWGD KQTLAPLAVK RISVVRLLDA LKTCAQIDRI IKGAEDGDAW TVFKQLVVSL AE // ID Q5FA74_NEIG1 Unreviewed; 44 AA. AC Q5FA74; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88913.1}; GN ORFNames=NGO_0155 {ECO:0000313|EMBL:AAW88913.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88913.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88913.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88913; AAW88913; NGO_0155. DR PATRIC; 20333235; VBINeiGon24812_0200. DR HOGENOM; HOG000027839; -. DR OrthoDB; EOG6ZPT66; -. DR BioCyc; NGON242231:GI2G-143-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 44 AA; 4692 MW; FEF36A97630D2E7C CRC64; MPSERIFRSV LRLVGVSSDT VKRKFAGAGL SYAGKAAGES LYCL // ID Q5F6M5_NEIG1 Unreviewed; 291 AA. AC Q5F6M5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 68. 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 ECO:0000313|EMBL:AAW90162.2}; GN ORFNames=NGO_1526 {ECO:0000313|EMBL:AAW90162.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90162.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90162.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6M5; -. DR PRIDE; Q5F6M5; -. DR EnsemblBacteria; AAW90162; AAW90162; NGO_1526. DR PATRIC; 20336544; VBINeiGon24812_1820. DR HOGENOM; HOG000220041; -. DR OMA; LYDFLNY; -. DR OrthoDB; EOG6BGP03; -. DR BioCyc; NGON242231:GI2G-1428-MONOMER; -. DR UniPathway; UPA00946; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01939, ECO:0000256|RuleBase:RU361121, KW ECO:0000313|EMBL:AAW90162.2}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01939}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01939}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT REGION 45 47 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 122 123 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT REGION 209 211 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 85 85 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT METAL 87 87 Magnesium. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 157 157 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 187 187 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 240 240 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. FT BINDING 269 269 Substrate. {ECO:0000256|HAMAP- FT Rule:MF_01939}. SQ SEQUENCE 291 AA; 31626 MW; 3A121B759AB8797D CRC64; MSQHSAGARF RQAVKESNPL AVAGCVNAYF ARLATQSGFK AIYLSGGGVA ACSCGIPDLG ITTMEDVLID ARRITDNVDT PLLVDIDVGW GGAFNIARTI RNFERAGVAA VHIEDQVAQK RCGHRRNKAI VSKDEMVDRI KAAVDARVDE NFVIMARTDA LAVEGLDAAI ERAQACVEAG ADMIFPEAMT DLKMYRQFAD AVKVPVLANI TEFGATPLYT QSELAENGVS LVLYPLSSFR AASKAALNVY EAIMRDGTQA AVVDSMQTRA ELYEHLNYHA FDQKLDKLFQ K // ID Q5F518_NEIG1 Unreviewed; 277 AA. AC Q5F518; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AAW90719.1}; GN ORFNames=NGO_2121 {ECO:0000313|EMBL:AAW90719.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90719.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90719.1; -; Genomic_DNA. DR RefSeq; WP_010951410.1; NC_002946.2. DR RefSeq; YP_209131.1; NC_002946.2. DR EnsemblBacteria; AAW90719; AAW90719; NGO_2121. DR GeneID; 3282799; -. DR KEGG; ngo:NGO2121; -. DR PATRIC; 20338089; VBINeiGon24812_2567. DR HOGENOM; HOG000220800; -. DR KO; K04754; -. DR OMA; CRIAAHG; -. DR OrthoDB; EOG6677N2; -. DR BioCyc; NGON242231:GI2G-2013-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 277 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256018. SQ SEQUENCE 277 AA; 29640 MW; 7C69EF22B08AE46E CRC64; MKKTAYAILL LIGFASAPAF AETRPADPYE GYNRAVSKFN DQADRYIFAP AARGYRKVTP KPVRAGVSNF FNNLRDVVSF GSNILRLDIK RASEDLVRVG INTTFGLGGL IDIAGAGGVP DNKNTLGDTF ASWGWKNSNY FVLPVLGPST VRDALGTGIT SVYPPKNIVF HTPAGRWGTT AAAAVSTREG LLDLTDSLDE AAIDKYSYTR DLYMKVRARQ TGATPAEGTE DNIDIDIDEL VESAETGAAE PAVHEDSVSE TQAEAAGEAE TQPGTQP // ID Q5FAH4_NEIG1 Unreviewed; 85 AA. AC Q5FAH4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 41. DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxyl carrier protein {ECO:0000313|EMBL:AAW88813.1}; GN ORFNames=NGO_0046 {ECO:0000313|EMBL:AAW88813.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88813.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88813.1; -; Genomic_DNA. DR RefSeq; WP_003687268.1; NC_002946.2. DR RefSeq; YP_207225.1; NC_002946.2. DR EnsemblBacteria; AAW88813; AAW88813; NGO_0046. DR GeneID; 3282375; -. DR KEGG; ngo:NGO0046; -. DR PATRIC; 20332932; VBINeiGon24812_0051. DR HOGENOM; HOG000071338; -. DR OMA; KHILTVV; -. DR OrthoDB; EOG6RJV8K; -. DR BioCyc; NGON242231:GI2G-41-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 85 AA; 10160 MW; 593378887DF397A8 CRC64; MRKIKLPAHF PQKPPFFDIL LDIYRQLREN EHNFTVVSHH RKTVSEHHSA RFAPLPQAGC FLKNQRNNPP EHRQPLKEQK WICAN // ID Q5F648_NEIG1 Unreviewed; 512 AA. AC Q5F648; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE RecName: Full=Putative lipid II flippase MurJ {ECO:0000256|PIRNR:PIRNR002869}; GN ORFNames=NGO_1718 {ECO:0000313|EMBL:AAW90339.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90339.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90339.1; -; Genomic_DNA. DR RefSeq; WP_003689904.1; NC_002946.2. DR RefSeq; YP_208751.1; NC_002946.2. DR EnsemblBacteria; AAW90339; AAW90339; NGO_1718. DR GeneID; 3281263; -. DR KEGG; ngo:NGO1718; -. DR PATRIC; 20337030; VBINeiGon24812_2055. DR HOGENOM; HOG000263812; -. DR KO; K03980; -. DR OMA; IFAEGSF; -. DR OrthoDB; EOG6C0131; -. DR BioCyc; NGON242231:GI2G-1614-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|PIRNR:PIRNR002869, ECO:0000256|SAM:Phobius}; KW Peptidoglycan synthesis {ECO:0000256|PIRNR:PIRNR002869}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|PIRNR:PIRNR002869}. FT TRANSMEM 90 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 161 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 188 213 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 234 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 274 292 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 313 334 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 354 376 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 383 402 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 408 429 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 441 462 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 482 502 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 512 AA; 55558 MW; 3D9FA704E5AAFA6B CRC64; MNMLGALAKV GSLTMVSRVL GFVRDTVIAR AFGAGMATDA FFVAFKLPNL LRRVFAEGAF AQAFVPILAE YKETRSKEAT EAFIRHVAGM LSFVLIVVTA LGILAAPWVI YVSAPGFTKD ADKFQLSISL LRITFPYILL ISLSSFVGSI LNSYHKFGIP AFTPTFLNIS FIVFALFFVP YFDPPVTALA WAVFVGGILQ LGFQLPWLAK LGFLKLPKLN FKDAAVNRVM KQMAPAILGV SVAQISLVIN TIFASYLQSG SVSWMYYADR MMELPGGVLG AALGTILLPT LSKHSANQDT EQFSALLDWG LRLCMLLTLP AAAGLAVLSF PLVATLFMYR EFTLFDAQMT QHALIAYSFG LIGLIMIKVL ASGFYARQNI KTPVKIAIFT LICTQLMNLA FIGPLKHAGL SLAIGLGACI NAGLLFFLLR KHGIYRPGRG WAAFLAKMLL ALAVMCGGLW AAQACLPFEW AHAGGMRKAG QLCILIAVGG GLYFASLAAL GFRPRHFKRV ES // ID Q5F681_NEIG1 Unreviewed; 62 AA. AC Q5F681; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90306.1}; GN ORFNames=NGO_1681 {ECO:0000313|EMBL:AAW90306.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90306.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90306.1; -; Genomic_DNA. DR RefSeq; WP_003689830.1; NC_002946.2. DR RefSeq; YP_208718.1; NC_002946.2. DR EnsemblBacteria; AAW90306; AAW90306; NGO_1681. DR GeneID; 3281246; -. DR KEGG; ngo:NGO1681; -. DR PATRIC; 20336920; VBINeiGon24812_2004. DR HOGENOM; HOG000027894; -. DR OrthoDB; EOG696C2C; -. DR BioCyc; NGON242231:GI2G-1576-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 7100 MW; AECED858ED09A127 CRC64; MDIEGFENLK CRLKILEICS DGILNAEAPE IRYNRAPSVS HLQTFRRCGT RAAYPRKTSV FL // ID Q5F8I3_NEIG1 Unreviewed; 52 AA. AC Q5F8I3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89504.1}; GN ORFNames=NGO_0790 {ECO:0000313|EMBL:AAW89504.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89504.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89504.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89504; AAW89504; NGO_0790. DR PATRIC; 20334728; VBINeiGon24812_0936. DR HOGENOM; HOG000027814; -. DR OMA; SESGFAF; -. DR OrthoDB; EOG6PCQ3K; -. DR BioCyc; NGON242231:GI2G-744-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 52 AA; 5988 MW; 4EB37A2A264E5E5E CRC64; MRDVLFSCSV MMCCLIVYGM PSESGFAFQT ASDVQYFSLN HDNRLSGRRR LF // ID Q5F644_NEIG1 Unreviewed; 767 AA. AC Q5F644; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 81. DE SubName: Full=ATP-dependent DNA helicase RecQ {ECO:0000313|EMBL:AAW90343.1}; GN ORFNames=NGO_1722 {ECO:0000313|EMBL:AAW90343.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90343.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90343.1; -; Genomic_DNA. DR RefSeq; WP_003689907.1; NC_002946.2. DR RefSeq; YP_208755.1; NC_002946.2. DR ProteinModelPortal; Q5F644; -. DR EnsemblBacteria; AAW90343; AAW90343; NGO_1722. DR GeneID; 3281296; -. DR KEGG; ngo:NGO1722; -. DR PATRIC; 20337036; VBINeiGon24812_2058. DR HOGENOM; HOG000044388; -. DR KO; K03654; -. DR OMA; WDATEPA; -. DR OrthoDB; EOG6ZSPDC; -. DR BioCyc; NGON242231:GI2G-1618-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90343.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000256|RuleBase:RU000452, ECO:0000313|EMBL:AAW90343.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAW90343.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000452, KW ECO:0000313|EMBL:AAW90343.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 28 196 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT DOMAIN 217 367 Helicase C-terminal. FT {ECO:0000259|PROSITE:PS51194}. FT DOMAIN 525 605 HRDC. {ECO:0000259|PROSITE:PS50967}. FT DOMAIN 611 691 HRDC. {ECO:0000259|PROSITE:PS50967}. FT DOMAIN 692 767 HRDC. {ECO:0000259|PROSITE:PS50967}. SQ SEQUENCE 767 AA; 86099 MW; F240542156F97A0B CRC64; MTHRPTARQI LHEVFGYPEF RGRQEDVINT LAGGGSLTVL MPTGGGKSLC YQIPALMREG VAVVVSPLIA LMNDQVASLH VAGIEAAAVN SGTSADEARE IADKLAQGRL KLLYVAPERL VTDRFLRFLD QQTVSLFAID EAHCVSRWGH DFRPEYQQLG MLAERYPNIP RIALTATADA ATRADIKHYL HLDDASEFVS SFDRTNIYYQ VIEKNNGKKQ LLDFIRKEMT GQSGIVYCLS RKKVEDAAQF LRENGLNAIP YHAGLSMDVR EENQRRFTHE DNIIVVATVA FGMGIDKPDV RFVAHLDMPQ SVEHFYQESG RAGRDGLPAV SWLCYGLNDW VLLRERIAEG NSDEVQKQIE MQKLDAMLSV CETAACRRVL LLKHFGEASE PCGHCDNCLH PPVRFDGTVL VQKLLSCVYR AGQRFAAGYI TNLLRGKSDD WIRGNRHEQL STFGIGAELS DKEWRSVIRQ CISLGYLTVN IARYQALQLT EAAKKVLKGE TEVMLRPLKR DKPATRTLKD NWLRTEREER LWQALRVWRM KQAEAEGIPA YMIFGDKTLR DLVEKMPQNL NGLHDIYGLG EAKTERFGHG ILKVCQNAAD FSHDAVIRPQ TEREQQLRQK LEAWRYEQAR AENCALHTVL SDESLADMLA ATPETETDLE AVHGLGSVRA AKYGRDILAV CRPFSDGIDE TAKHKRCLMR ALIQWCNETA KHEQSEPYRI LSKAALRAIA AKQPEGLAEL AAVYGVGEEK AARYGAAVLA VLERDAV // ID Q5F7G1_NEIG1 Unreviewed; 318 AA. AC Q5F7G1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 83. DE RecName: Full=Glutathione synthetase {ECO:0000256|HAMAP-Rule:MF_00162}; DE EC=6.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00162}; DE AltName: Full=GSH synthetase {ECO:0000256|HAMAP-Rule:MF_00162}; DE AltName: Full=Glutathione synthase {ECO:0000256|HAMAP-Rule:MF_00162}; GN Name=gshB {ECO:0000256|HAMAP-Rule:MF_00162}; GN ORFNames=NGO_1217 {ECO:0000313|EMBL:AAW89876.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89876.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine = CC ADP + phosphate + glutathione. {ECO:0000256|HAMAP-Rule:MF_00162}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00162}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00162}; CC Note=Binds 1 magnesium or manganese ion per subunit. CC {ECO:0000256|HAMAP-Rule:MF_00162}; CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 2/2. {ECO:0000256|HAMAP- CC Rule:MF_00162}. CC -!- SIMILARITY: Belongs to the prokaryotic GSH synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00162}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|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; AE004969; AAW89876.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7G1; -. DR EnsemblBacteria; AAW89876; AAW89876; NGO_1217. DR PATRIC; 20335745; VBINeiGon24812_1431. DR HOGENOM; HOG000265022; -. DR OMA; MKPLHGH; -. DR OrthoDB; EOG6WMHWB; -. DR BioCyc; NGON242231:GI2G-1128-MONOMER; -. DR UniPathway; UPA00142; UER00210. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_00162}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Glutathione biosynthesis {ECO:0000256|HAMAP-Rule:MF_00162}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00162}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00162}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00162}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00162}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00162}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 128 313 ATP-grasp. {ECO:0000256|HAMAP- FT Rule:MF_00162, FT ECO:0000259|PROSITE:PS50975}. FT NP_BIND 154 210 ATP. {ECO:0000256|HAMAP-Rule:MF_00162}. FT METAL 284 284 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00162}. FT METAL 286 286 Magnesium or manganese. FT {ECO:0000256|HAMAP-Rule:MF_00162}. SQ SEQUENCE 318 AA; 35156 MW; F1D61D765160A825 CRC64; MKVLFIADPM ASFKTYKDTT YAMMREMAKR GWRLFHTLSG ELSVNGGLVT AQASAFEFSG AKNDDDHEWF KAADKVQTAL KEFDAVIMRT DPPFDMQYLY STQLLTLAEQ QGAKVFNSGR AMRDFNEKLA ILNFSRFTAP TLVTTRSADV RAFLKEHGDI IVKPLDGMGG MGIFRLTEKD PNIGSILETL MRFDSRTIMA QRYIPEIVHG DKRILIIGGE VVPYALARIP QNGETRGNLA AGGRGVAQEL DGRDREIAET LAPELKRSGI LLAGLDVIGS NLTEVNVTSP TGFQEIMKQK SFDVAAMFAD AVAAWSVR // ID Q5F519_NEIG1 Unreviewed; 92 AA. AC Q5F519; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 53. DE SubName: Full=Sulfate transporter {ECO:0000313|EMBL:AAW90718.1}; GN ORFNames=NGO_2120 {ECO:0000313|EMBL:AAW90718.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90718.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90718.1; -; Genomic_DNA. DR RefSeq; WP_003687106.1; NC_002946.2. DR RefSeq; YP_209130.1; NC_002946.2. DR DNASU; 3282800; -. DR EnsemblBacteria; AAW90718; AAW90718; NGO_2120. DR GeneID; 3282800; -. DR KEGG; ngo:NGO2120; -. DR PATRIC; 20338087; VBINeiGon24812_2566. DR HOGENOM; HOG000218745; -. DR KO; K07122; -. DR OMA; RADSACM; -. DR OrthoDB; EOG6VMTP1; -. DR BioCyc; NGON242231:GI2G-2012-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.30.750.24; -; 1. DR InterPro; IPR002645; STAS_dom. DR Pfam; PF13466; STAS_2; 1. DR SUPFAM; SSF52091; SSF52091; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 10 85 STAS. {ECO:0000259|Pfam:PF13466}. SQ SEQUENCE 92 AA; 10138 MW; 35855AB59D75B76B CRC64; MHTELKNGTL HIGGDITVKT LTGDAFGRFR QQCRLKETIA VDFGGVKRAD SACMSLLLEV LRGCKGSVRL TGIPESVRAL SELYEIKDWL KS // ID Q5F784_NEIG1 Unreviewed; 245 AA. AC Q5F784; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=MORN repeat variant family protein {ECO:0000313|EMBL:AAW89953.1}; GN ORFNames=NGO_1299 {ECO:0000313|EMBL:AAW89953.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89953.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89953.1; -; Genomic_DNA. DR RefSeq; WP_003691604.1; NC_002946.2. DR RefSeq; YP_208365.1; NC_002946.2. DR ProteinModelPortal; Q5F784; -. DR DNASU; 3281919; -. DR EnsemblBacteria; AAW89953; AAW89953; NGO_1299. DR GeneID; 3281919; -. DR KEGG; ngo:NGO1299; -. DR PATRIC; 20335945; VBINeiGon24812_1527. DR HOGENOM; HOG000219061; -. DR OMA; HGKEIKY; -. DR OrthoDB; EOG615VF2; -. DR BioCyc; NGON242231:GI2G-1211-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011652; MORN_2. DR Pfam; PF07661; MORN_2; 4. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256604. SQ SEQUENCE 245 AA; 27922 MW; 0D7925AB27354EF2 CRC64; MKKLSRIVFS IVLLGFSAAL PAQTYSVYFN QNGKLTATMS SAAYIRQYSV AAGIAHAQDF YYPSMKKYSE PYIVASTQIK SFVPTLQNGM LILWHFNGQK KMAGGFSKGK PDGEWVNWYP NGKKSAVMPY KNGLSEGTGY RYYRNGGKES EIQFKQNKAN GVWKQWYADG SIKTEMVMVN DEPAKILTWD ESGRLLSELS IRHHKRNGVV LEWYEDGSKK SEAVYQDDKL VRKTQWDKDG YLIEP // ID Q5F968_NEIG1 Unreviewed; 51 AA. AC Q5F968; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89269.1}; GN ORFNames=NGO_0531 {ECO:0000313|EMBL:AAW89269.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89269.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89269.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89269; AAW89269; NGO_0531. DR PATRIC; 20334108; VBINeiGon24812_0626. DR OMA; HLKTICR; -. DR OrthoDB; EOG6MD9DZ; -. DR BioCyc; NGON242231:GI2G-509-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 51 AA; 5196 MW; AD97B626C2F5C6C0 CRC64; MVADGERPHL KTICRLKTEG GSLSSLPSDG ISNAAFAPHA GGSPPSFLCL T // ID Q5F7L2_NEIG1 Unreviewed; 50 AA. AC Q5F7L2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89825.1}; GN ORFNames=NGO_1159 {ECO:0000313|EMBL:AAW89825.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89825.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89825.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89825; AAW89825; NGO_1159. DR PATRIC; 20335589; VBINeiGon24812_1358. DR OrthoDB; EOG6WDSSJ; -. DR BioCyc; NGON242231:GI2G-1072-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 50 AA; 5634 MW; 9C32784F4C0FAFA5 CRC64; MPSENRSAGF VVHYYVVLQD KAQGKAAGCI VATDNEKRGR CRLNRVLRRV // ID Q5F7Y2_NEIG1 Unreviewed; 462 AA. AC Q5F7Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 76. 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 ORFNames=NGO_1029 {ECO:0000313|EMBL:AAW89705.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89705.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89705.1; -; Genomic_DNA. DR RefSeq; WP_003691001.1; NC_002946.2. DR RefSeq; YP_208117.1; NC_002946.2. DR ProteinModelPortal; Q5F7Y2; -. DR SMR; Q5F7Y2; 4-459. DR EnsemblBacteria; AAW89705; AAW89705; NGO_1029. DR GeneID; 3282108; -. DR KEGG; ngo:NGO1029; -. DR PATRIC; 20335274; VBINeiGon24812_1203. DR HOGENOM; HOG000061737; -. DR KO; K01679; -. DR OMA; FELNVYN; -. DR OrthoDB; EOG6V1M4M; -. DR BioCyc; NGON242231:GI2G-950-MONOMER; -. DR UniPathway; UPA00223; UER01007. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00743}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00743, KW ECO:0000256|SAAS:SAAS00429438}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 49282 MW; ED4546A4FFA924F7 CRC64; MNTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV KKAAAATNVS LGRIKPEQAD LITQAADDVL NGRLDGQFPL VVWQTGSGTQ SNMNMNEVLA NRANEIAGTG LAAYRPVHPN DHVNHAQSTN DAFPTAIHVA AAIEINRHLI PAVKALRDTL DKKAQAFAPI VKIGRTHLQD ATPLTLGQEF SGYVSQLDHS LGRLNDALKG LYELALGGTA VGTGLNSHPE YAEIAAAKLA ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG ASGNFELNVY MPVIAYNLLQ SIRLLGDACN SFNENCAAGI EPVPEKIDYF LHHSLMLVTA LNRKIGYENA AKVAKTAYKN DKSLRETAVG LGLLTGEEFD ELVVPADMVH PR // ID Q5F672_NEIG1 Unreviewed; 48 AA. AC Q5F672; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90315.1}; GN ORFNames=NGO_1691 {ECO:0000313|EMBL:AAW90315.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90315.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90315.1; -; Genomic_DNA. DR RefSeq; WP_003703439.1; NC_002946.2. DR RefSeq; YP_208727.1; NC_002946.2. DR EnsemblBacteria; AAW90315; AAW90315; NGO_1691. DR GeneID; 3281197; -. DR KEGG; ngo:NGO1691; -. DR PATRIC; 20336946; VBINeiGon24812_2017. DR HOGENOM; HOG000071332; -. DR OrthoDB; EOG66B488; -. DR BioCyc; NGON242231:GI2G-1585-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5456 MW; D7F0D2A8B00601C1 CRC64; MCELSSMDLS ILPPFCGKDL FDLFIRLILS RFPSGLPVQY RFSEGCGR // ID Q5F6Z0_NEIG1 Unreviewed; 308 AA. AC Q5F6Z0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 83. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90047.1}; GN ORFNames=NGO_1399 {ECO:0000313|EMBL:AAW90047.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90047.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90047.1; -; Genomic_DNA. DR RefSeq; WP_003705795.1; NC_002946.2. DR RefSeq; YP_208459.1; NC_002946.2. DR ProteinModelPortal; Q5F6Z0; -. DR EnsemblBacteria; AAW90047; AAW90047; NGO_1399. DR GeneID; 3281242; -. DR KEGG; ngo:NGO1399; -. DR PATRIC; 20336193; VBINeiGon24812_1645. DR KO; K19340; -. DR OMA; MYVVETH; -. DR OrthoDB; EOG65J54C; -. DR BioCyc; NGON242231:GI2G-1312-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90047.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90047.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 308 AA; 33722 MW; ABDC21CE417CC7D4 CRC64; MPSENTKGTT MTTHHVELRK VTKRFGAQKA VSQVDLVLKA GESVGLAGHN GAGKSTIMKL ILGLITPTEG EVMLLGERTG SKAGARLRSQ IGYLPETVAL HPSLTGIETL DFYAKLKKQP LTQNRGLLER VGISQTAHRR VGTYSKGMRQ RLALAQALLG EPKVLLFDEP TTGPDPASRQ MFYEVVRELN GRGATILLST HALAELDGHA DRIVVMKNGV KVADGSMDEL HVQSGLPLTV NIRLNAPRTL SSRWQPLSDG ISYRAQCQAE ERMELLGELG SLSDLAYFDI HTPTLDEMYA RFLKREDV // ID Q5F5G1_NEIG1 Unreviewed; 118 AA. AC Q5F5G1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90576.1}; GN ORFNames=NGO_1966 {ECO:0000313|EMBL:AAW90576.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90576.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90576.1; -; Genomic_DNA. DR RefSeq; WP_002225728.1; NC_002946.2. DR RefSeq; YP_208988.1; NC_002946.2. DR EnsemblBacteria; AAW90576; AAW90576; NGO_1966. DR GeneID; 3282656; -. DR KEGG; ngo:NGO1966; -. DR PATRIC; 20337687; VBINeiGon24812_2370. DR HOGENOM; HOG000218701; -. DR OMA; VDWAYKN; -. DR OrthoDB; EOG63JRBD; -. DR BioCyc; NGON242231:GI2G-1866-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR031891; DMP12. DR Pfam; PF16779; DMP12; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 118 AA; 13810 MW; 71E8D7A0E64421E2 CRC64; MNEHNLLIFC LKDNVSISEY TEMVDWAYEN IQSETVVEIT ENQIIEYQNR GLWGLVSEIT DNWLFGPSEG DWLIDKESIL AVKEKLQNSD FSTEPLVKNI IHVLEYAIKN EKTVIFHF // ID Q5F7H3_NEIG1 Unreviewed; 758 AA. AC Q5F7H3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 75. DE SubName: Full=Ligand-gated channel {ECO:0000313|EMBL:AAW89864.2}; GN ORFNames=NGO_1205 {ECO:0000313|EMBL:AAW89864.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89864.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89864.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7H3; -. DR EnsemblBacteria; AAW89864; AAW89864; NGO_1205. DR PATRIC; 20335711; VBINeiGon24812_1414. DR HOGENOM; HOG000191365; -. DR OMA; RYDKALI; -. DR OrthoDB; EOG64R616; -. DR BioCyc; NGON242231:GI2G-1116-MONOMER; -. DR Proteomes; UP000000535; 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; -; 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. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003357}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW TonB box {ECO:0000256|RuleBase:RU003357}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 758 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364487. FT DOMAIN 55 154 Plug. {ECO:0000259|Pfam:PF07715}. FT DOMAIN 488 757 TonB_dep_Rec. {ECO:0000259|Pfam:PF00593}. SQ SEQUENCE 758 AA; 84929 MW; 8A1271FBBE830C27 CRC64; MAQITLKPIV LSILLINTPL LAQAHETEQS VGLETVSVVG KSRPRATSGL LHTSTASDKI ISGDTLRQKA VNLGDALDGV PGIHASQYGG GASAPVIRGQ TGRRIKVLNH HGETGDMADF SPDHAIMVDT ALSQQVEILR GPVTLLYSSG NVAGLVDVAD GKIPEKMPEN GVSGEAGLRL SSGNLEKLTS AGINIGLGKN FVLHTEGLYR KSGDYAVPRY RNLKRLPDSH ADSQTGSIGL SWVGEKGFIG AAYSDRRDRY GLPAHSHEYD DCHADIIWQK SLINKRYLQL YPHLLTEEDI DYDNPGLSCG FHDGDGAHAH THNGKPWIDL RNKRYELRAE WKQPFPGFEA LRVHLNRNDY HHDEKAGDAV ENFFNNKTHN ARIELRHQPI GRLKGSWGVQ YLGQKSSALS AIPETVQQPM LIDNNVRHYS FFGVEQANWD NFTLEGGVRV EKQKASIRYD KALIDRENYY NQPLPDLGAH RQTARSFALS GNWYFTPHHK LSLTASHQER LPSTQELYAH GKHVATNTFE VGNKHLNKER SNNIELALGY EGDRWQYNLA AYRNRFGNYI YAQTLNDGRG PKSIEDDSEM KLVRYNQSGA DFYGAEGEIY FKPTPRYRIG VSGDYVRGRL KNLPSLPGRE DPYGKRPFIA QADQNAPRIP AARLGFHLKT SLTDRIDANL DYYRVFAQNK LARYETRTPG HHMLNLGANY RRNTRYGEWN WYVKADNLLN QSVYAHSSFL SDTPQMGRSF TGGVNVKF // ID Q5F6D2_NEIG1 Unreviewed; 133 AA. AC Q5F6D2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90255.1}; GN ORFNames=NGO_1627 {ECO:0000313|EMBL:AAW90255.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90255.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90255.1; -; Genomic_DNA. DR RefSeq; WP_003691454.1; NC_002946.2. DR RefSeq; YP_208667.1; NC_002946.2. DR ProteinModelPortal; Q5F6D2; -. DR EnsemblBacteria; AAW90255; AAW90255; NGO_1627. DR GeneID; 3281398; -. DR KEGG; ngo:NGO1627; -. DR PATRIC; 20336792; VBINeiGon24812_1941. DR HOGENOM; HOG000130864; -. DR OMA; WILAYIC; -. DR OrthoDB; EOG6GN73C; -. DR BioCyc; NGON242231:GI2G-1524-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR031807; HicB-like. DR Pfam; PF15919; HicB_lk_antitox; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 133 AA; 14634 MW; 8F9C1EE9E3981FF3 CRC64; MFIPAALHKD EHSAYGVTIP DLPGCFSCGD TVEEAVANAR SAAYMHIDGM IEDGGFKNLA VSSIADLSQE PDYHGATWVM IEIDPAKISR QQIRFNVSWP QYLLDRVDEY TSANHETRSG FLAKAALLTM NQA // ID Q5F5F1_NEIG1 Unreviewed; 193 AA. AC Q5F5F1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 62. DE RecName: Full=5-formyltetrahydrofolate cyclo-ligase {ECO:0000256|RuleBase:RU361279}; DE EC=6.3.3.2 {ECO:0000256|RuleBase:RU361279}; GN ORFNames=NGO_1977 {ECO:0000313|EMBL:AAW90586.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90586.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90586.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5F1; -. DR EnsemblBacteria; AAW90586; AAW90586; NGO_1977. DR PATRIC; 20337719; VBINeiGon24812_2386. DR HOGENOM; HOG000007299; -. DR OMA; PERPSEM; -. DR OrthoDB; EOG6RVG1P; -. DR BioCyc; NGON242231:GI2G-1876-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW90586.2}; 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:UP000000535}. SQ SEQUENCE 193 AA; 22234 MW; 765FB7EE34253103 CRC64; MRNEEKRALR RELRGRRSQM GRDVRAAAAV KINRLLKRYI KRGRKIGVYW PMGKELRLGG FVRAAQKRGA KLYLPYIEPH TRRMWFTPYP ERGMERERKR GRAKLHVPQF AGRKIRVHGL SVLLVPLVGI DREGYRLGQA GGYYDATLSA MKYRLQAKTV GVGFACQLVD RLPREAHDLP LDGFVSEAGI LCF // ID Q5F7Q3_NEIG1 Unreviewed; 179 AA. AC Q5F7Q3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89784.1}; GN ORFNames=NGO_1117 {ECO:0000313|EMBL:AAW89784.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89784.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89784.1; -; Genomic_DNA. DR RefSeq; WP_003695998.1; NC_002946.2. DR RefSeq; YP_208196.1; NC_002946.2. DR EnsemblBacteria; AAW89784; AAW89784; NGO_1117. DR GeneID; 3281924; -. DR KEGG; ngo:NGO1117; -. DR PATRIC; 20335488; VBINeiGon24812_1310. DR HOGENOM; HOG000139022; -. DR OMA; FIIRAYE; -. DR OrthoDB; EOG67HK0Q; -. DR BioCyc; NGON242231:GI2G-1029-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025272; DUF4065. DR Pfam; PF13274; DUF4065; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 28 120 DUF4065. {ECO:0000259|Pfam:PF13274}. SQ SEQUENCE 179 AA; 20708 MW; EF110A3E54DD54CF CRC64; MLNAYDVADF FLSPFEEEDG EQISNLKLQK LLYYAQGYAL AILNRPLFAE NIEHWQHGPV VPCIYRTYKK YGGSPLPAAH IEPDKYADEE LVVLNRVRKE QGCYTAWALR NKTHQEAPWI QTRQGEVIGI ALMGEYFRHA LPQTDYNFNL EKLKTAVEDS FVSVPHFNGA DDLEKWLEQ // ID Q5FA89_NEIG1 Unreviewed; 178 AA. AC Q5FA89; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88898.1}; GN ORFNames=NGO_0140 {ECO:0000313|EMBL:AAW88898.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88898.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88898.1; -; Genomic_DNA. DR RefSeq; WP_003704878.1; NC_002946.2. DR RefSeq; YP_207310.1; NC_002946.2. DR EnsemblBacteria; AAW88898; AAW88898; NGO_0140. DR GeneID; 3281291; -. DR KEGG; ngo:NGO0140; -. DR PATRIC; 20333191; VBINeiGon24812_0178. DR HOGENOM; HOG000183101; -. DR OMA; QDRRWFP; -. DR OrthoDB; EOG6VF37Q; -. DR BioCyc; NGON242231:GI2G-128-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 61 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 123 146 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 152 173 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 178 AA; 19420 MW; 11E58AA5F7F0F6E4 CRC64; MPDKKGAYGC AVFLHRPPPF GGGVKIPYNP SPIFTCLGLF AMIPSYTYAA LAFSAFTSAT LLPGTSEAAF ALFVRNFPKH AYGALLCAGL ANGLGSMVSY WMGRLLPSRK MPSEKTLNLI RRFGIWLLAF AWLPVVGDAL PLTAGWLRLN PWTSGLMLVI GKTARYAFIL WGMQYYAA // ID Q5F8B5_NEIG1 Unreviewed; 109 AA. AC Q5F8B5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89572.1}; GN ORFNames=NGO_0871 {ECO:0000313|EMBL:AAW89572.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89572.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89572.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89572; AAW89572; NGO_0871. DR PATRIC; 20334915; VBINeiGon24812_1027. DR HOGENOM; HOG000071283; -. DR OMA; FTLACIM; -. DR OrthoDB; EOG6K9QK4; -. DR BioCyc; NGON242231:GI2G-814-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 53 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 109 AA; 12188 MW; 4E32032F25FE2135 CRC64; MFKRPEEIIV LILAVLWIAG TYFLAALFGA DAYTVLKITA LTLLWSAASF LLWQKKPQPA YLAAAARLPD HLLVAVSESI GRTRFFTLAC IMDVQNHLSP DSRNRRLSV // ID Q5FAA2_NEIG1 Unreviewed; 71 AA. AC Q5FAA2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88885.1}; GN ORFNames=NGO_0125 {ECO:0000313|EMBL:AAW88885.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88885.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88885.1; -; Genomic_DNA. DR RefSeq; WP_003687400.1; NC_002946.2. DR RefSeq; YP_207297.1; NC_002946.2. DR EnsemblBacteria; AAW88885; AAW88885; NGO_0125. DR GeneID; 3281221; -. DR KEGG; ngo:NGO0125; -. DR PATRIC; 20333153; VBINeiGon24812_0160. DR OrthoDB; EOG6BW57G; -. DR BioCyc; NGON242231:GI2G-114-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 63 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 71 AA; 8239 MW; 6F05B7252823565D CRC64; MDFAHYLKHW KAAVLIYLAI SILTDILCYF LNFDGVFYKG RFFSVTVAGP VGALSFLAYL LYLKREENRS H // ID Q5FAH1_NEIG1 Unreviewed; 177 AA. AC Q5FAH1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88816.1}; GN ORFNames=NGO_0049 {ECO:0000313|EMBL:AAW88816.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88816.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88816.1; -; Genomic_DNA. DR RefSeq; WP_003692498.1; NC_002946.2. DR RefSeq; YP_207228.1; NC_002946.2. DR EnsemblBacteria; AAW88816; AAW88816; NGO_0049. DR GeneID; 3282365; -. DR KEGG; ngo:NGO0049; -. DR BioCyc; NGON242231:GI2G-44-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 177 AA; 20987 MW; 2270094713B19D08 CRC64; MFSDIYLNPK NYFGIEKRLP FKAFWDNGGQ CYLDLKVVDG KIIALCGQLI NYTNTSIVNA AEEVYRSIID YLISNEILIV RTKFSFKNIF STNEKKYKEI EKEINKFLYK NMDWYLFFNN DITLDPYTGN DLIWHVQIDP NDGGAQFLET YQSWEKLQQK YPNITFSYDK NDLILTK // ID Q5F8Y5_NEIG1 Unreviewed; 463 AA. AC Q5F8Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 73. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW89352.2}; GN ORFNames=NGO_0624 {ECO:0000313|EMBL:AAW89352.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89352.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89352.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8Y5; -. DR EnsemblBacteria; AAW89352; AAW89352; NGO_0624. DR PATRIC; 20334332; VBINeiGon24812_0738. DR HOGENOM; HOG000218987; -. DR OMA; PMIHTEP; -. DR OrthoDB; EOG60PH76; -. DR BioCyc; NGON242231:GI2G-592-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 28 109 Acyl-CoA_dh_N. FT {ECO:0000259|Pfam:PF02771}. FT DOMAIN 222 359 Acyl-CoA_dh_1. FT {ECO:0000259|Pfam:PF00441}. SQ SEQUENCE 463 AA; 52285 MW; 5CB57C347238EA03 CRC64; MDTAAFLKHI ESAFRRIFSD GIDLMRYLPE DKWLALKQAG LLLPFLDKKH GGRKGSQFEI QEVLRIAGHY GVPVTLRTGI EGALVLQPLQ EFGGEAQVAQ GLDMIFKGEG GGLGVTEPET SGAAIAREMQ SCYEYTDEQT IYVNAAKYWQ GNSQSDFLLV AAKERKNGKL AKVIDLLLVP KTYIRCETLA SEGLRAVRYA VNRIDAEMPA TAVMKLSRGD AAGLRAFQNI FIRSRLQLIG MTHGIMEYIL DNLNRYVRND IRFVDYERRE IQRRHQVSEI LYRYVCHSVS PVAPVAHQLM EANIVKTLAT EYTYAAAQML QKLLGAKGFE RGHPAGNIAI DIRPFTIFEG PNDMLYAEIY DQFVRATAEE KEAGIKLDKN QTLLDRLQTD VRFAAVARDY ALPEDIRSFL QEHTLTDACA LQKVFIGKII ARLFVFVQEE HEDTTAFLLN DIRKDILDCR YCG // ID Q5F9P7_NEIG1 Unreviewed; 376 AA. AC Q5F9P7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 59. DE SubName: Full=Twitching motility protein PilT {ECO:0000313|EMBL:AAW89090.2}; GN ORFNames=NGO_0346 {ECO:0000313|EMBL:AAW89090.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89090.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89090.2; -; Genomic_DNA. DR RefSeq; WP_003704392.1; NC_002946.2. DR RefSeq; YP_207502.2; NC_002946.2. DR ProteinModelPortal; Q5F9P7; -. DR EnsemblBacteria; AAW89090; AAW89090; NGO_0346. DR GeneID; 3283037; -. DR KEGG; ngo:NGO0346; -. DR PATRIC; 20333689; VBINeiGon24812_0422. DR HOGENOM; HOG000008425; -. DR KO; K02670; -. DR OMA; TIRDMIK; -. DR OrthoDB; EOG6JMMWM; -. DR BioCyc; NGON242231:GI2G-325-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 203 217 T2SP_E. {ECO:0000259|PROSITE:PS00662}. SQ SEQUENCE 376 AA; 42215 MW; 73D1EBDEEA10C69A CRC64; MFTDENMTAK EELFAWLRHM NKNKGSDLFV TTHFPPAMKL DGKITRITDE PLTAEKCMEI AFSIMSAKQA EEFSSTNECN FAISLPDTSR FRVNAMIQRG ATALVFRAIT SKIPKFESLN LPPALKDVAL KKRGLVIFVG GTGSGKSTSL ASLIDYRNEN SFGHIITIED PIEFVHEHKN CIITQREVGV DTENWMAALK NTLRQAPDVI LIGEIRDRET MDYAIAFAET GHLCMATLHA NSTNQALDRI INFFPEERRE QLLTDLSLNL QAFISQRLVP RDGGKGRVAA VEVLLNSPLI SELIHNGNIH EIKEVMKKST TLGMQTFDQH LYQLYEKGEI SLQDALKNAD SAHDLRLAVQ LRSRRAQSSD PDLELL // ID Q5F6G0_NEIG1 Unreviewed; 427 AA. AC Q5F6G0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90227.1}; GN ORFNames=NGO_1599 {ECO:0000313|EMBL:AAW90227.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90227.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90227.1; -; Genomic_DNA. DR RefSeq; WP_003689532.1; NC_002946.2. DR RefSeq; YP_208639.1; NC_002946.2. DR ProteinModelPortal; Q5F6G0; -. DR TCDB; 2.A.1.25.3; the major facilitator superfamily (mfs). DR EnsemblBacteria; AAW90227; AAW90227; NGO_1599. DR GeneID; 3281643; -. DR KEGG; ngo:NGO1599; -. DR PATRIC; 20336734; VBINeiGon24812_1913. DR HOGENOM; HOG000217208; -. DR KO; K08218; -. DR OMA; GYFSWIA; -. DR OrthoDB; EOG6PS5R8; -. DR BioCyc; NGON242231:GI2G-1495-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 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; 46381 MW; 6113AC1E24E14632 CRC64; MTASKSGFIG QIFSRNMLVC IFTGFASGLP LYFLINLIPA WLRSEQVDLK SIGLMALIGL PFTWKFLWSP LMDAVRLPVL GRRRGWMLLT QAGLLAALAA YAFLNPRNHL PLIAGLSVLV AFFSASQDIV LDAFRREILS DEELGLGNSV HVNAYRVAAL IPGSLSLVLA DRMPWSEVFV ITSLFMLPGL LMTLFLAHEP VLPPSVPKTL KQTVVEPFKE FFMRKGIASA VCVLLFIFLY KLGDSMATAL ATPFYLDMGF SKTDIGLIAK NAGLWPAVAA GILGGVWMLK IGVNKALWLF GAVQAITVLG FVWLAGFGHF DTVGTGERLM LAAVIGAEAV GVGLGTAAFV SYMARETNPA FTATQLALFT SLSAVPRTVI NSFAGYLIEW MGYVPFFRLC FILALPGMLL LLKVAPWNGE KTQDAGR // ID Q5F9Y7_NEIG1 Unreviewed; 65 AA. AC Q5F9Y7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 09-DEC-2015, entry version 49. DE SubName: Full=Transposase {ECO:0000313|EMBL:AAW89000.2}; GN ORFNames=NGO_0247 {ECO:0000313|EMBL:AAW89000.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89000.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89000.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89000; AAW89000; NGO_0247. DR PATRIC; 20333445; VBINeiGon24812_0304. DR HOGENOM; HOG000218835; -. DR OMA; MVHGHKA; -. DR OrthoDB; EOG6JMN06; -. DR BioCyc; NGON242231:GI2G-231-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7293 MW; D3D8906B7835D2AF CRC64; MVHGHKARAD GLVQQPDKAA EANEEEYLTK ALSQNLLSTL DAALARFPED AWFQEIKQDA QKHFA // ID Q5F6S3_NEIG1 Unreviewed; 303 AA. AC Q5F6S3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=LysR family transcriptional regulator {ECO:0000313|EMBL:AAW90114.1}; GN ORFNames=NGO_1474 {ECO:0000313|EMBL:AAW90114.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90114.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90114.1; -; Genomic_DNA. DR RefSeq; WP_003689351.1; NC_002946.2. DR RefSeq; YP_208526.1; NC_002946.2. DR ProteinModelPortal; Q5F6S3; -. DR EnsemblBacteria; AAW90114; AAW90114; NGO_1474. DR GeneID; 3281621; -. DR KEGG; ngo:NGO1474; -. DR PATRIC; 20336383; VBINeiGon24812_1740. DR HOGENOM; HOG000233519; -. DR OMA; CESPLRI; -. DR OrthoDB; EOG6Q8J00; -. DR BioCyc; NGON242231:GI2G-1379-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 303 AA; 33804 MW; 225B2E12EC2C5B83 CRC64; MKTNSEELTV FVQVVESGSF SRAAEQLEMA NSAVSRIVKR LEEKLGVNLL NRTTRQLNLT EEGAQYFRRA QRILQEMAAA ETEMLAVHEV PQGVLRVDSA MPMVLHLLAP LAAKFNERYP HIRLSLVSSE GYINLIERKV DIALRAGELD DSGLRARHLF DSHFRVVASP EYLAKHGTPQ SAEDLANHQC LGFTEPGSLN TWAVLDAQGN PYKISPHFTA SSGEILRSLC LSSCGIACLS DFLVDNDITE GKLIPLFAEQ TSNKTHPFNA VYYSDKAVNL RLRVFLDFLV KELGKNMNRT NTK // ID Q5F509_NEIG1 Unreviewed; 130 AA. AC Q5F509; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW90728.1}; GN ORFNames=NGO_2131 {ECO:0000313|EMBL:AAW90728.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90728.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90728.1; -; Genomic_DNA. DR RefSeq; WP_003690431.1; NC_002946.2. DR RefSeq; YP_209140.1; NC_002946.2. DR ProteinModelPortal; Q5F509; -. DR EnsemblBacteria; AAW90728; AAW90728; NGO_2131. DR GeneID; 3282790; -. DR KEGG; ngo:NGO2131; -. DR PATRIC; 20338111; VBINeiGon24812_2578. DR HOGENOM; HOG000255240; -. DR KO; K03600; -. DR OMA; AFPVERS; -. DR OrthoDB; EOG6X6RFF; -. DR BioCyc; NGON242231:GI2G-2022-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 130 AA; 14698 MW; 2545597DA19D3AD5 CRC64; MPTSTKPYIL RALCEWCSDN SLTPHILVWV NEHTRVPMQY VRDNEIMLNI GATATQNLRI DNDWISFSAR FGGQAHDIWI PVGHVLSLFA RETGEGMGFE LEEYRPDTPS ENTSAETAPR PAKKGLKLVK // ID Q5F517_NEIG1 Unreviewed; 160 AA. AC Q5F517; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90720.1}; GN ORFNames=NGO_2122 {ECO:0000313|EMBL:AAW90720.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90720.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90720.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90720; AAW90720; NGO_2122. DR PATRIC; 20338091; VBINeiGon24812_2568. DR HOGENOM; HOG000218746; -. DR OMA; QMFREWF; -. DR OrthoDB; EOG6WT8DD; -. DR BioCyc; NGON242231:GI2G-2014-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 160 AA; 18557 MW; 7928D54C4F88B9F4 CRC64; MPSENPCSDG IPFRRNGQSD TTDWAIIPFL RIPRDSKGKT MYEVNRSVFV LIPLEPFWNW LQTLPGNHLD GLTLEDIQAD ANSYLVRPCE TADEVWDEIE ARFEDIFAAE LADWCEDERE WPALDADIFN EWFDIQLSTV ITDLEHEPLA REAFQPINLN // ID Q5F5G7_NEIG1 Unreviewed; 67 AA. AC Q5F5G7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90570.1}; GN ORFNames=NGO_1959 {ECO:0000313|EMBL:AAW90570.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90570.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90570.1; -; Genomic_DNA. DR RefSeq; WP_003688134.1; NC_002946.2. DR RefSeq; YP_208982.1; NC_002946.2. DR EnsemblBacteria; AAW90570; AAW90570; NGO_1959. DR GeneID; 3282662; -. DR KEGG; ngo:NGO1959; -. DR PATRIC; 20337667; VBINeiGon24812_2360. DR OrthoDB; EOG6NSGRD; -. DR BioCyc; NGON242231:GI2G-1860-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR006231; MQO. DR Pfam; PF06039; Mqo; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 67 AA; 7024 MW; 1A4AF8624BCEDBEF CRC64; MLMPPEAQVF ITAGRRVQII KQAPEKGGIP KSGTEIAARI GGIPQPAGET VGSSRNVGYF RPPFSGC // ID Q5F9N6_NEIG1 Unreviewed; 322 AA. AC Q5F9N6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Methyltransferase {ECO:0000313|EMBL:AAW89101.1}; GN ORFNames=NGO_0357 {ECO:0000313|EMBL:AAW89101.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89101.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89101.1; -; Genomic_DNA. DR RefSeq; WP_003687768.1; NC_002946.2. DR RefSeq; YP_207513.1; NC_002946.2. DR REBASE; 12956; S.NgoAVIII. DR EnsemblBacteria; AAW89101; AAW89101; NGO_0357. DR GeneID; 3283034; -. DR KEGG; ngo:NGO0357; -. DR PATRIC; 20333709; VBINeiGon24812_0432. DR HOGENOM; HOG000071242; -. DR OMA; CITANRY; -. DR OrthoDB; EOG6FV859; -. DR BioCyc; NGON242231:GI2G-336-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW89101.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89101.1}. FT DOMAIN 2 107 Methylase_S. {ECO:0000259|Pfam:PF01420}. FT DOMAIN 163 314 Methylase_S. {ECO:0000259|Pfam:PF01420}. SQ SEQUENCE 322 AA; 36323 MW; 45DB7160C772D4D4 CRC64; MVELQEIFDV SYGSKLDLNK MSSFNPTINF VGRSGKNNGV TASVDLLKNT KPYPAGLLTV ALGGSVLSTF LQNKPFYTAQ NVAVLNPKTE MTEQQKLFYC AAIFANAYRF SACGREANRT LRQLFVPSLD EIPSWVESVN LNPSAGVTEP KLKESLDLPV VRQSKRLDEI FTIQNGIAAT KLKEFEQRQK DTVVYIRPAS TQARTLRSYI ARDSVDEKHI FPCHTLFTST NGEGSHTYSY VSTCEFVANS DVAVLTPIQS DMPIEVKLYY AKCITANRYL FSYGRKPKGE KLKSIMLPYF DQQEDFDYIC RFIHTLLFSN NL // ID Q5F6I2_NEIG1 Unreviewed; 54 AA. AC Q5F6I2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90205.1}; GN ORFNames=NGO_1576 {ECO:0000313|EMBL:AAW90205.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90205.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90205.1; -; Genomic_DNA. DR RefSeq; WP_003689498.1; NC_002946.2. DR RefSeq; YP_208617.1; NC_002946.2. DR EnsemblBacteria; AAW90205; AAW90205; NGO_1576. DR GeneID; 3281090; -. DR KEGG; ngo:NGO1576; -. DR OMA; EYCNSTR; -. DR OrthoDB; EOG6X9MXD; -. DR BioCyc; NGON242231:GI2G-1473-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 54 AA; 6438 MW; 696A69DCB73A9020 CRC64; MNLNPNPNLH PDSDDSRFRK PPKKTNPAKA GFVSHHRYRP TFHEYCNSTR YKIR // ID Q5FA28_NEIG1 Unreviewed; 378 AA. AC Q5FA28; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574}; GN ORFNames=NGO_0206 {ECO:0000313|EMBL:AAW88959.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88959.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88959.1; -; Genomic_DNA. DR RefSeq; WP_010951012.1; NC_002946.2. DR RefSeq; YP_207371.1; NC_002946.2. DR ProteinModelPortal; Q5FA28; -. DR EnsemblBacteria; AAW88959; AAW88959; NGO_0206. DR GeneID; 3281089; -. DR KEGG; ngo:NGO0206; -. DR PATRIC; 20333349; VBINeiGon24812_0257. DR HOGENOM; HOG000263815; -. DR KO; K02055; -. DR OMA; SVYPPQA; -. DR OrthoDB; EOG66XBH9; -. DR BioCyc; NGON242231:GI2G-189-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Periplasm {ECO:0000256|PIRNR:PIRNR019574}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|PIRNR:PIRNR019574}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 378 Putrescine-binding periplasmic protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255567. SQ SEQUENCE 378 AA; 41182 MW; EB65E2E8D11E0E25 CRC64; MKKTLVAAIL SLALTACGGG SDTAAQTPSA KPEAEQSGKL NIYNWSDYVD PETVAAFEKE TGIKMRSDYY DSNETLEAKV LTGKSGYDLT APSIANVGRQ IKAGAYQKID KAQIPHYGNI DKDLLKMMEA VDPGNEYAVP YFWGINTLAI NTRQVQKALG TDKLPENEWD LVFKPEYTAK LKSCGISYFD SAIEQIPLAL HYLGKDPNSE NPEDIKAAVD MMKAVRGDVK RFSSSGYIDD MAAGNLCAAI GYGGDLNIAK TRAEEAANGV EIKVLTPKTG VGVWVDSFMI PRDAQNVANA HRYIDYTLRP EVAAKNGSFV TYAPASRPAR ELMDEKYTSD ASIFPTKELM EKSFIVSPKS AESVKLGVKL WQGLKAGK // ID Q5F9M4_NEIG1 Unreviewed; 119 AA. AC Q5F9M4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 09-DEC-2015, entry version 57. DE SubName: Full=Phage-shock protein {ECO:0000313|EMBL:AAW89113.2}; GN ORFNames=NGO_0369 {ECO:0000313|EMBL:AAW89113.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89113.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89113.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9M4; -. DR EnsemblBacteria; AAW89113; AAW89113; NGO_0369. DR PATRIC; 20333739; VBINeiGon24812_0447. DR HOGENOM; HOG000247776; -. DR OMA; GHRCRRF; -. DR OrthoDB; EOG68DD6K; -. DR BioCyc; NGON242231:GI2G-348-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5005364419. FT DOMAIN 33 115 Rhodanese. {ECO:0000259|PROSITE:PS50206}. SQ SEQUENCE 119 AA; 12985 MW; 40FAF85C7CFE2BF8 CRC64; MNIKQLITAA LIASAAFATQ AAPQKPVSAA QTAQHSAVWI DVRSEQEFSE GHLHNAVNIP VDQIVRRIYE AAPDKDTPVN LYCRSGRRAE AALQELKKAG YTNVANHGGY EDLLKKGMK // ID Q5F9L5_NEIG1 Unreviewed; 120 AA. AC Q5F9L5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=VanZ family protein {ECO:0000313|EMBL:AAW89122.1}; GN ORFNames=NGO_0378 {ECO:0000313|EMBL:AAW89122.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89122.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89122.1; -; Genomic_DNA. DR RefSeq; WP_003690830.1; NC_002946.2. DR RefSeq; YP_207534.1; NC_002946.2. DR EnsemblBacteria; AAW89122; AAW89122; NGO_0378. DR GeneID; 3281961; -. DR KEGG; ngo:NGO0378; -. DR PATRIC; 20333759; VBINeiGon24812_0457. DR HOGENOM; HOG000218865; -. DR OMA; FAQIXLL; -. DR OrthoDB; EOG6HXJ5Z; -. DR BioCyc; NGON242231:GI2G-357-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 38 113 VanZ. {ECO:0000259|Pfam:PF04892}. SQ SEQUENCE 120 AA; 12912 MW; 51AE3BF036210419 CRC64; MKLPRNRFSL LSALWFAGGI YSLLFKAADT APPPFPHFDK AAHLALFFAQ ILLLAKAFKT GKLPIPYRSL IAFAFCFAVG SECAQAWFTA TRTGSLGDVL ADLTGAALAL FAARSACRPD // ID Q5F5K1_NEIG1 Unreviewed; 160 AA. AC Q5F5K1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:AAW90536.1}; GN ORFNames=NGO_1923 {ECO:0000313|EMBL:AAW90536.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90536.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90536.1; -; Genomic_DNA. DR RefSeq; WP_003688077.1; NC_002946.2. DR RefSeq; YP_208948.1; NC_002946.2. DR ProteinModelPortal; Q5F5K1; -. DR EnsemblBacteria; AAW90536; AAW90536; NGO_1923. DR GeneID; 3282855; -. DR KEGG; ngo:NGO1923; -. DR PATRIC; 20337584; VBINeiGon24812_2319. DR HOGENOM; HOG000218689; -. DR OMA; WKDGTAQ; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NGON242231:GI2G-1826-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256188. FT DOMAIN 6 157 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 160 AA; 17610 MW; 29AC6F90C168B6F3 CRC64; MKRLNLAAIA LAATFAAHTA SADELAGWKD NTPQNLQSLK APVRIANLWA TWCGPCRKEM PAMSKWYKAQ KKGSVDMVGI ALDTSDNIGN FLKQTPVSYP IWRYTGANSR NFMKSYGNNV GVLPFTVVEA PKCGYRQTIT GEVNEKSLTE AVKLAHSKCR // ID Q5F6A9_NEIG1 Unreviewed; 126 AA. AC Q5F6A9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90278.1}; GN ORFNames=NGO_1651 {ECO:0000313|EMBL:AAW90278.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90278.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90278.1; -; Genomic_DNA. DR RefSeq; WP_003689781.1; NC_002946.2. DR RefSeq; YP_208690.1; NC_002946.2. DR ProteinModelPortal; Q5F6A9; -. DR EnsemblBacteria; AAW90278; AAW90278; NGO_1651. DR GeneID; 3281335; -. DR KEGG; ngo:NGO1651; -. DR PATRIC; 20336846; VBINeiGon24812_1968. DR HOGENOM; HOG000152348; -. DR OMA; CDMIYTV; -. DR OrthoDB; EOG6K6V8J; -. DR BioCyc; NGON242231:GI2G-1547-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 126 AA; 14386 MW; 0F306F5BDF344F91 CRC64; MPLKFQPRER SVIMCDFRGY EEPEMVKKRP VVVIARNRHN GKLVTVVPLS STEPVPLADC HHKMSENPLP DKPHIQCRAK CDMTATVGLA RLDRYKPKGR DRCIPIISEE DFQAVKTAVA KAFKLY // ID Q5FA16_NEIG1 Unreviewed; 113 AA. AC Q5FA16; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88971.1}; GN ORFNames=NGO_0218 {ECO:0000313|EMBL:AAW88971.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88971.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88971.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88971; AAW88971; NGO_0218. DR PATRIC; 20333375; VBINeiGon24812_0270. DR HOGENOM; HOG000218826; -. DR OMA; LGKEIRH; -. DR OrthoDB; EOG6HMXFG; -. DR BioCyc; NGON242231:GI2G-201-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025402; DUF4375. DR Pfam; PF14300; DUF4375; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 31 102 DUF4375. {ECO:0000259|Pfam:PF14300}. SQ SEQUENCE 113 AA; 12801 MW; AF60023B8CCF7D7B CRC64; MTDTDTQADR FEQMMRQAVD KLFEQHDGKL ESMDGREQEL VLIWRAEADI GNGGILQFVC NWGFPAAEKT CSVLKKIGAV HSAMLIHRAA DALGKEIRHL QSEGKNLKEM WDI // ID Q5F953_NEIG1 Unreviewed; 159 AA. AC Q5F953; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 60. DE RecName: Full=Cys-tRNA(Pro)/Cys-tRNA(Cys) deacylase {ECO:0000256|PIRNR:PIRNR006181}; DE EC=4.2.-.- {ECO:0000256|PIRNR:PIRNR006181}; GN ORFNames=NGO_0550 {ECO:0000313|EMBL:AAW89284.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89284.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89284.1; -; Genomic_DNA. DR RefSeq; WP_003691371.1; NC_002946.2. DR RefSeq; YP_207696.1; NC_002946.2. DR ProteinModelPortal; Q5F953; -. DR EnsemblBacteria; AAW89284; AAW89284; NGO_0550. DR GeneID; 3282124; -. DR KEGG; ngo:NGO0550; -. DR PATRIC; 20334152; VBINeiGon24812_0648. DR HOGENOM; HOG000262089; -. DR OMA; EHPYDYV; -. DR OrthoDB; EOG6XDH1K; -. DR BioCyc; NGON242231:GI2G-524-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|PIRNR:PIRNR006181}; KW Protein biosynthesis {ECO:0000256|PIRNR:PIRNR006181}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 36 147 tRNA_edit. {ECO:0000259|Pfam:PF04073}. SQ SEQUENCE 159 AA; 17653 MW; 0E7156924B4D1B4B CRC64; MSKHTYPITP AVRVLRENGI EFEPFTYAYE EHGGTAQFAR LFGKDEHLVI KTIVLQDENG KGPIVLMHGD KQISTRNLAR HLGAKHIEPA APAQANKWTG YLVGGTTPFG IRTKLDIYVE QSVMDLETIY INGGKRGFII GIRPDDLNIL NPKTIQAAV // ID Q5F9G6_NEIG1 Unreviewed; 74 AA. AC Q5F9G6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89171.1}; GN ORFNames=NGO_0428 {ECO:0000313|EMBL:AAW89171.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89171.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89171.1; -; Genomic_DNA. DR RefSeq; WP_003706621.1; NC_002946.2. DR RefSeq; YP_207583.1; NC_002946.2. DR EnsemblBacteria; AAW89171; AAW89171; NGO_0428. DR GeneID; 3281815; -. DR KEGG; ngo:NGO0428; -. DR PATRIC; 20333871; VBINeiGon24812_0513. DR HOGENOM; HOG000218886; -. DR OrthoDB; EOG657JHF; -. DR BioCyc; NGON242231:GI2G-406-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 72 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 74 AA; 8348 MW; 150F5D61F8F4D951 CRC64; MMKNKYILIK AAIGITAISI FYLLTQGSIG KTEEPSYFLM FMFLNSLWFE ENKTVMAAVT AMIAAHFIFV ALSD // ID Q5F7X9_NEIG1 Unreviewed; 460 AA. AC Q5F7X9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 81. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89708.1}; GN ORFNames=NGO_1032 {ECO:0000313|EMBL:AAW89708.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89708.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89708.1; -; Genomic_DNA. DR RefSeq; WP_010951164.1; NC_002946.2. DR RefSeq; YP_208120.1; NC_002946.2. DR ProteinModelPortal; Q5F7X9; -. DR EnsemblBacteria; AAW89708; AAW89708; NGO_1032. DR GeneID; 3282556; -. DR KEGG; ngo:NGO1032; -. DR PATRIC; 20335284; VBINeiGon24812_1208. DR HOGENOM; HOG000264695; -. DR OMA; VQLSMWV; -. DR OrthoDB; EOG6T7N4X; -. DR BioCyc; NGON242231:GI2G-953-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 73 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 103 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 130 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 142 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 169 190 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 219 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 300 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 306 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 345 366 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 372 392 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 16 397 MFS. {ECO:0000259|PROSITE:PS50850}. SQ SEQUENCE 460 AA; 48875 MW; 01C2949623D2BFEB CRC64; MARDNRIQMF PHEWRASTTL SGVYALRMLG MFLVLPVLAI YAASLPGAED NKTLVGLAMG IYGLTQALLQ LPLGIASDKF GRKKTIYVGL VVFAAGSFLA AAADTLPMLV AARAIQGAGA VSAAVTALLA DLTRDGVRTR AMAMIGLSIG LTFSVSLVVA PMIADVAGVR GLFMLTGILT AISIGVVAWM TPDPEVSKLH EDTQAQPSRI GEVLKNRRLL TLDFGIFALH AAQMALFTAL PFAMTRLGLE KIQHWKVYLP STITGLVVMV PLIIVGETRN KLKQVFVLGI VCIAAAQLGL LSGMHSIWLI TAYLVVYFIG FNVLEASLPS MVSKIAPSDL KGTAMGVYNT MQSLGLFAGG AAGGLLFQKC GFAGVFAFCS ILMLLWLVIA VLSPAPKPVK NLSYPVGGVW QGNRDGLQRA LLQLEGVEDI GFSFDGQTVY LKVLQKGFDQ AAAEKIITGV // ID Q5F984_NEIG1 Unreviewed; 77 AA. AC Q5F984; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89253.1}; GN ORFNames=NGO_0515 {ECO:0000313|EMBL:AAW89253.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89253.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89253.1; -; Genomic_DNA. DR RefSeq; WP_003692884.1; NC_002946.2. DR RefSeq; YP_207665.1; NC_002946.2. DR EnsemblBacteria; AAW89253; AAW89253; NGO_0515. DR GeneID; 3282933; -. DR KEGG; ngo:NGO0515; -. DR PATRIC; 20334072; VBINeiGon24812_0608. DR BioCyc; NGON242231:GI2G-493-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 77 AA; 8838 MW; A7B753DDADCE9161 CRC64; MRSLSAGGSI RFHTRPYFKA FKISAGFQIN AVKGAAHKTA RKNRRTDRYF SNKSNILRNS LKILVYSAYS YSFLNKD // ID Q5F6S0_NEIG1 Unreviewed; 86 AA. AC Q5F6S0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90117.2}; GN ORFNames=NGO_1478 {ECO:0000313|EMBL:AAW90117.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90117.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90117.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90117; AAW90117; NGO_1478. DR PATRIC; 20336399; VBINeiGon24812_1747. DR HOGENOM; HOG000071354; -. DR OMA; MLYKVMP; -. DR OrthoDB; EOG628FFB; -. DR BioCyc; NGON242231:GI2G-1383-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 9494 MW; 7AB23ACCA1D51E90 CRC64; MLYKVMPLNL NDILNYLAAT YTTGFLSVDL KTVSQQAYSD MADKINIGAD SASDSEMMKK AEKITTPSQS QSRGLLQRLM KKLLGS // ID Q5F702_NEIG1 Unreviewed; 180 AA. AC Q5F702; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Suppressor of fused family protein {ECO:0000313|EMBL:AAW90035.1}; GN ORFNames=NGO_1387 {ECO:0000313|EMBL:AAW90035.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90035.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90035.1; -; Genomic_DNA. DR RefSeq; WP_003705815.1; NC_002946.2. DR RefSeq; YP_208447.1; NC_002946.2. DR EnsemblBacteria; AAW90035; AAW90035; NGO_1387. DR GeneID; 3281204; -. DR KEGG; ngo:NGO1387; -. DR PATRIC; 20336167; VBINeiGon24812_1632. DR HOGENOM; HOG000220705; -. DR OMA; IVDSTKM; -. DR OrthoDB; EOG6MSS2S; -. DR BioCyc; NGON242231:GI2G-1300-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR020941; SUFU-like_domain. DR Pfam; PF05076; SUFU; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 25 176 SUFU. {ECO:0000259|Pfam:PF05076}. SQ SEQUENCE 180 AA; 20975 MW; A574A9626EBC5220 CRC64; MINHIEKYIG TISHGSKSDS GSQYKLNIAA IPSSPNRDLK TYITLGLSKH DLNYKSRFEI LFVCSLKYDE NQIFPFLRWL AETIIENKKI LLRGQVVYLP RSIVNSTKMD ALYVSAPFYF DDDFQVCYGE HYNIVFPLLV PLYKQEAELV EKKGWNAFEQ FLLDNEVGNL SDMNRKPFTW // ID Q5F7M7_NEIG1 Unreviewed; 72 AA. AC Q5F7M7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89810.1}; GN ORFNames=NGO_1143 {ECO:0000313|EMBL:AAW89810.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89810.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89810.1; -; Genomic_DNA. DR RefSeq; WP_003691584.1; NC_002946.2. DR RefSeq; YP_208222.1; NC_002946.2. DR EnsemblBacteria; AAW89810; AAW89810; NGO_1143. DR GeneID; 3282215; -. DR KEGG; ngo:NGO1143; -. DR PATRIC; 20335546; VBINeiGon24812_1338. DR HOGENOM; HOG000218812; -. DR OrthoDB; EOG6X112N; -. DR BioCyc; NGON242231:GI2G-1056-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 72 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256220. FT TRANSMEM 50 67 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 72 AA; 7539 MW; F6E4AF655CDA4217 CRC64; MKFINTCRKY GAKLAVVTAA PLALAAQANA ALPETAKNAL EAAKADGMEA GWIVVGVFAA LFVFSIVKRV MK // ID Q5F7D0_NEIG1 Unreviewed; 140 AA. AC Q5F7D0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89907.1}; GN ORFNames=NGO_1248 {ECO:0000313|EMBL:AAW89907.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89907.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89907.1; -; Genomic_DNA. DR RefSeq; WP_003689711.1; NC_002946.2. DR RefSeq; YP_208319.1; NC_002946.2. DR EnsemblBacteria; AAW89907; AAW89907; NGO_1248. DR GeneID; 3281833; -. DR KEGG; ngo:NGO1248; -. DR PATRIC; 20335825; VBINeiGon24812_1467. DR HOGENOM; HOG000219035; -. DR OMA; IRARQVK; -. DR OrthoDB; EOG6JTCBX; -. DR BioCyc; NGON242231:GI2G-1165-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 135 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 140 AA; 15592 MW; 3FEB4FD9C1E37A33 CRC64; MSAVFIAPYL TAFHEQEKIF EYADLTVTAP NRSGRAIKLE ADGRQYRLSC YGFDSLCTGG NIGRAIRARQ VKIVLSETVG KGFLNGVLLE YRNSGSVYSN KDFSRTEDRL VEVLAQPAVF SLKPGILLLL PAIFLRLKKM // ID Q5F8V4_NEIG1 Unreviewed; 513 AA. AC Q5F8V4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=MFS transporter {ECO:0000313|EMBL:AAW89383.1}; GN ORFNames=NGO_0656 {ECO:0000313|EMBL:AAW89383.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89383.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89383.1; -; Genomic_DNA. DR RefSeq; WP_003688844.1; NC_002946.2. DR RefSeq; YP_207795.1; NC_002946.2. DR ProteinModelPortal; Q5F8V4; -. DR EnsemblBacteria; AAW89383; AAW89383; NGO_0656. DR GeneID; 3282508; -. DR KEGG; ngo:NGO0656; -. DR PATRIC; 20334404; VBINeiGon24812_0774. DR HOGENOM; HOG000058265; -. DR OMA; QDTAWIS; -. DR OrthoDB; EOG64XXNP; -. DR BioCyc; NGON242231:GI2G-623-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 118 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 180 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; 54424 MW; 7EDCCACAE7A44ACA CRC64; MKFLDREASI AKPGFNRWLV PPAALAVHLA IGQIYAYSVF NAPLTKLIGI TESAAGDWKL TTVGWIFSIA LAMLGASAAL FGTWMERVGP RKAIFAAACC FSLGFFVSAF GVRTHNLFLL YLGNGVIGGV GLGLGYIGPV STLMKWFPDK PGMATGLAIM GFGGGAMLAS PLSVSLMNAF SNAASVGVAE TFAVLGLFYL ALMMFGAFTI RVPADGWKPE GYTVPKTQNK PVSSNHVNVS QAMKTPQFWL LFWVLCLNVT AGIGVLGQAS VMIQELFSET SAGRQAAVGA GAAAGFVSLL SLFNMGGRFL WSSVSDKIGR KNTYTIFFVL GSLLYFAVPS IGEGGSKALF IIGFCVIISM YGGGFAAIPA YLKDLFGTYQ VGAIHGRILL AWSTAAVIGP VLVNYIRQSQ IDSGIPAAQA YSVTMYIMAG LLIVGLLCNL AVKSVHEKHH EKDIKTAARS GNPDDETAIS DAYLVGEKVS GDGISVWWRW ALAVIPLAYG VVMVFVKALD LFS // ID Q5F7Z9_NEIG1 Unreviewed; 288 AA. AC Q5F7Z9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89688.1}; GN ORFNames=NGO_1005 {ECO:0000313|EMBL:AAW89688.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89688.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89688.1; -; Genomic_DNA. DR RefSeq; WP_003688251.1; NC_002946.2. DR RefSeq; YP_208100.1; NC_002946.2. DR EnsemblBacteria; AAW89688; AAW89688; NGO_1005. DR GeneID; 3282123; -. DR KEGG; ngo:NGO1005; -. DR PATRIC; 20335212; VBINeiGon24812_1174. DR OrthoDB; EOG63588F; -. DR BioCyc; NGON242231:GI2G-931-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010144; CRISPR-assoc_prot_Csd1-typ. DR Pfam; PF09709; Cas_Csd1; 1. DR TIGRFAMs; TIGR01863; cas_Csd1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 288 AA; 31844 MW; 6C0012807890B17F CRC64; MILASLVRYY RRLATETDET GNPKVPSYGF SEEKIGWILV LDKEGRLKTV VPNLTADKKP QPKLMSVPRP EKRTSGIKPN FLWDKTAYAL GVEANKNKAE AKEKPFTPSE KTFEAFKQYH LDLLQNSEDE GLQALCRFLQ NWQPAHFAAE NLPAEMLDSN TAFSLEKPTA LIHKREAAQT LWAGCLKSDE ALESLCLISG DTAPIARLHP AIKGVFGGQS SGGSIISFNK EAFSSFGKEQ GANAPVSEQS AFAYTTALNY LLRRENNHCL TIGDASTVFW AEADDIVD // ID Q5F9U8_NEIG1 Unreviewed; 576 AA. AC Q5F9U8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 71. DE SubName: Full=Potassium transporter {ECO:0000313|EMBL:AAW89039.2}; GN ORFNames=NGO_0291 {ECO:0000313|EMBL:AAW89039.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89039.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89039.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9U8; -. DR EnsemblBacteria; AAW89039; AAW89039; NGO_0291. DR PATRIC; 20333561; VBINeiGon24812_0361. DR HOGENOM; HOG000019567; -. DR OMA; YFNVAFA; -. DR OrthoDB; EOG6RZB2N; -. DR BioCyc; NGON242231:GI2G-271-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR InterPro; IPR006153; Cation/H_exchanger. DR InterPro; IPR030151; NhaP. DR InterPro; IPR005170; Transptr-assoc_dom. DR PANTHER; PTHR32507:SF7; PTHR32507:SF7; 1. DR Pfam; PF00999; Na_H_Exchanger; 1. DR SMART; SM01091; CorC_HlyC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003721}. FT TRANSMEM 49 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 119 139 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 290 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 302 322 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 334 354 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 366 386 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 495 576 CorC_HlyC. {ECO:0000259|SMART:SM01091}. SQ SEQUENCE 576 AA; 61557 MW; 26D14BBB847AB456 CRC64; MDWMNSLFLL GGALLFLSVV STTLSARLGM PLLLVFLAVG MLAGEEGVGG IAFNNVVMAN FISQLALAVI LLDGGLRTQL SSFRIALKPA SVLASWGVFA TVLPLGLFAT FYLGLDWKFG VLMAAIVGST DAGAVFSLLR NSGVRLNERV QATLEIESGA NDPMAVFLVT ALITMIMQPA ESGAAAFVRM LALQIGFGLL TGWAGGKILA KLVRRLNLAE GLYALMIVSG GLLVFAFTNT IGGSGFLAVY LAGIIVGNQR NRATEHVLRV MDGLAWLAQA TLFVMLGLLV SPAGVLDRAA EALAIAAFLM LVARPLAVFG GLWKFNYSLR EKAYISWLGL RGAVPISLAM MPLVMGVPNS HLLFDVAFAV VVLSLLIQGT TIPVMARLLK VAMPNKPEPK DTHDIWLAEK EIVRMSAFKV VAESEAEGHH PDTVEPISDS FDARCFALIR NGSRIEMQSD TVLQAEDLAW YILADGKVDK MAKYFTETGI GVRENFDFFG EFVVSPAARS GDLALAYGLK LEAGEEGLSL AELFDKRSDS QEPVEGDRID IGGFMLTAKE VDGGGNIGSM GLKVPR // ID Q5F877_NEIG1 Unreviewed; 95 AA. AC Q5F877; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89610.1}; GN ORFNames=NGO_0914 {ECO:0000313|EMBL:AAW89610.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89610.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89610.1; -; Genomic_DNA. DR RefSeq; WP_003688407.1; NC_002946.2. DR RefSeq; YP_208022.1; NC_002946.2. DR EnsemblBacteria; AAW89610; AAW89610; NGO_0914. DR GeneID; 3281759; -. DR KEGG; ngo:NGO0914; -. DR PATRIC; 20335011; VBINeiGon24812_1075. DR HOGENOM; HOG000218901; -. DR OrthoDB; EOG6C0198; -. DR BioCyc; NGON242231:GI2G-852-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 10973 MW; 162B4D4B7DED2F05 CRC64; MNKEIVGIFF IPMGIISMCM AALWQMYVMM TETYTLNRFK DKELVWRVAL LFISFSLAVY LLCPNSRKKG IVFFILGGGG AVMYLLARMW LPFSK // ID Q5F6P3_NEIG1 Unreviewed; 269 AA. AC Q5F6P3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 61. DE SubName: Full=NTP pyrophosphohydrolase {ECO:0000313|EMBL:AAW90144.1}; GN ORFNames=NGO_1506 {ECO:0000313|EMBL:AAW90144.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90144.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90144.1; -; Genomic_DNA. DR RefSeq; WP_003689389.1; NC_002946.2. DR RefSeq; YP_208556.1; NC_002946.2. DR ProteinModelPortal; Q5F6P3; -. DR EnsemblBacteria; AAW90144; AAW90144; NGO_1506. DR GeneID; 3281562; -. DR KEGG; ngo:NGO1506; -. DR PATRIC; 20336486; VBINeiGon24812_1791. DR HOGENOM; HOG000137832; -. DR KO; K03574; -. DR OMA; REGQAWS; -. DR OrthoDB; EOG6W19NW; -. DR BioCyc; NGON242231:GI2G-1410-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW90144.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 137 Nudix hydrolase. FT {ECO:0000259|PROSITE:PS51462}. SQ SEQUENCE 269 AA; 29633 MW; 564542F47A14274E CRC64; MIQDTRPLIR VVAGILLDSD GNYLLGSRPE GKPYAGYWEF AGGKVEAGET DFQALQREFG EELGIRILAA TPWLTKIHSY EHARVCLKFL WVNPDQWEGG PQSREGQEWS WQKAGDFTVA PMLPANGALL RSLSVPRRLY GSLKTGLYGE NSMGAYRVLP LGSAGGSGAN VLMEAAQWQD RSEHAGSVWM MVQTREQWRQ AQEKGADVVV WRVCDDVQAQ EAAEALRQGV SVPLVLAANG QTVARYGKLW LGLGAHAVVR DETIGKNHE // ID Q5F7T4_NEIG1 Unreviewed; 66 AA. AC Q5F7T4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89753.1}; GN ORFNames=NGO_1086 {ECO:0000313|EMBL:AAW89753.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89753.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89753.1; -; Genomic_DNA. DR RefSeq; WP_010951175.1; NC_002946.2. DR RefSeq; YP_208165.1; NC_002946.2. DR EnsemblBacteria; AAW89753; AAW89753; NGO_1086. DR GeneID; 3281767; -. DR KEGG; ngo:NGO1086; -. DR PATRIC; 20335422; VBINeiGon24812_1277. DR HOGENOM; HOG000218908; -. DR OMA; CEKQIAY; -. DR OrthoDB; EOG6ZWJNH; -. DR BioCyc; NGON242231:GI2G-998-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 7888 MW; 158B2373BCD4D8A1 CRC64; MSAEEFCRKQ IAYWLNESRK ASDNADLKAF EFAGREPADY REMLKRYARV KNAVRRFGRH FPFTLP // ID Q5F9K8_NEIG1 Unreviewed; 333 AA. AC Q5F9K8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 76. DE RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515}; DE EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515}; GN ORFNames=NGO_0385 {ECO:0000313|EMBL:AAW89129.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89129.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89129.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9K8; -. DR EnsemblBacteria; AAW89129; AAW89129; NGO_0385. DR PATRIC; 20333777; VBINeiGon24812_0466. DR HOGENOM; HOG000020323; -. DR OMA; MDPANSN; -. DR OrthoDB; EOG6VXFCB; -. DR BioCyc; NGON242231:GI2G-364-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Lyase {ECO:0000256|RuleBase:RU000515, ECO:0000313|EMBL:AAW89129.2}; 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:UP000000535}. 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; 36778 MW; EA1035D3A473D376 CRC64; MQFPYRNVPA SRMRRMRRDD FSRRLMREHM LTADDLIYPV FVLEGAAREE DVPSMPGVKR QSLDRLLFTA EEAVKLGIPM LALFPVVTAN KTGRAQEAYN PEGLVPSTVR ALRERFSELG IMTDVALDPY TVHGQDGLTD ENGYVMNDET VEVLVKQALC HAEAGTQVVA PSDMMDGRIG AIREALEDAG HIHTRIMAYS AKYASAFYGP FRDAVGSSGN LGKADKKTYQ MDPANTDEAL HEVALDIQEG ADMVMVKPGL PYLDVVRRVK DEFGVPTYAY QVSGEYAMLQ AAVANGWLDG GKVVLESLLA FKRAGADGIL TYYAIEAAKM LKR // ID Q5F5J5_NEIG1 Unreviewed; 42 AA. AC Q5F5J5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90542.1}; GN ORFNames=NGO_1929 {ECO:0000313|EMBL:AAW90542.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90542.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90542.1; -; Genomic_DNA. DR RefSeq; WP_003699129.1; NC_002946.2. DR RefSeq; YP_208954.1; NC_002946.2. DR EnsemblBacteria; AAW90542; AAW90542; NGO_1929. DR GeneID; 3282690; -. DR KEGG; ngo:NGO1929; -. DR PATRIC; 20337596; VBINeiGon24812_2325. DR HOGENOM; HOG000071363; -. DR OrthoDB; EOG6C8N6S; -. DR BioCyc; NGON242231:GI2G-1832-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 42 AA; 4591 MW; FA22D91A0BBD4BCB CRC64; MGRCRLSCSD GIFYVWKFPV RYSGLTKTGT ALPRPGSKGT VP // ID Q5F8W7_NEIG1 Unreviewed; 174 AA. AC Q5F8W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89370.2}; GN ORFNames=NGO_0643 {ECO:0000313|EMBL:AAW89370.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89370.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89370.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89370; AAW89370; NGO_0643. DR PATRIC; 20334370; VBINeiGon24812_0757. DR HOGENOM; HOG000284716; -. DR OMA; DTFHIRY; -. DR OrthoDB; EOG6NKR19; -. DR BioCyc; NGON242231:GI2G-610-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 174 AA; 19950 MW; 5082A7A7478D0CFD CRC64; MNNLIPEHLA AYAHSDNLQI EGGHRCFSLS CQGRDTFHIR YYGEPFDGLI TDTDKAPVKI VAVEAVSGDE IVLFDGAEHG YNAMFCDKYS QNQKQNRTLT DLDEYTYRVP IHLYYNIDYE DEYEDFVNSE GQVPLIDGRI ISFDSLKRNG FDAISIDLID EKHSVRELLN EELS // ID Q5F9Z8_NEIG1 Unreviewed; 428 AA. AC Q5F9Z8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 63. DE RecName: Full=Cell division protein ZipA {ECO:0000256|RuleBase:RU003612}; GN ORFNames=NGO_0236 {ECO:0000313|EMBL:AAW88989.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88989.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88989.1; -; Genomic_DNA. DR RefSeq; WP_003687577.1; NC_002946.2. DR RefSeq; YP_207401.1; NC_002946.2. DR ProteinModelPortal; Q5F9Z8; -. DR EnsemblBacteria; AAW88989; AAW88989; NGO_0236. DR GeneID; 3281509; -. DR KEGG; ngo:NGO0236; -. DR PATRIC; 20333421; VBINeiGon24812_0292. DR HOGENOM; HOG000218832; -. DR OMA; MIAMIYI; -. DR OrthoDB; EOG63JR6H; -. DR BioCyc; NGON242231:GI2G-220-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU003613}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 47003 MW; 944061B50C8BBAF8 CRC64; MIYIVLFLAA VLAVVAYNMY QENQYRKKVR DQFGHSDKDA LLNSKTSHVR DGKPSGGPVM MPKPQPAVKK PAKPQDSAMR NLQEQDAVYI AKQKQAKASP FKTEIETALE EIGIIGNSAH TVSEPQTGHS APKPADAPAK PVPVPQTPAK PLITLKELSK VELPWFDVRF DFISYIALTE AKELHALPRL SNRCRYQIVG CTMDDHFQIA EPIPGIRYQA FIVGIQAVSR NGLASQEELS AFNRQADAFA QSMGGQTLHT DLAAFIEVAS ALDAFCARVD QTIAIHLVSP TSISGVELRS AVTGVGFVLE DDGAFHYTDT SGSTMFSICS LNNEPFTNAL LDNQSYKGFS MLLDIPHSPA GEKTFDDLFM DLAVRLSGQL NLNLVNDKME EVSTQWLKDV RTYVLARQSE MLKVGIEPGG KTALRLFS // ID Q5F540_NEIG1 Unreviewed; 528 AA. AC Q5F540; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 71. DE RecName: Full=Transporter {ECO:0000256|RuleBase:RU003732}; GN ORFNames=NGO_2096 {ECO:0000313|EMBL:AAW90697.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90697.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90697.1; -; Genomic_DNA. DR RefSeq; WP_003687063.1; NC_002946.2. DR RefSeq; YP_209109.1; NC_002946.2. DR ProteinModelPortal; Q5F540; -. DR EnsemblBacteria; AAW90697; AAW90697; NGO_2096. DR GeneID; 3282821; -. DR KEGG; ngo:NGO2096; -. DR PATRIC; 20338029; VBINeiGon24812_2537. DR HOGENOM; HOG000033130; -. DR KO; K03308; -. DR OMA; KREWQIF; -. DR OrthoDB; EOG6WT8F5; -. DR BioCyc; NGON242231:GI2G-1991-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 34 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 131 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 242 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 279 304 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 366 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 378 402 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 408 427 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 467 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 487 508 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 528 AA; 56773 MW; 52D1640F9FAFE2A5 CRC64; MFAYNGLFLI NNSRGINVSD SKTKERATFG TRRAFMIAAI GSAVGLGNIW RFPYIAFENG GGAFILPYLV ALLTAGIPLL LLDYAIGHRY RGSAPLAFRR LGRWFEPVGW WNVMTNIVIC IYYAVIIGWA ASYTYYSVNA AWGADPQGFF FKDFLQMAGP EALGLDFVGK VAGPLAGVWV FTAAIMALGV QKGVARASSF FMPLLLVMFL IMVGISLTLP GAAKGLDALF TPDWSKLADS KVWVAAYGQI FFSLSICFGI MVTYSSYLKK KTDLGGTGLV VGFANSSFEL LAGIGVFAAL GFMAQAGGKA VNEVASGGIG LAFIAFPTII NQAPMGWLIG ILFFGSLVFA GVTSMISILE VIVAAIQDKL NIGRVNATLL VCIPMGIVST LLFGTATGLP VLDVMDKFVN TYGIVAAGFV YVAAIIIGGR LPELRRHLNA LSSIRVGGLW TACVVFTVVM LGYMLYQDTA GLLEKNYGDY PDGFLNIFGW GMSAALIMFG LLLSLLPWKH GQDFNVKDEH EHEQGGEK // ID Q5F6B5_NEIG1 Unreviewed; 96 AA. AC Q5F6B5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89923.1}; GN ORFNames=NGO_1264 {ECO:0000313|EMBL:AAW89923.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89923.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89923.1; -; Genomic_DNA. DR RefSeq; WP_003689734.1; NC_002946.2. DR RefSeq; YP_208335.1; NC_002946.2. DR RefSeq; YP_208684.1; NC_002946.2. DR EnsemblBacteria; AAW89923; AAW89923; NGO_1264. DR GeneID; 3281340; -. DR GeneID; 3281885; -. DR KEGG; ngo:NGO1264; -. DR KEGG; ngo:NGO1645; -. DR PATRIC; 20335863; VBINeiGon24812_1486. DR HOGENOM; HOG000218808; -. DR OrthoDB; EOG6VHZGB; -. DR BioCyc; NGON242231:GI2G-1181-MONOMER; -. DR BioCyc; NGON242231:GI2G-1541-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 10305 MW; 5895E577DC85E41C CRC64; MPLLSGLIPL LGILLKMLIV RIILATGLTF VTYAGYLAAL EKFKGYTANA INSMPSDILN LLLISGFGQG LGCLFGAFSF FIGMHAFKKL TFVFPG // ID Q5F8F7_NEIG1 Unreviewed; 261 AA. AC Q5F8F7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 57. DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:AAW89530.1}; GN ORFNames=NGO_0819 {ECO:0000313|EMBL:AAW89530.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89530.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89530.1; -; Genomic_DNA. DR RefSeq; WP_003697046.1; NC_002946.2. DR RefSeq; YP_207942.1; NC_002946.2. DR ProteinModelPortal; Q5F8F7; -. DR EnsemblBacteria; AAW89530; AAW89530; NGO_0819. DR GeneID; 3281974; -. DR KEGG; ngo:NGO0819; -. DR PATRIC; 20334792; VBINeiGon24812_0966. DR HOGENOM; HOG000218799; -. DR KO; K03437; -. DR OMA; WLARYKG; -. DR OrthoDB; EOG6GBMDM; -. DR BioCyc; NGON242231:GI2G-772-MONOMER; -. DR Proteomes; UP000000535; 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; 3.30.1330.30; -; 1. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Methyltransferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAW89530.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00477853, KW ECO:0000313|EMBL:AAW89530.1}. FT DOMAIN 115 252 SpoU_methylase. FT {ECO:0000259|Pfam:PF00588}. SQ SEQUENCE 261 AA; 28310 MW; FE4A084E713C8479 CRC64; MKHISSTNNE HIRHLHRLLS QGKFRRQYAQ TVLEGVHLLQ VFLQSGRKPV GVYIPEAKMP SEEVLKLTAV LPEDGIFSVS DGILKKISSL SCADDILTLI DIPLGGTLPD KGDCAVLDGV QDPGNVGTVL RSAAAAGVGT VVLGRGCADA WSPKVLRAGM GAHFLLDIYS QADLEIWLAH YEDRVFATAL REEKQAVLYG EDLCEPTAWV FGNEGAGVGK AVLDRADKCV RIPMHDATES LNVAMAATIC LFEQMRQRAA Y // ID Q5F8S3_NEIG1 Unreviewed; 258 AA. AC Q5F8S3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:AAW89414.1}; GN ORFNames=NGO_0687 {ECO:0000313|EMBL:AAW89414.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89414.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89414.1; -; Genomic_DNA. DR RefSeq; WP_003702769.1; NC_002946.2. DR RefSeq; YP_207826.1; NC_002946.2. DR ProteinModelPortal; Q5F8S3; -. DR SMR; Q5F8S3; 4-258. DR EnsemblBacteria; AAW89414; AAW89414; NGO_0687. DR GeneID; 3281921; -. DR KEGG; ngo:NGO0687; -. DR PATRIC; 20334470; VBINeiGon24812_0807. DR HOGENOM; HOG000265759; -. DR KO; K00528; -. DR OMA; DELAYHD; -. DR OrthoDB; EOG6FZ49Q; -. DR BioCyc; NGON242231:GI2G-654-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 102 FAD-binding FR-type. FT {ECO:0000259|PROSITE:PS51384}. SQ SEQUENCE 258 AA; 29331 MW; CA4E2C4302173E8B CRC64; MAAFNTQKVL SVHHWTDAYF TFTCIRDESL RFENGQFVMV GLMADGKPLM RAYSVASANW EEHLEFFSIK VQDGPLTSRL QHLKVGDEVL ISKKPTGTLV AGDLNPGKHL YLLSTGTGIA PFLSITKDPE IYEQFEKIIL VHGVRYKKDL AYYDRFTKEL PEHEYLGDLV KEKLIYYPIV SREEFEHRGR LTDLMVSGKL FEDIGLPKIN PQDDRAMLCG SPAMLKDTCK VLDDFGLTVS PKTGVRGDYL IERAFVDQ // ID Q5F550_NEIG1 Unreviewed; 435 AA. AC Q5F550; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Surface exposed protein {ECO:0000313|EMBL:AAW90687.1}; GN ORFNames=NGO_2086 {ECO:0000313|EMBL:AAW90687.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90687.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90687.1; -; Genomic_DNA. DR RefSeq; WP_010951402.1; NC_002946.2. DR RefSeq; YP_209099.1; NC_002946.2. DR ProteinModelPortal; Q5F550; -. DR EnsemblBacteria; AAW90687; AAW90687; NGO_2086. DR GeneID; 3282831; -. DR KEGG; ngo:NGO2086; -. DR PATRIC; 20338005; VBINeiGon24812_2525. DR HOGENOM; HOG000071374; -. DR OMA; ARANGNH; -. DR OrthoDB; EOG6VTJX8; -. DR BioCyc; NGON242231:GI2G-1981-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR Gene3D; 2.150.10.10; -; 2. DR InterPro; IPR008640; Adhesin_Head_dom. DR InterPro; IPR008635; Coiled_stalk_dom. DR InterPro; IPR011049; Serralysin-like_metalloprot_C. DR InterPro; IPR005594; YadA_C. DR Pfam; PF03895; YadA_anchor; 1. DR Pfam; PF05658; YadA_head; 4. DR Pfam; PF05662; YadA_stalk; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 282 302 YadA_stalk. {ECO:0000259|Pfam:PF05662}. FT DOMAIN 316 394 YadA_anchor. {ECO:0000259|Pfam:PF03895}. SQ SEQUENCE 435 AA; 45267 MW; 3F14045EB4CB8670 CRC64; MCYLHISRVT YLLIWYSPKK YAVALGSSST ASGEYSYASG YNSVASGNKS YAAGYASVAS AEGSVVIGDS RQVKPEADQG VAVGSKATVK NKAKQRVVVG SEAKVNAERG IAIGKEAKAG GKTTNTLLDG PAYYADAIAV GYQAEAGKGG AIALGKQAKA TKQNGMALGV ESEAAGDFST AVGNESKAKG QGGVGLGNQS KAEADFAVAV GNKAEATKEN SLVIGRYARA NGNHSVSLGS RSEIKDGVSN SVAPGYGSVA SENNVVSVAY KETPQSTELS YRKIVGVDDG VNDFDAVNVR QLKAMQGQNM AELFSVRSEV RGVAASSAAL SALTPLSYDA NNPTQFMVGF GTYKGRQAMA LGLSHFVNDR FMVKVGGTLG GNKTGHMMNV GLTWKFGTSQ GVPATSDKVL MEQLMQDNRQ LKPRLEKLEA RLNAM // ID Q5F697_NEIG1 Unreviewed; 332 AA. AC Q5F697; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Branched-chain amino acid aminotransferase {ECO:0000313|EMBL:AAW90290.1}; GN ORFNames=NGO_1665 {ECO:0000313|EMBL:AAW90290.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90290.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90290.1; -; Genomic_DNA. DR RefSeq; WP_003689799.1; NC_002946.2. DR RefSeq; YP_208702.1; NC_002946.2. DR ProteinModelPortal; Q5F697; -. DR EnsemblBacteria; AAW90290; AAW90290; NGO_1665. DR GeneID; 3281289; -. DR KEGG; ngo:NGO1665; -. DR PATRIC; 20336880; VBINeiGon24812_1985. DR HOGENOM; HOG000276704; -. DR KO; K00826; -. DR OMA; YSRAANG; -. DR OrthoDB; EOG67MF3R; -. DR BioCyc; NGON242231:GI2G-1559-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90290.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90290.1}. FT MOD_RES 179 179 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR006468-1}. SQ SEQUENCE 332 AA; 36129 MW; 9A79B276E9DD4E91 CRC64; MSRPVPAVFG SVFHSQMPVL AYREGKWQPT EWQSSQDLTL APGAHALHYG SECFEGLKAF RQADGKIVLF RPTANIARMR QSADILHLPR PETQAYLDAL VELVKRAADE IPDAPAALYL RPTLIGTDPV IGKAGSPSET ALLYILASPV GDYFKVGSPV KILVETEHIR CAPHMGRVKC GGNYASAMHW LLKAKAEYGA NQVLFCPNGD VQETGASNFI LINGDEIITK PLTDEFLHGV TRDSVLTVAK DLGYTVSERN FTVDELKAAV ENGAEAILTG TAAVISPVTS FVIGGKEIEV KNQERGYAIR KAITDIQYGL AEDKYGWLVE VC // ID Q5F9G0_NEIG1 Unreviewed; 263 AA. AC Q5F9G0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:AAW89177.1}; DE EC=2.5.1.16 {ECO:0000313|EMBL:AAW89177.1}; GN ORFNames=NGO_0435 {ECO:0000313|EMBL:AAW89177.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89177.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89177.1; -; Genomic_DNA. DR RefSeq; WP_003687893.1; NC_002946.2. DR RefSeq; YP_207589.1; NC_002946.2. DR ProteinModelPortal; Q5F9G0; -. DR EnsemblBacteria; AAW89177; AAW89177; NGO_0435. DR GeneID; 3282074; -. DR KEGG; ngo:NGO0435; -. DR PATRIC; 20333885; VBINeiGon24812_0520. DR HOGENOM; HOG000263005; -. DR KO; K00797; -. DR OMA; YHRHYWE; -. DR OrthoDB; EOG6ZPT03; -. DR BioCyc; NGON242231:GI2G-412-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51006; PABS_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89177.1}. FT DOMAIN 1 221 PABS (polyamine biosynthesis). FT {ECO:0000259|PROSITE:PS51006}. SQ SEQUENCE 263 AA; 29782 MW; 17ED724B11774181 CRC64; MARHPYRRLR PAKSGFPEVG ISEEGNIRSL HLGSDTVQSS MNLDRPSELV LSYSRAMMGW LLFAERLPQH ITQIGLGGGS FARWTDTYLP DTRQTAVDIN PQVIAIARNL FELPFEGGKF EIIEADGAEY IKVFRHNTDI ILVDGFDGEQ IIDTLVEEPF FRDCRNALSS DGIFVTNWWS GDKRYQRFIE RLLSVFEGRV LELPAESHGN VAVMAFQSSP KEQNIDKLKK RADKLSNAYG LDFHRMLAGL KASNPNNGKH FHL // ID Q5F6I5_NEIG1 Unreviewed; 558 AA. AC Q5F6I5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 89. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90202.1}; GN ORFNames=NGO_1573 {ECO:0000313|EMBL:AAW90202.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90202.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90202.1; -; Genomic_DNA. DR RefSeq; WP_010951297.1; NC_002946.2. DR RefSeq; YP_208614.1; NC_002946.2. DR ProteinModelPortal; Q5F6I5; -. DR EnsemblBacteria; AAW90202; AAW90202; NGO_1573. DR GeneID; 3281424; -. DR KEGG; ngo:NGO1573; -. DR PATRIC; 20336672; VBINeiGon24812_1882. DR HOGENOM; HOG000271639; -. DR KO; K06020; -. DR OMA; LEIAMDA; -. DR OrthoDB; EOG6F297F; -. DR BioCyc; NGON242231:GI2G-1470-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90202.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90202.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 62035 MW; F3DC5766DD9D6C97 CRC64; MSQQYVYSML RVSKVVPPQK TIIKDISLSF FPGAKIGLLG LNGTGKSTVL RIMAGVDKEF EGEAVPMGGI KIGYLPQEPE LDPEKTVREE VESGLGEVAA AQKRLEEVYA EYANPDADFD ALAEEQGRLE AIIAAGSSTG GGAEHELEIA ADALRLPDWD AKIGNLSGGE KRRVALCKLL LSKPDMLLLD EPTNHLDAES VEWLEQFLVR FPGTVVAVTH DRYFLDNAAE WILELDRGHG IPWKGNYSSW LEQKEKRLEN EAKSEAARVK AMKQELEWVR QNAKGRQAKP KARLARFEEM SNYEYQKRNE TQEIFIPVAE RLGNEVIEFV NVSKSFGDKV LIDGLSFKVP AGAIVGIIGP NGAGKSTLFK MIAGKEQPDS GEVKIGQTVK MSLIDQSREG LQNDKTVFDN IAEGRDILQV GQFEIPARQY LGRFNFKGSD QSKIARQLSG GERGRLHLAK TLLGGGNVLL LDEPSNDLDV ETLRALEDAL LEFAGSVMVI SHDRWFLDRI ATHILACEGD SKWVFFDGNY QEYEADKKRR LGKEGAKPKR IKYKPVTR // ID Q5F6Q0_NEIG1 Unreviewed; 369 AA. AC Q5F6Q0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Addiction module protein {ECO:0000313|EMBL:AAW90137.1}; GN ORFNames=NGO_1499 {ECO:0000313|EMBL:AAW90137.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90137.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90137.1; -; Genomic_DNA. DR RefSeq; WP_003689382.1; NC_002946.2. DR RefSeq; YP_208549.1; NC_002946.2. DR ProteinModelPortal; Q5F6Q0; -. DR SMR; Q5F6Q0; 3-368. DR EnsemblBacteria; AAW90137; AAW90137; NGO_1499. DR GeneID; 3281593; -. DR KEGG; ngo:NGO1499; -. DR PATRIC; 20336470; VBINeiGon24812_1783. DR HOGENOM; HOG000295052; -. DR OMA; PYCRIGN; -. DR OrthoDB; EOG6SR92R; -. DR BioCyc; NGON242231:GI2G-1403-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 111 261 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 369 AA; 41572 MW; 124AD17D60F92F04 CRC64; MSNWKPDIPY NDLPPLPPKQ DIESKTILKR CIAARASLAR LKQAAELIPN QAMLINTLPV MEARASSEIE NIVTTTDKLF QSLQMDTERQ DPATKEALQY RTALFAGYES LASRPLCTQT AIMVCNAIKH PYETAIRKTG GTALKGGNSG NVVYTPPEGE ETIRGKLANW ERFIHESGDL DPLVIMAAAH YQFEAIHPFT DGNGRTGRIL NSLLLIEKGL LDLPILYLSR YIIENRADYY RLLLGVTERQ DWESWIIYIL DGVADTADWT VSKIDAIRCL FEQTRQHIRT HAQGIYTHEL VNLLFEQPYT RIANLEAAGI AKRQTASKYL KELSGIGVLQ EIAIGRDKLF IHPRLMELLR GEGNSFTSF // ID Q5F5C3_NEIG1 Unreviewed; 64 AA. AC Q5F5C3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Thiamine biosynthesis protein ThiS {ECO:0000313|EMBL:AAW90614.1}; GN ORFNames=NGO_2006 {ECO:0000313|EMBL:AAW90614.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90614.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90614.1; -; Genomic_DNA. DR RefSeq; WP_003692010.1; NC_002946.2. DR RefSeq; YP_209026.1; NC_002946.2. DR ProteinModelPortal; Q5F5C3; -. DR EnsemblBacteria; AAW90614; AAW90614; NGO_2006. DR GeneID; 3282618; -. DR KEGG; ngo:NGO2006; -. DR PATRIC; 20337789; VBINeiGon24812_2418. DR HOGENOM; HOG000248060; -. DR KO; K03154; -. DR OMA; NIEGAFA; -. DR OrthoDB; EOG6KMBD9; -. DR BioCyc; NGON242231:GI2G-1907-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 6710 MW; 20F5456CB6091C6C CRC64; MNIILNGGPA ELHGTSVADL IAQTAPQKPF AVAVNTVFIP KGAYTETVLH ENDKIDIVRP VVGG // ID Q5F8H6_NEIG1 Unreviewed; 105 AA. AC Q5F8H6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=XRE family transcriptional regulator {ECO:0000313|EMBL:AAW89511.1}; GN ORFNames=NGO_0797 {ECO:0000313|EMBL:AAW89511.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89511.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89511.1; -; Genomic_DNA. DR RefSeq; WP_010358148.1; NC_002946.2. DR RefSeq; YP_207923.1; NC_002946.2. DR ProteinModelPortal; Q5F8H6; -. DR EnsemblBacteria; AAW89511; AAW89511; NGO_0797. DR GeneID; 3282012; -. DR KEGG; ngo:NGO0797; -. DR PATRIC; 20334742; VBINeiGon24812_0943. DR HOGENOM; HOG000225390; -. DR OMA; ERLNLMT; -. DR OrthoDB; EOG615VS0; -. DR BioCyc; NGON242231:GI2G-751-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 25 79 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 105 AA; 11817 MW; 63B50E1594D27673 CRC64; MGNKLTLPAE LPDEQDLRAV LAYNMRLFRV NKGWSQEELA RQCGLDRTYV SAVERKRWNI ALSNIEKMAA ALGVAAYQLL LPPQERLNLM TNSADTRQVP SESGI // ID Q5F593_NEIG1 Unreviewed; 145 AA. AC Q5F593; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=PTS mannose transporter subunit IIA {ECO:0000313|EMBL:AAW90644.1}; GN ORFNames=NGO_2036 {ECO:0000313|EMBL:AAW90644.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90644.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90644.1; -; Genomic_DNA. DR RefSeq; WP_003694418.1; NC_002946.2. DR RefSeq; YP_209056.1; NC_002946.2. DR ProteinModelPortal; Q5F593; -. DR DNASU; 3282711; -. DR EnsemblBacteria; AAW90644; AAW90644; NGO_2036. DR GeneID; 3282711; -. DR KEGG; ngo:NGO2036; -. DR PATRIC; 20337855; VBINeiGon24812_2451. DR HOGENOM; HOG000095324; -. DR KO; K02821; -. DR OMA; ISHIYGG; -. DR OrthoDB; EOG6QRWFP; -. DR BioCyc; NGON242231:GI2G-1937-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 126 PTS EIIA type-4. FT {ECO:0000259|PROSITE:PS51096}. SQ SEQUENCE 145 AA; 15686 MW; 5C6A05EC4EF92418 CRC64; MIGLLIITHE TIGEAYRKLA HHFFPGGLPE NVRILGVQPT EDQDDIINNA ISALQEFPEN HGVLIMTDIF GATPCNAARR LVRENKSAIL TGLNAPMMIK AVQYSPAAED LAAFTECVRE AAVKGIFAIT SAPEDLVCRR SGDAV // ID Q5F7A7_NEIG1 Unreviewed; 134 AA. AC Q5F7A7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89930.1}; GN ORFNames=NGO_1273 {ECO:0000313|EMBL:AAW89930.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89930.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89930.1; -; Genomic_DNA. DR RefSeq; WP_003689175.1; NC_002946.2. DR RefSeq; YP_208342.1; NC_002946.2. DR ProteinModelPortal; Q5F7A7; -. DR EnsemblBacteria; AAW89930; AAW89930; NGO_1273. DR GeneID; 3282068; -. DR KEGG; ngo:NGO1273; -. DR PATRIC; 20335879; VBINeiGon24812_1494. DR HOGENOM; HOG000061066; -. DR OMA; FGNMVPH; -. DR OrthoDB; EOG6MM1NC; -. DR BioCyc; NGON242231:GI2G-1188-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 106 HIT. {ECO:0000259|PROSITE:PS51084}. SQ SEQUENCE 134 AA; 15125 MW; 789CEE7342B4C38A CRC64; MTAQPCPICT AQDEDILLQT PKLRVIAVHN DSGSPAFCRV IWHGHIAEIT DLSAAERGEL MEMVYKVEAA MRQVFRPAKI NLASLGNVVP HLHWHIIARF ENDATFPAPI WANPVRKHGM TLPQNWTEQL KKLL // ID Q5F892_NEIG1 Unreviewed; 43 AA. AC Q5F892; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89595.1}; GN ORFNames=NGO_0896 {ECO:0000313|EMBL:AAW89595.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89595.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89595.1; -; Genomic_DNA. DR RefSeq; WP_010951147.1; NC_002946.2. DR RefSeq; YP_208007.1; NC_002946.2. DR EnsemblBacteria; AAW89595; AAW89595; NGO_0896. DR GeneID; 3281127; -. DR KEGG; ngo:NGO0896; -. DR PATRIC; 20334965; VBINeiGon24812_1052. DR OrthoDB; EOG6WT8RM; -. DR BioCyc; NGON242231:GI2G-837-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 43 AA; 4599 MW; 38792313A012176B CRC64; MSETAKIKLN DRSENAEKPN EKVELPIVDN DKKGGHGEGG CCG // ID Q5F9H4_NEIG1 Unreviewed; 244 AA. AC Q5F9H4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89163.1}; GN ORFNames=NGO_0420 {ECO:0000313|EMBL:AAW89163.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89163.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89163.1; -; Genomic_DNA. DR RefSeq; WP_010951040.1; NC_002946.2. DR RefSeq; YP_207575.1; NC_002946.2. DR EnsemblBacteria; AAW89163; AAW89163; NGO_0420. DR GeneID; 3282996; -. DR KEGG; ngo:NGO0420; -. DR PATRIC; 20333853; VBINeiGon24812_0504. DR HOGENOM; HOG000218873; -. DR OMA; YPRYGKD; -. DR OrthoDB; EOG6RJV4P; -. DR BioCyc; NGON242231:GI2G-398-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007497; DUF541. DR Pfam; PF04402; SIMPL; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 244 AA; 27203 MW; A1CD2BC367C6F822 CRC64; MAVFQVRIRI CCVLFWRLPC WRYLFPAAAE ALNYNIVEFS ESAGIEVAQD TMSARFQVAA EGRDKNAVNA EFVKKFNNFT RKSKNGSFKT ELVSRSAMPR YQYTNGRRIQ TGWEERAEFK AEGRDFDALN RFIADVQTDA SLEDTDFSVS RERRNEVIDQ VSKDAVLRFK ARAEKLAGVL GASGYKIVKL NFGQIGSHIA GDGAVRAKML RAMPMAASVN MKGTDSAAPG VEEISISING TVQF // ID Q5F676_NEIG1 Unreviewed; 430 AA. AC Q5F676; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:AAW90311.1}; GN ORFNames=NGO_1686 {ECO:0000313|EMBL:AAW90311.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90311.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90311.1; -; Genomic_DNA. DR RefSeq; WP_003689841.1; NC_002946.2. DR RefSeq; YP_208723.1; NC_002946.2. DR ProteinModelPortal; Q5F676; -. DR MEROPS; M23.009; -. DR EnsemblBacteria; AAW90311; AAW90311; NGO_1686. DR GeneID; 3281229; -. DR KEGG; ngo:NGO1686; -. DR PATRIC; 20336930; VBINeiGon24812_2009. DR HOGENOM; HOG000281148; -. DR OMA; NARVSSH; -. DR OrthoDB; EOG61KBD1; -. DR BioCyc; NGON242231:GI2G-1581-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 294 387 Peptidase_M23. FT {ECO:0000259|Pfam:PF01551}. SQ SEQUENCE 430 AA; 46325 MW; 8115557CA9D25A89 CRC64; MAVFPLSAKH RKYALRALAV SIILVSAAYI ASTEGTERVR PQRVEQKLPP LSWGGSGVQT AYWVQEAVQP GDSLADVLAR SGMARDEIAR ITEKYGGEAD LRHLRADQSV HVLVGGDGSA REVQFFTDED GERNLVALEK KGGIWRRSAS DADMKVLPTL RSVVVKTSAR GSLARAEVPV EIRESLSGIF AGRFSLDGLK EGDAVRLLYD SLYFHGQQVA AGDILAAEVV KGGTTHQAFY YRSDKEGGGG GNYYDEDGRV LQEKGGFNIE PLVYTRISSP FGYRMHPILH TWRLHTGIDY AAPQGTPVRA SADGVITFKG RKGGYGNAVM IRHANGVETL YAHLSAFSQA QGNVRGGEVI GFVGSTGRST GPHLHYEARI NGQPVNPVSV ALPTPELTQA DKAAFAAQKQ KADALLARLR GIPVTVSQSD // ID Q5F7G3_NEIG1 Unreviewed; 157 AA. AC Q5F7G3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89874.1}; GN ORFNames=NGO_1215 {ECO:0000313|EMBL:AAW89874.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89874.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89874.1; -; Genomic_DNA. DR RefSeq; WP_010951218.1; NC_002946.2. DR RefSeq; YP_208286.1; NC_002946.2. DR ProteinModelPortal; Q5F7G3; -. DR EnsemblBacteria; AAW89874; AAW89874; NGO_1215. DR GeneID; 3281873; -. DR KEGG; ngo:NGO1215; -. DR PATRIC; 20335739; VBINeiGon24812_1428. DR HOGENOM; HOG000217164; -. DR KO; K09796; -. DR OMA; KMGGAFM; -. DR OrthoDB; EOG699768; -. DR BioCyc; NGON242231:GI2G-1126-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256219. FT DOMAIN 24 133 DUF461. {ECO:0000259|Pfam:PF04314}. SQ SEQUENCE 157 AA; 16974 MW; DD3E61EB80093467 CRC64; MKKLLAAVMM AGLAGAVSAA GVHVEDGWAR TTVEGMKMGG AFMKIPNDEA KQDFLLVGSS PVADRVEVHT HINDNGVMRM REVKGGVPLE AKSVTELKPG SYHVMFMGLK KQLKEGDKIP VTLKFKNAKA QTVQLEVKTA PMSAMNHGHH HGEAHQH // ID Q5FA20_NEIG1 Unreviewed; 500 AA. AC Q5FA20; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 56. DE SubName: Full=Phosphate acetyltransferase {ECO:0000313|EMBL:AAW88967.1}; GN ORFNames=NGO_0214 {ECO:0000313|EMBL:AAW88967.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88967.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88967.1; -; Genomic_DNA. DR RefSeq; WP_010357022.1; NC_002946.2. DR RefSeq; YP_207379.1; NC_002946.2. DR ProteinModelPortal; Q5FA20; -. DR EnsemblBacteria; AAW88967; AAW88967; NGO_0214. DR GeneID; 3281410; -. DR KEGG; ngo:NGO0214; -. DR PATRIC; 20333365; VBINeiGon24812_0265. DR HOGENOM; HOG000053796; -. DR KO; K13788; -. DR OMA; NHICRTP; -. DR OrthoDB; EOG6BKJ5W; -. DR BioCyc; NGON242231:GI2G-197-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00469150}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 500 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256639. FT DOMAIN 177 492 PTA_PTB. {ECO:0000259|Pfam:PF01515}. SQ SEQUENCE 500 AA; 52098 MW; B8DAA37972122B54 CRC64; MAKVLVVPVS AGLNTSAAAQ AFAKALDAQV FQAVDATAET LLAQGKSDDW FDALVGKVAA LDAANLVIEG IAPDADKIYL AGKNVELALS LDAAAVFAVR SDNTDADALA HQLNLAKQFF AAAPGVLEGF VVDGAAASVA EAAAEKTGLT FFGSSDALKD VSVLAGREAK RLSPAQFRYN LIDFARQAGK 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 AVQRSANVLS VGPLLQGLRK PVNDLSRGAL VEDIVFTIAL TAVQAKQMEG // ID Q5F559_NEIG1 Unreviewed; 461 AA. AC Q5F559; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Permease {ECO:0000313|EMBL:AAW90678.1}; GN ORFNames=NGO_2077 {ECO:0000313|EMBL:AAW90678.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90678.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90678.1; -; Genomic_DNA. DR RefSeq; WP_010951400.1; NC_002946.2. DR RefSeq; YP_209090.1; NC_002946.2. DR EnsemblBacteria; AAW90678; AAW90678; NGO_2077. DR GeneID; 3282840; -. DR KEGG; ngo:NGO2077; -. DR PATRIC; 20337985; VBINeiGon24812_2515. DR HOGENOM; HOG000237114; -. DR KO; K03299; -. DR OMA; PVILGCW; -. DR OrthoDB; EOG6B8XPC; -. DR BioCyc; NGON242231:GI2G-1972-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 111 136 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; 47377 MW; 0EBCFC978E81D09D CRC64; MDGRTQTLSA QTLLGISAAA IILILILIVK FRIRALLTLV IASLLTALAT GLPTGSIVND VLVKNFGGTL GGVALLVGLG AMLGRLVETS GGAQSLADAL IRMFGEKRAP FAPGVASLIF GFPIFFDAGL IVMLPIVFAT ARRMKQDVLP FALASVGAFS VMHVFLPPHP GPIAASEFYG ANIGQVLILG LPTAFITWYF SGYMLGKVLG RAIHVPVPEL LSGGTQDSDP PKEPAKAGTV VAVMLIPMLL IFLNTGVSAL ISEKLVSADE TWVQTAKMIG STPVALLISV LAALLVLGRK RGESGSTLEK TVDGALAPAC SVILITGAGG MFGGVLRASG IGKALADSMA DLGIPVLLGC FLVALALRIA QGSATVALTT AAALMAPAVA AAGFTDWQLA CIVLATAAGS VGCSHFNDSG FWLVGRLLDM DVPTTLKTWT VNQTLIAFIG FALSALLFAI V // ID Q5F7Z8_NEIG1 Unreviewed; 116 AA. AC Q5F7Z8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89689.1}; GN ORFNames=NGO_1006 {ECO:0000313|EMBL:AAW89689.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89689.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89689.1; -; Genomic_DNA. DR RefSeq; WP_003706358.1; NC_002946.2. DR RefSeq; YP_208101.1; NC_002946.2. DR EnsemblBacteria; AAW89689; AAW89689; NGO_1006. DR GeneID; 3281128; -. DR KEGG; ngo:NGO1006; -. DR PATRIC; 20335216; VBINeiGon24812_1176. DR OMA; AGCCTIL; -. DR OrthoDB; EOG65J5B1; -. DR BioCyc; NGON242231:GI2G-932-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 116 AA; 13344 MW; 10EED10E94833100 CRC64; MYGSRRLPCA QTDADGAQKK TAAYKGQDPA KVTHYLTRPA GFSDCQRVCP DETGFDRRLF RPYARSLKGQ MAKARIRVNR CRRRRYRKAR QTAIWAGCCT ILILITATRR IFSARK // ID Q5F530_NEIG1 Unreviewed; 111 AA. AC Q5F530; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90707.1}; GN ORFNames=NGO_2106 {ECO:0000313|EMBL:AAW90707.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90707.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90707.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90707; AAW90707; NGO_2106. DR BioCyc; NGON242231:GI2G-2001-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 111 AA; 12845 MW; 5A606009987DB4AD CRC64; MWLYVRFGVF CRFCSEMVQG RAGRKKRGFL STRRSNRWVA HKGIILNTKS YHTLLYPRSF SVGTPPFSAV KTDRRRNAGQ GFVPCGVGIS FYTSRQCHLK AEPSDFRRHL L // ID Q5F9G4_NEIG1 Unreviewed; 96 AA. AC Q5F9G4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89173.1}; GN ORFNames=NGO_0430 {ECO:0000313|EMBL:AAW89173.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89173.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89173.1; -; Genomic_DNA. DR RefSeq; WP_003690880.1; NC_002946.2. DR RefSeq; YP_207585.1; NC_002946.2. DR EnsemblBacteria; AAW89173; AAW89173; NGO_0430. DR GeneID; 3281991; -. DR KEGG; ngo:NGO0430; -. DR PATRIC; 20333877; VBINeiGon24812_0516. DR HOGENOM; HOG000218882; -. DR OMA; RDIKVPF; -. DR OrthoDB; EOG6JDWFH; -. DR BioCyc; NGON242231:GI2G-408-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 11034 MW; 0C44C4E21226236C CRC64; MDDLILYFLS GIFGNQVAEY IIKNNREIKV PFIALYAIFF TLIYTVALLF LSLIYWVNGA EIAWKGIGIF SMSVSFCIVF CLYLIDKAGR CKDKKQ // ID Q5F8H0_NEIG1 Unreviewed; 603 AA. AC Q5F8H0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 84. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:AAW89517.1}; GN ORFNames=NGO_0803 {ECO:0000313|EMBL:AAW89517.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89517.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89517.1; -; Genomic_DNA. DR RefSeq; WP_003688609.1; NC_002946.2. DR RefSeq; YP_207929.1; NC_002946.2. DR ProteinModelPortal; Q5F8H0; -. DR EnsemblBacteria; AAW89517; AAW89517; NGO_0803. DR GeneID; 3281979; -. DR KEGG; ngo:NGO0803; -. DR PATRIC; 20334760; VBINeiGon24812_0950. DR HOGENOM; HOG000282351; -. DR KO; K06207; -. DR OMA; SMLFTIN; -. DR OrthoDB; EOG67HJSM; -. DR BioCyc; NGON242231:GI2G-759-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW GTP-binding {ECO:0000256|RuleBase:RU000323}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000323}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 197 Tr-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51722}. SQ SEQUENCE 603 AA; 67182 MW; D0D287EE2ABABB3D CRC64; MKQIRNIAII AHVDHGKTTL VDQLLRQSGT FRANQQVDER VMDSNDLEKE RGITILAKNT AIDYEGCHIN IVDTPGHADF GGEVERVLGM VDCVVLLVDA QEGPMPQTRF VTKKALALGL KPIVVINKID KPSARPSWVI DQTFELFDNL GATDEQLDFP IVYASGLSGF AKLEETDESS DMRPLFDTIL KYTPAPSGSA DEPLQLQISQ LDYDNYTGRL GIGRILNGRI KPGQTVAVMN HEQQIAQGRI 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 Q5F5M7_NEIG1 Unreviewed; 333 AA. AC Q5F5M7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 73. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_1894 {ECO:0000313|EMBL:AAW90510.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90510.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90510.1; -; Genomic_DNA. DR RefSeq; WP_003690264.1; NC_002946.2. DR RefSeq; YP_208922.1; NC_002946.2. DR ProteinModelPortal; Q5F5M7; -. DR REBASE; 10867; M2.NgoAXVIP. DR EnsemblBacteria; AAW90510; AAW90510; NGO_1894. DR GeneID; 3282284; -. DR KEGG; ngo:NGO1894; -. DR PATRIC; 20337492; VBINeiGon24812_2277. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; AIFIANR; -. DR OrthoDB; EOG6S52JC; -. DR BioCyc; NGON242231:GI2G-1794-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90510.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90510.1}. FT DOMAIN 6 328 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 333 AA; 37237 MW; 67DFF42AECBCACBE CRC64; MHTPLTYIDL FSGAGGLSLG FEQAGFQQLL SVEMESDYCQ TYRTNFPRHQ LLQKDLTTLT EQDLTNCLNG QSVDLVIGGP PCQGFSMAGK IGRTFTDDPR NHLFKEFVRI VKIVQPYFFV MENVARLYTH NSGKTRIEII QAFQNIGYSV ECKILSAADF GVPQIRSRVI FIGRRDKGKI SFPEPLQISH QTVGSAIGHF PKLAAGESNP HVANHEAMNH SAQMLEKMAF VKNGGNRNDI PEPLRPKTGD IRKYIRYNSN KPAVCITGDM RKVFHYEQNR ALTVRELAAL QSFPDNFIFC GSKIAQQQQV GNAVPPLLAK AIAESILKMS ENE // ID Q5FA11_NEIG1 Unreviewed; 177 AA. AC Q5FA11; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE RecName: Full=Inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00209}; DE EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00209}; DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00209}; GN Name=ppa {ECO:0000256|HAMAP-Rule:MF_00209}; GN ORFNames=NGO_0223 {ECO:0000313|EMBL:AAW88976.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88976.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00209}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00209}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}. CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000256|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; AE004969; AAW88976.1; -; Genomic_DNA. DR RefSeq; WP_003687553.1; NC_002946.2. DR RefSeq; YP_207388.1; NC_002946.2. DR ProteinModelPortal; Q5FA11; -. DR EnsemblBacteria; AAW88976; AAW88976; NGO_0223. DR GeneID; 3281467; -. DR KEGG; ngo:NGO0223; -. DR PATRIC; 20333385; VBINeiGon24812_0275. DR HOGENOM; HOG000236472; -. DR KO; K01507; -. DR OMA; SEVEYFF; -. DR OrthoDB; EOG6NKR4X; -. DR BioCyc; NGON242231:GI2G-206-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00209}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT METAL 67 67 Magnesium 1. {ECO:0000256|HAMAP- FT Rule:MF_00209}. FT METAL 72 72 Magnesium 1. {ECO:0000256|HAMAP- FT Rule:MF_00209}. FT METAL 72 72 Magnesium 2. {ECO:0000256|HAMAP- FT Rule:MF_00209}. FT METAL 104 104 Magnesium 1. {ECO:0000256|HAMAP- FT Rule:MF_00209}. SQ SEQUENCE 177 AA; 19767 MW; 600FBB241AE81567 CRC64; MADFNQILTP GDVDGGIINV VNEIPAGSNH KIEWNRKLAA FQLDRIEPAI FAKPTNYGFI PQTLDEDGDE LDVLLVTEQP LATGVFLEAR VIGVMKFVDD GEVDDKIVCV PADDRNNGNA YKTLSDLPQQ LIKQIEFHFN HYKDLKKAGT TKVESWGGAE EAKKVIKESI ERWNKQA // ID Q5F832_NEIG1 Unreviewed; 223 AA. AC Q5F832; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Thermonuclease {ECO:0000313|EMBL:AAW89655.2}; GN ORFNames=NGO_0969 {ECO:0000313|EMBL:AAW89655.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89655.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89655.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F832; -. DR EnsemblBacteria; AAW89655; AAW89655; NGO_0969. DR PATRIC; 20335132; VBINeiGon24812_1135. DR HOGENOM; HOG000017398; -. DR OMA; MDSVGEW; -. DR OrthoDB; EOG632D5H; -. DR BioCyc; NGON242231:GI2G-897-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 62 190 TNase-like. FT {ECO:0000259|PROSITE:PS50830}. SQ SEQUENCE 223 AA; 24719 MW; 6E6CBCC1A79DDCC6 CRC64; MQIKKIMKWL PVALSLLGAL GYTGYDSEAV RTAVAVLDVL GTAGDVGFDA PVRRRASAKS GHSYTGTVSK VYDGDTLHVI DGDGAKHKIR MAYIDAPEMK QAYGTRSRDN LRAAAEGRKV SVRVFETDRY QREVAQVSAG KTDLNLMQVQ DGAAWHYKSY AKEQQDKADF ADYADAQIQA ERERKGLWKA KNPQAPWAYR RAGRSGGGNK DWMDSVGEWL GIW // ID Q5FAD0_NEIG1 Unreviewed; 215 AA. AC Q5FAD0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Pilus assembly protein PilO {ECO:0000313|EMBL:AAW88857.1}; GN ORFNames=NGO_0096 {ECO:0000313|EMBL:AAW88857.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88857.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88857.1; -; Genomic_DNA. DR RefSeq; WP_010356664.1; NC_002946.2. DR RefSeq; YP_207269.1; NC_002946.2. DR ProteinModelPortal; Q5FAD0; -. DR EnsemblBacteria; AAW88857; AAW88857; NGO_0096. DR GeneID; 3282139; -. DR KEGG; ngo:NGO0096; -. DR PATRIC; 20333089; VBINeiGon24812_0128. DR HOGENOM; HOG000218780; -. DR KO; K02664; -. DR OMA; TARTFRY; -. DR OrthoDB; EOG6VQPV4; -. DR BioCyc; NGON242231:GI2G-86-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.540; -; 1. DR Gene3D; 3.30.70.60; -; 1. DR InterPro; IPR007445; PilO. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. DR InterPro; IPR023218; UPF0291_struct_dom. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 23345 MW; 7EB63CD495160158 CRC64; MASKSSKTNL DLNNLHLLNL PARLFIALLV VAAVLGLGYA GLFKSQMESL EEYEAKETEL KNTYKQKSID AASLNNLRDE LASIRSTFDI MLKQLPTDAE IPNLVQELHQ AGSSNGLRLD SVMPQPPVDD GPIKKLPYSI SITGNYEQIS QFTRDVGSLS RIITLESLKI AQSPENGGNP DGKSSILNLS AIATTYQAKS VEELAAEAAQ NAEQK // ID Q5F545_NEIG1 Unreviewed; 322 AA. AC Q5F545; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 59. DE SubName: Full=Iron ABC transporter permease {ECO:0000313|EMBL:AAW90692.1}; GN ORFNames=NGO_2091 {ECO:0000313|EMBL:AAW90692.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90692.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90692.1; -; Genomic_DNA. DR RefSeq; WP_010951404.1; NC_002946.2. DR RefSeq; YP_209104.1; NC_002946.2. DR ProteinModelPortal; Q5F545; -. DR EnsemblBacteria; AAW90692; AAW90692; NGO_2091. DR GeneID; 3282826; -. DR KEGG; ngo:NGO2091; -. DR PATRIC; 20338015; VBINeiGon24812_2530. DR HOGENOM; HOG000045408; -. DR KO; K02015; -. DR OMA; VFMLLIR; -. DR OrthoDB; EOG61ZTDC; -. DR BioCyc; NGON242231:GI2G-1986-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of 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 Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00417419, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00417419, KW ECO:0000256|SAM:Phobius}. 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 246 262 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; 34459 MW; 4B9399CA8A4E964C CRC64; MTAKPFSLNL ANLLLPAVLF AVSLSVGIAD FRWSDVFSLS DSQQVMFISR LPRTFAIVLT GASMAVAGMI MQILMRNRFV EPSMAGAGQS AALGLLLMSL LLPAAPLPVK MSVAAVAALI GMLVFMLLIR RLPPTAQLMV PLVGIIFGGV VEAVATFVAY EFEMLQMLGV WQQGDFSSVL LGRYELLWIT GGLAVFAYLI ADRLTILGLG ETVSVNLGLN RTAVLWSGLI IVALITSLVI VTVGNIPFIG LVVPNIVSRL MGDRLRQSLP AVALLGASLV LLCDIIGRMI VFPFEIPVST VFGVLGTALF LWLLLRKPAY AV // ID Q5F730_NEIG1 Unreviewed; 81 AA. AC Q5F730; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90007.2}; GN ORFNames=NGO_1359 {ECO:0000313|EMBL:AAW90007.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90007.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90007.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90007; AAW90007; NGO_1359. DR PATRIC; 20336103; VBINeiGon24812_1600. DR HOGENOM; HOG000071326; -. DR OMA; ERADNEM; -. DR OrthoDB; EOG6GN754; -. DR BioCyc; NGON242231:GI2G-1272-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 81 AA; 9352 MW; E07C00A65975D33B CRC64; MNTVQTVWHI RMYRYSELNL NQYGVASPCR TICTVCGSPP CPDLNLIHYS ITRFERADNE MPSEQHLRFG RHFVCGAEAF A // ID Q5F865_NEIG1 Unreviewed; 245 AA. AC Q5F865; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. DE SubName: Full=Glutathione peroxidase {ECO:0000313|EMBL:AAW89622.1}; GN ORFNames=NGO_0926 {ECO:0000313|EMBL:AAW89622.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89622.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89622.1; -; Genomic_DNA. DR RefSeq; WP_003688387.1; NC_002946.2. DR RefSeq; YP_208034.1; NC_002946.2. DR ProteinModelPortal; Q5F865; -. DR SMR; Q5F865; 8-243. DR PeroxiBase; 4781; NgPrxGrx. DR PRIDE; Q5F865; -. DR EnsemblBacteria; AAW89622; AAW89622; NGO_0926. DR GeneID; 3282577; -. DR KEGG; ngo:NGO0926; -. DR PATRIC; 20335035; VBINeiGon24812_1087. DR HOGENOM; HOG000255884; -. DR OMA; DKMFIEP; -. DR OrthoDB; EOG6PKFB5; -. DR BioCyc; NGON242231:GI2G-864-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; 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; -; 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89622.1}; KW Peroxidase {ECO:0000313|EMBL:AAW89622.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 162 245 Glutaredoxin. FT {ECO:0000259|PROSITE:PS51354}. SQ SEQUENCE 245 AA; 26880 MW; 3C2E397EB010D0B1 CRC64; MALQDRTGQK VPSVVFRTRV GDTWKDVSTD DLFKGKKVVV FSLPGAFTPT CSSSHLPRYN ELFGAFKENG VDAICCVSVN DTFVMNAWAA EEESDNIYMI PDGNGEFTEG MGMLVGKEDL GFGKRSWRYS MLVNDGVVEK MFIEPEEPGD PFKVSDADTM LKFVAPDWKA QESVAIFTKP GCQFCAKVKQ ALQDKGLSYE EIVLGKDATV TSVRAITGKM TAPQVFIGGK YIGGSEDLEA YLAKN // ID Q5F6S8_NEIG1 Unreviewed; 42 AA. AC Q5F6S8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90109.1}; GN ORFNames=NGO_1469 {ECO:0000313|EMBL:AAW90109.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90109.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90109.1; -; Genomic_DNA. DR RefSeq; WP_003693645.1; NC_002946.2. DR RefSeq; YP_208521.1; NC_002946.2. DR EnsemblBacteria; AAW90109; AAW90109; NGO_1469. DR GeneID; 3281657; -. DR KEGG; ngo:NGO1469; -. DR PATRIC; 20336371; VBINeiGon24812_1734. DR OrthoDB; EOG647V7T; -. DR BioCyc; NGON242231:GI2G-1374-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 42 AA; 4908 MW; 8C006222B626FF5C CRC64; MLRRACLQSE NDFKRKRQYV SDNTGKCATI ASLMKIRYKG II // ID Q5F7L1_NEIG1 Unreviewed; 268 AA. AC Q5F7L1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 57. DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AAW89826.1}; GN ORFNames=NGO_1160 {ECO:0000313|EMBL:AAW89826.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89826.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89826.1; -; Genomic_DNA. DR RefSeq; WP_003689761.1; NC_002946.2. DR RefSeq; YP_208238.1; NC_002946.2. DR ProteinModelPortal; Q5F7L1; -. DR EnsemblBacteria; AAW89826; AAW89826; NGO_1160. DR GeneID; 3282238; -. DR KEGG; ngo:NGO1160; -. DR PATRIC; 20335591; VBINeiGon24812_1359. DR HOGENOM; HOG000225273; -. DR KO; K00941; -. DR OMA; FAFHCVH; -. DR OrthoDB; EOG6XWV53; -. DR BioCyc; NGON242231:GI2G-1073-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro. 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:UP000000535}; KW Kinase {ECO:0000256|SAAS:SAAS00440394, ECO:0000313|EMBL:AAW89826.1}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00440402}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00440394, KW ECO:0000313|EMBL:AAW89826.1}. FT DOMAIN 15 262 Phos_pyr_kin. {ECO:0000259|Pfam:PF08543}. SQ SEQUENCE 268 AA; 28354 MW; DFD6E938E4679844 CRC64; MKGSFVQTLA IAGSDSGGGA GIQADLKTFQ MRGVFGTCVI TAVTAQNTLG VSAVHLVPTE TITAQIQAIR EDFDIRAYKI GMLGTAEIIE CVADKLKHCS FGRRVLDPVM IAKGGAPLLQ DSAVAALTRL LLPDTDILTP NLPEAEALTG VHIENRKDAE RAAKILLDYG VKNVIIKGGH LNGSTSGRCT DWLFTQNETL ELDSPRFPTA HTHGTGCTFS ACITAELAKG LDVCKAVQTA KAYITAAISN PLEIGAGHGP VNHWAYRD // ID Q5F897_NEIG1 Unreviewed; 139 AA. AC Q5F897; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89590.1}; GN ORFNames=NGO_0891 {ECO:0000313|EMBL:AAW89590.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89590.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89590.1; -; Genomic_DNA. DR RefSeq; WP_010951144.1; NC_002946.2. DR RefSeq; YP_208002.1; NC_002946.2. DR EnsemblBacteria; AAW89590; AAW89590; NGO_0891. DR GeneID; 3281394; -. DR KEGG; ngo:NGO0891; -. DR PATRIC; 20334955; VBINeiGon24812_1047. DR HOGENOM; HOG000071282; -. DR OMA; VEMPQGE; -. DR OrthoDB; EOG6Q8J9T; -. DR BioCyc; NGON242231:GI2G-832-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 139 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256616. SQ SEQUENCE 139 AA; 14664 MW; 3C59CBE3F4906DD7 CRC64; MKKLLMITLT GMLAACSTGV NVGRLMVEMP QGERPVVVQV PATNNPLSDA VAVGMIKTSG SPSASNMIEM LGADNINVGV AGGSQMFNKA TALYSLNHAK KVGNNVSVYM TGDSESDKAD LENAANAKNI KLHYFFNQK // ID Q5F6M6_NEIG1 Unreviewed; 382 AA. AC Q5F6M6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369}; GN ORFNames=NGO_1525 {ECO:0000313|EMBL:AAW90161.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90161.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90161.1; -; Genomic_DNA. DR RefSeq; WP_003697434.1; NC_002946.2. DR RefSeq; YP_208573.1; NC_002946.2. DR ProteinModelPortal; Q5F6M6; -. DR EnsemblBacteria; AAW90161; AAW90161; NGO_1525. DR GeneID; 3281530; -. DR KEGG; ngo:NGO1525; -. DR PATRIC; 20336542; VBINeiGon24812_1819. DR HOGENOM; HOG000021225; -. DR KO; K01659; -. DR OMA; NDEEDWS; -. DR OrthoDB; EOG6P8TP4; -. DR BioCyc; NGON242231:GI2G-1427-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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:AAW90161.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90161.1}. FT ACT_SITE 268 268 {ECO:0000256|PIRSR:PIRSR001369-1}. FT ACT_SITE 319 319 {ECO:0000256|PIRSR:PIRSR001369-1}. SQ SEQUENCE 382 AA; 42561 MW; 6BA6E9E01DFE8F12 CRC64; MTETTQTPTF KPKKSVALSG VAAGNTALCT VGRTGNDLSH RGYDILNLAQ KCEFEEVAHL LIHGHLPNKF ELAAYKTKLK SMRGLPIRVI KVLESLPAHT HPMDVMRTGV SMLGCVHPER ESHPDSEARD IADKLIASLG SILLYWYQYS HNGKRIEVES DEETVGGHFL HLLHGKRPSE SHIKAMHVSL ILYAEHEFNA STFTARVIAG TGSDMYSCIT GAIGALKGPK HGGANEVAYD IQKRYRNADE ADIRERIGRK EIVIGFGHPV YTISDPRNVV IKEVARGLSR EAGDMRLFDI AERLESVMWE EKKMFPNLDW FSAVSYQKLG VPTAMFTPLF VISRSTGWAA HVLEQRKDGK IIRPSANYAG PEDLAFVEIE ER // ID Q5F828_NEIG1 Unreviewed; 244 AA. AC Q5F828; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 74. DE SubName: Full=DNA polymerase III subunit epsilon {ECO:0000313|EMBL:AAW89659.1}; GN ORFNames=NGO_0973 {ECO:0000313|EMBL:AAW89659.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89659.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89659.1; -; Genomic_DNA. DR RefSeq; WP_003693344.1; NC_002946.2. DR RefSeq; YP_208071.1; NC_002946.2. DR ProteinModelPortal; Q5F828; -. DR EnsemblBacteria; AAW89659; AAW89659; NGO_0973. DR GeneID; 3282875; -. DR KEGG; ngo:NGO0973; -. DR PATRIC; 20335140; VBINeiGon24812_1139. DR HOGENOM; HOG000258616; -. DR KO; K02342; -. DR OMA; FHVYLNP; -. DR OrthoDB; EOG696BTR; -. DR BioCyc; NGON242231:GI2G-901-MONOMER; -. DR Proteomes; UP000000535; 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; 3.30.420.10; -; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 178 Exonuclease. {ECO:0000259|SMART:SM00479}. SQ SEQUENCE 244 AA; 27151 MW; 050E3409F9E07888 CRC64; MMTRQIILDT ETTGLYADGG DRLVEFAGLE MVNRQMTDKN LHLYVHPERD MPEEAARVHG LTIQVLEEKN APPFAEVGRQ IADFLRGAEL IIHNAKFDVG FLNMEFRRVG LPTVEELGCT VTDTLAMARE MFPGQKASLD ALCNRFSVDR SKRVLHGALI DCELLGEVYL AMTRRQFDLM GETEEEEPTA KPVASAEMKL GAKLKVIKAD EAELAAHEEY LDGLGEACIW RKEAVPSENG GENA // ID Q5FAD7_NEIG1 Unreviewed; 369 AA. AC Q5FAD7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 68. DE RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769}; GN ORFNames=NGO_0089 {ECO:0000313|EMBL:AAW88850.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88850.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88850.1; -; Genomic_DNA. DR RefSeq; WP_003704923.1; NC_002946.2. DR RefSeq; YP_207262.1; NC_002946.2. DR ProteinModelPortal; Q5FAD7; -. DR EnsemblBacteria; AAW88850; AAW88850; NGO_0089. DR GeneID; 3282253; -. DR KEGG; ngo:NGO0089; -. DR PATRIC; 20333065; VBINeiGon24812_0116. DR HOGENOM; HOG000257442; -. DR KO; K11752; -. DR OMA; YRAGEPH; -. DR OrthoDB; EOG66F07R; -. DR BioCyc; NGON242231:GI2G-79-MONOMER; -. DR UniPathway; UPA00275; UER00401. DR UniPathway; UPA00275; UER00402. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR006769}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 40059 MW; 1EDDB0668DF00B59 CRC64; MFSDTNISMM ENALRLAALG RFSTSPNPRV GCVIAHGSQI VGQGFHVKAG EPHAEVHALR QAGEMAKGAT AFVTLEPCSH YGRTPPCAEA LLRSGVTRVV AAMRDPNPPV AGKGLVLLKA AGIKTECGLL ENKARELNRG FLSRIERRRP FVRLKCAVSL DGKTALSDGS SFWITGEEAR ADVQVLRAES CAVLTGIGTV LADNPRLNVR AFPTLRQPAR IVLDSRLRLP PNSHLVTDGQ SPTYIATLER DEDKLRPYRE HAHIRILMPS ETADGKIDLH HLMRLLADEG FGEIMVEAGS ELTSAFLAEN LADEIVLYRS PKILGGGKDL FSLPENRAAL SAPPLWTPVS SEILGHDIKT VFRKNGNAF // ID Q5F794_NEIG1 Unreviewed; 208 AA. AC Q5F794; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:AAW89943.1}; GN ORFNames=NGO_1289 {ECO:0000313|EMBL:AAW89943.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89943.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89943.1; -; Genomic_DNA. DR RefSeq; WP_003689203.1; NC_002946.2. DR RefSeq; YP_208355.1; NC_002946.2. DR EnsemblBacteria; AAW89943; AAW89943; NGO_1289. DR GeneID; 3282093; -. DR KEGG; ngo:NGO1289; -. DR PATRIC; 20335921; VBINeiGon24812_1515. DR HOGENOM; HOG000039438; -. DR KO; K11068; -. DR OMA; MSHEKPL; -. DR OrthoDB; EOG6QG8NQ; -. DR BioCyc; NGON242231:GI2G-1201-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 22655 MW; A406C0FF55C7EBF2 CRC64; MYAGERFNTY SHLSGLILAA AGLMLMLLKT IGHGDGYRIF SVSVYGISLL LLYLSSSLYH GIAAGKLKSI LKKTDHCMIY VLIAGSYTPF ALVSLRNGPG WTVFSLSWLL AAAGIAQELT IGRKSEKRLL SIAIYIVMGW MVLAVMKSLT ASLPPAGLAW LAAGGMLYSV GIYWFVNDEK IRHGHGIWHL FVLGGSITQF VSVYGYVI // ID Q5F701_NEIG1 Unreviewed; 75 AA. AC Q5F701; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90036.1}; GN ORFNames=NGO_1388 {ECO:0000313|EMBL:AAW90036.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90036.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90036.1; -; Genomic_DNA. DR RefSeq; WP_003695641.1; NC_002946.2. DR RefSeq; YP_208448.1; NC_002946.2. DR EnsemblBacteria; AAW90036; AAW90036; NGO_1388. DR GeneID; 3281756; -. DR KEGG; ngo:NGO1388; -. DR HOGENOM; HOG000220765; -. DR OMA; EIKFNTL; -. DR OrthoDB; EOG6N94DG; -. DR BioCyc; NGON242231:GI2G-1301-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 75 AA; 8696 MW; 6F87C0560A3007D1 CRC64; MDIKFNTLGV ILNGVNPEEK FIKIIDGQEN TGGFLILLSS NDKFSSFDSY DDWVENLEIL KEYLQESHWI IKWVG // ID Q5FAK4_NEIG1 Unreviewed; 309 AA. AC Q5FAK4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:AAW88779.1}; GN ORFNames=NGO_0007 {ECO:0000313|EMBL:AAW88779.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88779.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88779.1; -; Genomic_DNA. DR RefSeq; WP_010950969.1; NC_002946.2. DR RefSeq; YP_009115477.1; NC_002946.2. DR ProteinModelPortal; Q5FAK4; -. DR REBASE; 5852; NgoAVI. DR EnsemblBacteria; AAW88779; AAW88779; NGO_0007. DR GeneID; 3283054; -. DR KEGG; ngo:NGO0007; -. DR PATRIC; 20332844; VBINeiGon24812_0008. DR HOGENOM; HOG000067092; -. DR OMA; HHIMCSI; -. DR OrthoDB; EOG67Q982; -. DR BioCyc; NGON242231:GI2G-6-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR010324; DRP. DR InterPro; IPR024064; FdhE-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF06044; DpnI; 1. DR SUPFAM; SSF144020; SSF144020; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW88779.1}; KW Hydrolase {ECO:0000313|EMBL:AAW88779.1}; KW Nuclease {ECO:0000313|EMBL:AAW88779.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 309 AA; 35927 MW; BAEAABC6C5A5949E CRC64; MNLFFDTQLG KQQNKATHKI RVMSEAWLEK NGYCPCCGSK PMQRFANNKP VADLFCPNCH EQYELKSKNQ KTIGNSVPDG AYRTMLERIR SDTNPNFFFL AYKKADYSIR QLVLVPKHFI TPDMIIPRNK GIKNRPHHIM CSINLAPLPE SGKIFLIDDS RIIEPETVLK KWQSNLFLRN QNAERKDWLL AVMKCIDQLT EEFTLSQMYE FENKLSIQFP QNNHIKDKIR QQLQILRDQN MIEFIGRGLY KKNRQIAPNS QGVLISNHDT EFTRNIYSSA ILKTVEVQRN IAAKGSSRKK VGELLAIYD // ID Q5F9H6_NEIG1 Unreviewed; 185 AA. AC Q5F9H6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 56. DE SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:AAW89161.2}; GN ORFNames=NGO_0418 {ECO:0000313|EMBL:AAW89161.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89161.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89161.2; -; Genomic_DNA. DR RefSeq; WP_010357421.1; NC_002946.2. DR RefSeq; YP_207573.2; NC_002946.2. DR ProteinModelPortal; Q5F9H6; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW89161; AAW89161; NGO_0418. DR GeneID; 3282998; -. DR KEGG; ngo:NGO0418; -. DR PATRIC; 20333847; VBINeiGon24812_0501. DR HOGENOM; HOG000071246; -. DR OMA; YEHHADF; -. DR OrthoDB; EOG6C8MTC; -. DR BioCyc; NGON242231:GI2G-396-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89161.2}. FT DOMAIN 2 131 Glycos_transf_1. FT {ECO:0000259|Pfam:PF00534}. SQ SEQUENCE 185 AA; 20125 MW; C009C24D2A457D69 CRC64; MFCTVSHLRR LKGHDVLLTA FARALAQCPQ LRLNIGGSGQ EEQRLKQQAA DLGIAHAVTF LGALQPEAIL DLMRNSDAFI LASRTETFGV VYIEALSQGL PVIAIHCGGA ESIVSDGNGY LVSVDDADVL ALLKIYEHHA DFSAEQLRTD CLATFGEDAV IGRLIAVFRQ AARNTARKRP KNRLK // ID Q5F657_NEIG1 Unreviewed; 204 AA. AC Q5F657; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 51. DE SubName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000313|EMBL:AAW90330.1}; GN ORFNames=NGO_1709 {ECO:0000313|EMBL:AAW90330.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90330.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90330.1; -; Genomic_DNA. DR RefSeq; WP_003689891.1; NC_002946.2. DR RefSeq; YP_208742.1; NC_002946.2. DR ProteinModelPortal; Q5F657; -. DR EnsemblBacteria; AAW90330; AAW90330; NGO_1709. DR GeneID; 3281169; -. DR KEGG; ngo:NGO1709; -. DR PATRIC; 20337010; VBINeiGon24812_2045. DR HOGENOM; HOG000275690; -. DR OMA; GKTEETY; -. DR OrthoDB; EOG6JX7NH; -. DR BioCyc; NGON242231:GI2G-1605-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 43 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 204 AA; 21928 MW; C14EB60B43910FA9 CRC64; MNFTRLLNQV LSTVQKKGNT FSGSPLNSFG GGALVAGVAS MLLNGKNRKT ITKIGSTAAL GYLAYRGYQM WQQNKGRATV TQSDFQPAGK TEETYSRTVL RTMIAAAASD GMIDEAERRT IEQESGTDPE TAAWLAAEYR LPASIGDIAA AVGNDEALAA ETYLAARLVC ADLSRKETVF LARLSQALKL DDNLVESLER QLGI // ID Q5F4Y5_NEIG1 Unreviewed; 338 AA. AC Q5F4Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 62. DE SubName: Full=Glycosyl transferase family A {ECO:0000313|EMBL:AAW90752.1}; GN ORFNames=NGO_2158 {ECO:0000313|EMBL:AAW90752.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90752.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90752.1; -; Genomic_DNA. DR RefSeq; WP_010951417.1; NC_002946.2. DR RefSeq; YP_209164.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y5; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAW90752; AAW90752; NGO_2158. DR GeneID; 3282766; -. DR KEGG; ngo:NGO2158; -. DR PATRIC; 20338170; VBINeiGon24812_2607. DR HOGENOM; HOG000218750; -. DR OMA; KSGMGEY; -. DR OrthoDB; EOG6M0T47; -. DR BioCyc; NGON242231:GI2G-2046-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90752.1}. FT DOMAIN 6 145 Glyco_trans_2-like. FT {ECO:0000259|Pfam:PF00535}. SQ SEQUENCE 338 AA; 38554 MW; 175AFEC4C3C07BFE CRC64; MQPLVSVLIC AYNVEKYFAQ SLAAVVNQTW RNLDILIVDD GSTDGTPAIA RRFQEQDGRI RIISNPRNLG FIASLNIGLD ELAKSGGGGE YIARTDADDI ASPGWIEKIV GEMEKDRSII AMGAWLEVLS EENNKSVLAA IARNGAIWDK PTRHEDIVAV FPFGNPIHNN TMIMRRSVID GGLRFDPAYI HAEDYKFWYE AGKLGRLAYY PEALVKYRFH QDQTSSKYNL QQRRTAWKIK EEIRAGYWKA AGIAVGADCL NYGLLKSTAY ALYEKALSGQ DIGCLRLFLY EYFLSLEKYS LTDLLDFLTD RVMRKLFAAP QYRKILKKML RPWKYRSY // ID Q5F5A1_NEIG1 Unreviewed; 249 AA. AC Q5F5A1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog {ECO:0000256|RuleBase:RU004385}; GN ORFNames=NGO_2028 {ECO:0000313|EMBL:AAW90636.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90636.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|RuleBase:RU004385}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 CC family. {ECO:0000256|RuleBase:RU004385}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90636.1; -; Genomic_DNA. DR RefSeq; WP_010951384.1; NC_002946.2. DR RefSeq; YP_209048.1; NC_002946.2. DR ProteinModelPortal; Q5F5A1; -. DR EnsemblBacteria; AAW90636; AAW90636; NGO_2028. DR GeneID; 3282719; -. DR KEGG; ngo:NGO2028; -. DR PATRIC; 20337839; VBINeiGon24812_2443. DR HOGENOM; HOG000014258; -. DR OMA; RVGWCTG; -. DR OrthoDB; EOG6N3CRB; -. DR BioCyc; NGON242231:GI2G-1929-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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 {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 249 AA; 27414 MW; E83C5C2F6875CB9C CRC64; MVLRRDFLAW CDETLQTASF KDYAPNGLQV EGREYIGKIV TSVTASRAAI DFAVEQKADL LLVHHGMFWK SELPTVTGWK KERIAALLRH DINMAGYHLP LDVHPILGNN AQLADRLGFA TEKRFGEQNL LNSGSLKQAK TLGALAAHIE TVLQRKPVAI GNPEREIRRV AWCTGGAQGF FQTAIDEGVD LYLTGEISEA QYHLANETGT AFISAGHHAT ERYGVRALAE SAAEVFGLEV CHFDENNPA // ID Q5F8K1_NEIG1 Unreviewed; 581 AA. AC Q5F8K1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 87. 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 ORFNames=NGO_0771 {ECO:0000313|EMBL:AAW89486.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89486.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89486.1; -; Genomic_DNA. DR RefSeq; WP_010358120.1; NC_002946.2. DR RefSeq; YP_207898.1; NC_002946.2. DR ProteinModelPortal; Q5F8K1; -. DR EnsemblBacteria; AAW89486; AAW89486; NGO_0771. DR GeneID; 3282027; -. DR KEGG; ngo:NGO0771; -. DR PATRIC; 20334690; VBINeiGon24812_0917. DR HOGENOM; HOG000258341; -. DR KO; K03581; -. DR OMA; NRERYLP; -. DR OrthoDB; EOG60GRSZ; -. DR BioCyc; NGON242231:GI2G-726-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. 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; 63056 MW; 67A3CBD30F5EC3E9 CRC64; MELQTDEFAQ AAARAAIRFL ERYAGSGNEV LANCTERLFQ ALQNGHSFIR LSGDEADALS ALAPVVGTSA APLILEGRRL FLGRMWQLEY DLAAEIKRLA AAGTSAPDAA GARQNLAKWF QGAGSEGQRD AAALALLQFF MVITGGPGTG KTTTVAKLLA LICGENENLP HIALAAPTGK AAAHMARALH RSINGFDAPE AVRRHLLKLE GQTVHRLLKL SPPKMQAAFD HIRPLPFDVL IVDEASMLDT ALMLQLLKAV KTGARVILLG DENQLPSVGI GAVLSVLSQK TVLDGETHQR LAGFLPEHGF SVSANPPVLA QNTAHLSFSH RFGDNSGIGC LARAAVSGDE GAWALFDRFP DELEHSECSP NARVERLYRA HKAYWQAVKD GNIEAAYAGI SDIVVLAAWR QDAEDFNEAY CSYVRRKMNI PEHLAYFAGE PIMIRQNDYA LELFNGDIGL IMEDVGRQGS LAAYFADADG FKKVAVSCLP EFEPAFAMTV HKSQGSEYRE VWLLPPSDAP SDEGDDALSG LSKELLYTAI TRAREKFVFF GGKKTFCQAV NTVKVRQTAL GSMLERVFSQ E // ID Q5F981_NEIG1 Unreviewed; 179 AA. AC Q5F981; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89256.1}; GN ORFNames=NGO_0518 {ECO:0000313|EMBL:AAW89256.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89256.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89256.1; -; Genomic_DNA. DR RefSeq; WP_010951071.1; NC_002946.2. DR RefSeq; YP_207668.1; NC_002946.2. DR EnsemblBacteria; AAW89256; AAW89256; NGO_0518. DR GeneID; 3282930; -. DR KEGG; ngo:NGO0518; -. DR PATRIC; 20334078; VBINeiGon24812_0611. DR HOGENOM; HOG000148526; -. DR OMA; YLGAHEK; -. DR OrthoDB; EOG6J1DFJ; -. DR BioCyc; NGON242231:GI2G-496-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR013423; CHP02594. DR TIGRFAMs; TIGR02594; TIGR02594; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 179 AA; 19551 MW; 8A4E8937EE27A948 CRC64; MKELKWIEEA RKYLGAHEKV NGKSNPVLLA MLQEMGNFNQ EQKAWWKETD TPWCGLFVGY CLGKSGRAVI RDWYRAKAWS MSGLTKLEAP AYGCIAVKPR RGGGHVFFVV GKDAEGRILG LGGNQGNMVS IIPFDPADID GYFWPSKLIG GKAVPSSPAE GRYRLSDVAA TAKQGAGEA // ID Q5F539_NEIG1 Unreviewed; 140 AA. AC Q5F539; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90698.1}; GN ORFNames=NGO_2097 {ECO:0000313|EMBL:AAW90698.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90698.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90698.1; -; Genomic_DNA. DR RefSeq; WP_003687065.1; NC_002946.2. DR RefSeq; YP_209110.1; NC_002946.2. DR EnsemblBacteria; AAW90698; AAW90698; NGO_2097. DR GeneID; 3282820; -. DR KEGG; ngo:NGO2097; -. DR PATRIC; 20338031; VBINeiGon24812_2538. DR HOGENOM; HOG000071375; -. DR OMA; IQPANPY; -. DR OrthoDB; EOG6H1Q22; -. DR BioCyc; NGON242231:GI2G-1992-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 140 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256026. SQ SEQUENCE 140 AA; 15159 MW; C7D1A42FB635C3D4 CRC64; MKHAPIILLL TASSAALLSA GCTALPSDRP PLRTLPKSAP IQPANPYSRP PSGTPDGAFS TRASNGRVLK SIVKNGVFDR FVDIYHPNGK LHSHTPVENG VAQGYTEQGI LRTRILYRDG HIVRAQTLDA SGKVEREWQP // ID Q5F772_NEIG1 Unreviewed; 36 AA. AC Q5F772; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89965.1}; GN ORFNames=NGO_1313 {ECO:0000313|EMBL:AAW89965.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89965.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89965.1; -; Genomic_DNA. DR RefSeq; WP_003691637.1; NC_002946.2. DR RefSeq; YP_208377.1; NC_002946.2. DR EnsemblBacteria; AAW89965; AAW89965; NGO_1313. DR GeneID; 3281820; -. DR KEGG; ngo:NGO1313; -. DR HOGENOM; HOG000027871; -. DR OrthoDB; EOG6RC40H; -. DR BioCyc; NGON242231:GI2G-1228-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 36 AA; 4067 MW; D50C1385257F7C63 CRC64; MINPYKFPGK IDREHEKADN PPIFKHPSDG ICSNAV // ID Q5F8C6_NEIG1 Unreviewed; 281 AA. AC Q5F8C6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. 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 ORFNames=NGO_0859 {ECO:0000313|EMBL:AAW89561.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89561.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89561.1; -; Genomic_DNA. DR RefSeq; WP_010951135.1; NC_002946.2. DR RefSeq; YP_207973.1; NC_002946.2. DR ProteinModelPortal; Q5F8C6; -. DR EnsemblBacteria; AAW89561; AAW89561; NGO_0859. DR GeneID; 3282364; -. DR KEGG; ngo:NGO0859; -. DR PATRIC; 20334886; VBINeiGon24812_1013. DR HOGENOM; HOG000262479; -. DR OMA; TYAIWYP; -. DR OrthoDB; EOG6Q8J0P; -. DR BioCyc; NGON242231:GI2G-803-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00934}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 31935 MW; 7EEC42BFD106005F CRC64; MLSYRHAFHA GNHADMLKHF TLFLVLQYFN RKDKPYWYID THGGAGVYNL EGSEAQKVGE YRQGIALLRQ AQNLPAELSD FAAHIQKILP SPELYCGSPW LAQSLTCVGD KLRLFELHPT DFVHLQNNMG EAGLGKRGQV LREDGYKGLI SLLPPPPRRA AVLIDPPYEE KQDYRRVTET LKAALKRFES GCYLIWYPCL SREESRKLPE ELKKLLPDNY LYAELHVHAP KTDGFGMHGS GMFVINPPYL LAEQLAANLP ALTRLLAQDE GARYLLDSKI R // ID Q5F7U5_NEIG1 Unreviewed; 107 AA. AC Q5F7U5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89742.1}; GN ORFNames=NGO_1073 {ECO:0000313|EMBL:AAW89742.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89742.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89742.1; -; Genomic_DNA. DR RefSeq; WP_003688020.1; NC_002946.2. DR RefSeq; YP_208154.1; NC_002946.2. DR EnsemblBacteria; AAW89742; AAW89742; NGO_1073. DR GeneID; 3281119; -. DR KEGG; ngo:NGO1073; -. DR PATRIC; 20335382; VBINeiGon24812_1257. DR HOGENOM; HOG000218653; -. DR OMA; FEFSSHI; -. DR OrthoDB; EOG6W19MX; -. DR BioCyc; NGON242231:GI2G-987-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 107 AA; 13106 MW; A6EC8DAE78C09933 CRC64; MFLDDVNVFL DDLNTNPITD EWYMSNFADK HIKILESYEA FDILKQFVDY MIEEHDEKSE YEIMEILRQL KYQADTNEKF YTNTQKQKIV ELYKQEISQD ILNEIFR // ID Q5F5G8_NEIG1 Unreviewed; 429 AA. AC Q5F5G8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90569.1}; GN ORFNames=NGO_1958 {ECO:0000313|EMBL:AAW90569.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90569.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90569.1; -; Genomic_DNA. DR RefSeq; WP_003705160.1; NC_002946.2. DR RefSeq; YP_208981.1; NC_002946.2. DR ProteinModelPortal; Q5F5G8; -. DR EnsemblBacteria; AAW90569; AAW90569; NGO_1958. DR GeneID; 3282663; -. DR KEGG; ngo:NGO1958; -. DR PATRIC; 20337665; VBINeiGon24812_2359. DR HOGENOM; HOG000218697; -. DR OMA; ANQTGNN; -. DR OrthoDB; EOG6W45NK; -. DR BioCyc; NGON242231:GI2G-1859-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 429 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255466. SQ SEQUENCE 429 AA; 44644 MW; B4399A69CD5BFF6C CRC64; MFKRSVIAMA CIFPLSACGG GGGGSPDVKS ADTPSKPAAP VVAENAGEGV LPKEKKDEEA AGGAPQADTQ DATAGEGSQD MAAVSAENTG NGGAATTDNP KNEDAGAQND MPQNAAESAN QTGNNQPAGS SDSAPASNPA PANGGSDFGR TNVGNSVVID GPSQNITLTH CKGDSCNGDN LLDEEAPSKS EFEKLSDEEK IKRYKKDEQR ENFVGLVADR VKKDGTNKYI IFYTDKPPTR SARSRRSLPA EIPLIPVNQA DTLIVDGEAV SLTGHSGNIF APEGNYRYLT YGAEKLPGGS YALRVQGEPA KGEMLVGTAV YNGEVLHFHM ENGRPYPSGG RFAAKVDFGS KSVDGIIDSG DDLHMGTQKF KAAIDGNGFK GTWTENGGGD VSGRFYGPAG EEVAGKYSYR PTDAEKGGFG VFAGKKDRD // ID Q5F717_NEIG1 Unreviewed; 56 AA. AC Q5F717; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Cytochrome C oxidase subunit IV {ECO:0000313|EMBL:AAW90020.1}; GN ORFNames=NGO_1372 {ECO:0000313|EMBL:AAW90020.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90020.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90020.1; -; Genomic_DNA. DR RefSeq; WP_003693747.1; NC_002946.2. DR RefSeq; YP_208432.1; NC_002946.2. DR EnsemblBacteria; AAW90020; AAW90020; NGO_1372. DR GeneID; 3282495; -. DR KEGG; ngo:NGO1372; -. DR PATRIC; 20336133; VBINeiGon24812_1615. DR HOGENOM; HOG000027885; -. DR KO; K00407; -. DR OrthoDB; EOG6ZPT5F; -. DR BioCyc; NGON242231:GI2G-1285-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR008621; Cbb3-typ_cyt_oxidase_comp. DR Pfam; PF05545; FixQ; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 56 AA; 6644 MW; 7F9D32549300E6B1 CRC64; MDINGIRALF TVWIFICFLL VLYIVFNRRN KKNYDDAANS IFAENQDAQD KKSENR // ID Q5F983_NEIG1 Unreviewed; 115 AA. AC Q5F983; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Growth inhibitor PemK {ECO:0000313|EMBL:AAW89254.1}; GN ORFNames=NGO_0516 {ECO:0000313|EMBL:AAW89254.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89254.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89254.1; -; Genomic_DNA. DR RefSeq; WP_010951070.1; NC_002946.2. DR RefSeq; YP_207666.1; NC_002946.2. DR ProteinModelPortal; Q5F983; -. DR EnsemblBacteria; AAW89254; AAW89254; NGO_0516. DR GeneID; 3282932; -. DR KEGG; ngo:NGO0516; -. DR PATRIC; 20334074; VBINeiGon24812_0609. DR HOGENOM; HOG000290185; -. DR KO; K18841; -. DR OMA; LACPITT; -. DR OrthoDB; EOG67X204; -. DR BioCyc; NGON242231:GI2G-494-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 115 AA; 12437 MW; A8EB52369E1F7AD9 CRC64; MYIPERGDIF HLAFDPAAGT EMKGGHYAIA LSPRAYNRAT GLVYACPISQ GRAAAARSGG MISTLLGTGT ATQGNVHCHR MKALDWKIRR AAFRETVPDY VIEDVLARIG AVLFD // ID Q5F6R9_NEIG1 Unreviewed; 209 AA. AC Q5F6R9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90118.1}; GN ORFNames=NGO_1479 {ECO:0000313|EMBL:AAW90118.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90118.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90118.1; -; Genomic_DNA. DR DNASU; 3281613; -. DR EnsemblBacteria; AAW90118; AAW90118; NGO_1479. DR PATRIC; 20336403; VBINeiGon24812_1749. DR OrthoDB; EOG6JTC6K; -. DR BioCyc; NGON242231:GI2G-1384-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011006; CheY-like_superfamily. DR SUPFAM; SSF52172; SSF52172; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 209 AA; 23458 MW; B72DD3AA633EB0D3 CRC64; MEVQLPKIKT VRVMLAGMTA QQESVFKMAF KMHNTTRYET VSPSDGSAVP DLVLADTDAE GGFELWKELA GRYKAIPVAV CSEKVPDSEV PYLPKPIRFE TLFPMLRKLL QGENVYGKSF IAPADRSAKN NGNVQRTVTI RQFNPNKGLL GALRFAEKNR QDIAILHGNK PVLNCFPLDT TGFADRKCVK TRRIVQRRKF AGQLQDCSR // ID Q5F7F3_NEIG1 Unreviewed; 272 AA. AC Q5F7F3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915}; GN ORFNames=NGO_1225 {ECO:0000313|EMBL:AAW89884.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89884.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). {ECO:0000256|RuleBase:RU003915}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000256|RuleBase:RU004231}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89884.1; -; Genomic_DNA. DR RefSeq; WP_003702005.1; NC_002946.2. DR RefSeq; YP_208296.1; NC_002946.2. DR ProteinModelPortal; Q5F7F3; -. DR EnsemblBacteria; AAW89884; AAW89884; NGO_1225. DR GeneID; 3281825; -. DR KEGG; ngo:NGO1225; -. DR PATRIC; 20335763; VBINeiGon24812_1440. DR HOGENOM; HOG000154888; -. DR KO; K03772; -. DR OMA; GRYIANT; -. DR OrthoDB; EOG6DRPKW; -. DR BioCyc; NGON242231:GI2G-1136-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. 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. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU004231}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Rotamase {ECO:0000256|RuleBase:RU004231}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 272 Peptidyl-prolyl cis-trans isomerase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255511. FT DOMAIN 167 253 PPIase FKBP-type. FT {ECO:0000259|PROSITE:PS50059}. SQ SEQUENCE 272 AA; 28922 MW; E9A285D73C7A38DA CRC64; MNTIFKISAL TLSAALALSA CGKKEAAPAS ASEPAAASAA QGDTSSIGST MQQASYAMGV DIGRSLKQMK EQGAEIDLKV FTDAMQAVYD GKEIKMTEEQ AQEVMMKFLQ EQQAKAVEKH KADAKANKEK GEAFLKENAA KDGVKTTASG LQYKITKQGE GKQPTKDDIV TVEYEGRLID GTVFDSSKAN GGPATFPLSQ VIPGWTEGVR LLKEGGEATF YIPSNLAYRE QGAGEKIGPN ATLVFDVKLV KIGAPENAPA KQPDQVDIKK VN // ID Q5F8P6_NEIG1 Unreviewed; 337 AA. AC Q5F8P6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89441.1}; GN ORFNames=NGO_0721 {ECO:0000313|EMBL:AAW89441.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89441.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89441.1; -; Genomic_DNA. DR RefSeq; WP_003693055.1; NC_002946.2. DR RefSeq; YP_207853.1; NC_002946.2. DR EnsemblBacteria; AAW89441; AAW89441; NGO_0721. DR GeneID; 3282084; -. DR KEGG; ngo:NGO0721; -. DR PATRIC; 20334572; VBINeiGon24812_0858. DR HOGENOM; HOG000071296; -. DR OMA; SGKEISC; -. DR OrthoDB; EOG6SR8ZV; -. DR BioCyc; NGON242231:GI2G-681-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 195 225 {ECO:0000256|SAM:Coils}. FT COILED 296 330 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 337 AA; 37799 MW; 99961864D77C3CB6 CRC64; MKKNLPALAL ASMLILSGCD RLGIGNPFSG KEISCGSEET KEILVKLVRD NVEGETVKTF DDDAFKDQAF ADIGISHIRR MVERLGITVD EVRTTEKTDT SSKLKCEAAL KLDVPDDVVD YAVAANQSIG NSHKKTPDFF EPYYRKEGAY YVKTISYSVQ PTDDKSKIFA ELSQAHDIIH PLSELVSMAL IKEPLDKAKQ RNEKLEAAEA TAQEAREAEE AAAQEALGRE QEAARVSEWE ERYKLSRSEF EQFWKGLPQT VQNKLQASQK TWKSGMDKIC ANNAKAEGET PNGIKVSELA CKTAETEARL EELHNRKKAL IDEMVREEDK KELPKRL // ID Q5F6W1_NEIG1 Unreviewed; 233 AA. AC Q5F6W1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 68. DE SubName: Full=ABC transporter permease {ECO:0000313|EMBL:AAW90076.1}; GN ORFNames=NGO_1433 {ECO:0000313|EMBL:AAW90076.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90076.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90076.1; -; Genomic_DNA. DR RefSeq; WP_003705775.1; NC_002946.2. DR RefSeq; YP_208488.1; NC_002946.2. DR EnsemblBacteria; AAW90076; AAW90076; NGO_1433. DR GeneID; 3281714; -. DR KEGG; ngo:NGO1433; -. DR PATRIC; 20336285; VBINeiGon24812_1691. DR HOGENOM; HOG000146177; -. DR KO; K02050; -. DR OMA; MPPIIWV; -. DR OrthoDB; EOG6BPDMF; -. DR BioCyc; NGON242231:GI2G-1341-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|RuleBase:RU363032, KW ECO:0000256|SAAS:SAAS00524216}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 20 40 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 80 102 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 114 136 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 142 164 Helical. {ECO:0000256|RuleBase:RU363032}. FT TRANSMEM 185 207 Helical. {ECO:0000256|RuleBase:RU363032}. FT DOMAIN 72 233 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50928}. SQ SEQUENCE 233 AA; 25013 MW; 97DEB59DFB26FA93 CRC64; MIKTDKIRKP QPALFYIIDY LWSGFAGLSV AMAMVALWAW GSAVFGEFML PAPVEVFQKS LDLLKHFQEN EIGISLWRSV VGISVALIAG LAAGLVAGLV AGSFKTAMAL LKPVITILLA MPPIIWVVMA LFWFGFGNPS VLFTIIVLVA PLTFASAAVG MASVNKQHEE LFDAYKLGRL KKIRYLYIPH LTGYVISSVG VAVAMGVKAV IMAELLGASK GVGARIADAR AML // ID Q5F6A5_NEIG1 Unreviewed; 252 AA. AC Q5F6A5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 52. DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:AAW90282.1}; GN ORFNames=NGO_1655 {ECO:0000313|EMBL:AAW90282.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90282.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90282.1; -; Genomic_DNA. DR RefSeq; WP_003689788.1; NC_002946.2. DR RefSeq; YP_208694.1; NC_002946.2. DR ProteinModelPortal; Q5F6A5; -. DR EnsemblBacteria; AAW90282; AAW90282; NGO_1655. DR GeneID; 3281306; -. DR KEGG; ngo:NGO1655; -. DR PATRIC; 20336856; VBINeiGon24812_1973. DR HOGENOM; HOG000219114; -. DR OMA; PRRTGNT; -. DR OrthoDB; EOG654P29; -. DR BioCyc; NGON242231:GI2G-1551-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR InterPro; IPR000297; PPIase_PpiC. DR Pfam; PF13145; Rotamase_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Isomerase {ECO:0000313|EMBL:AAW90282.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256588. FT DOMAIN 112 225 PpiC. {ECO:0000259|Pfam:PF13145}. SQ SEQUENCE 252 AA; 28570 MW; 33687F5D395A0730 CRC64; MKQKKTAAAV IAAMLAGFAA AKAPEIDPAL VDTLVAQIMQ QADRHAEQSQ RPDGQAIRND AVRRLQTLEV LKNRALKEGL DKDKDVQNRF KIAEASFYAE EYVRFLERSE TVSESALRQF YERQIRMIKL QQVSFATEEE ARQAQQLLLK GLSFEGLMKR YPNDEQAFDG FIMAQQLPEP LASQFAGMNR GDVTRNPVKL GERYYLFKLG AVGKNPDAQP FELVRNQLEQ GLRQEKARLK IDALLEENGV KP // ID Q5F884_NEIG1 Unreviewed; 233 AA. AC Q5F884; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89603.1}; GN ORFNames=NGO_0905 {ECO:0000313|EMBL:AAW89603.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89603.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89603.1; -; Genomic_DNA. DR RefSeq; WP_003688414.1; NC_002946.2. DR RefSeq; YP_208015.1; NC_002946.2. DR ProteinModelPortal; Q5F884; -. DR DNASU; 3281189; -. DR EnsemblBacteria; AAW89603; AAW89603; NGO_0905. DR GeneID; 3281189; -. DR KEGG; ngo:NGO0905; -. DR PATRIC; 20334991; VBINeiGon24812_1065. DR HOGENOM; HOG000257978; -. DR KO; K00782; -. DR OMA; VHTEIHL; -. DR OrthoDB; EOG6VB704; -. DR BioCyc; NGON242231:GI2G-845-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 43 217 DUF162. {ECO:0000259|Pfam:PF02589}. SQ SEQUENCE 233 AA; 25794 MW; 5EF9188E9CEAA373 CRC64; MSARENILAK LKKAGALPME EPAVFDYYRE KGVSWDSEAE RLKHWAAAMR AVKTEIYWVT KSNWMQVFRE AAEGKGLKNI LLPLATEHGQ IARAALAGSN IDPIAFEREI DTWKTEFFTN IDAGFSGAQC GIARTGTLML FSSPEEPRTL SLVPPVHFCL FDTSKMYNEF HNAVEGEKLV ENGMPTNVFL ISGPSKTADI QLTLAYGAHG PRDLVILAIL PDHISPADLE ENA // ID Q5FAC3_NEIG1 Unreviewed; 395 AA. AC Q5FAC3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Cytochrome C biogenesis protein {ECO:0000313|EMBL:AAW88864.1}; GN ORFNames=NGO_0103 {ECO:0000313|EMBL:AAW88864.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88864.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88864.1; -; Genomic_DNA. DR RefSeq; WP_003687361.1; NC_002946.2. DR RefSeq; YP_207276.1; NC_002946.2. DR EnsemblBacteria; AAW88864; AAW88864; NGO_0103. DR GeneID; 3282441; -. DR KEGG; ngo:NGO0103; -. DR PATRIC; 20333105; VBINeiGon24812_0136. DR HOGENOM; HOG000099341; -. DR OMA; MWYSVAR; -. DR OrthoDB; EOG6Z9B0Z; -. DR BioCyc; NGON242231:GI2G-93-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 44584 MW; C241FF172443561B CRC64; MTEHYKTLPE HELLIQKSLI RNLNLWDWVF AVLVFAATVF VQTRSGMHMD IYETVMLWAS AGIAVFLGWF FKPMRWFVPL SVLLAYAAVG LYGGNIKSAE IFLLRYFLSS QSAIMWQCAF VFFALFAYIS GAVLASVKNV PTNTLLGMGT VFAWVSAVAG FTGLLVRWHE SYLLRPDAGH IPVSNLYEVF ILFLVITALM YLYYEGKFAV QKLGGFVFGF MAVVVGFVLW YSVSREAHTI QPLIPALQSW WMKIHVPANF IGYGAFCISA MLGIAELVSL RAEEKGGKLW LPPSALIDEV MYKAIAVGFL FFTIATILGA LWAADAWGRY WSWDPKETWA FIVWLNYAVW LHLRLVAGWR GKVLAWWAII GLFVTAFAFI GVNMFLSGLH SYGTL // ID Q5F8B8_NEIG1 Unreviewed; 263 AA. AC Q5F8B8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89569.1}; GN ORFNames=NGO_0868 {ECO:0000313|EMBL:AAW89569.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89569.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89569.1; -; Genomic_DNA. DR RefSeq; WP_010951138.1; NC_002946.2. DR RefSeq; YP_207981.1; NC_002946.2. DR ProteinModelPortal; Q5F8B8; -. DR EnsemblBacteria; AAW89569; AAW89569; NGO_0868. DR GeneID; 3281834; -. DR KEGG; ngo:NGO0868; -. DR PATRIC; 20334908; VBINeiGon24812_1024. DR HOGENOM; HOG000218928; -. DR OMA; TKINEYG; -. DR OrthoDB; EOG64V2B4; -. DR BioCyc; NGON242231:GI2G-811-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256066. SQ SEQUENCE 263 AA; 28894 MW; E06D7E31697F7CA8 CRC64; MKKALLALTI AAISGTAMAQ LPDFLGKGEY TVRTDISKQT LKNADLKEKH KVQKNIGFRA DMPFDDIHHG MRFEVSHSRD KKDMYVVTES TTKPFGKDVE EKRTDVYAGY TYTQPISEAT KLRAGLGLGY EKYKDAVANE KGTVSTEREA FYTKAHADLT SDLGGGWYLN PWAEVKVDLD AKLKHNATVA GVSADINAKT RGWGVGVGAN IGKQITDTVG IEAGPFYKHR HFKASGSFVL DGGNIRVDPT KINEYGVRVG VKF // ID Q5F6G4_NEIG1 Unreviewed; 181 AA. AC Q5F6G4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90223.1}; GN ORFNames=NGO_1595 {ECO:0000313|EMBL:AAW90223.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90223.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90223.1; -; Genomic_DNA. DR RefSeq; WP_003689520.1; NC_002946.2. DR RefSeq; YP_208635.1; NC_002946.2. DR EnsemblBacteria; AAW90223; AAW90223; NGO_1595. DR GeneID; 3281738; -. DR KEGG; ngo:NGO1595; -. DR PATRIC; 20336718; VBINeiGon24812_1905. DR HOGENOM; HOG000220705; -. DR OMA; ITVEHLE; -. DR OrthoDB; EOG6MSS2S; -. DR BioCyc; NGON242231:GI2G-1491-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR020941; SUFU-like_domain. DR Pfam; PF05076; SUFU; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 26 177 SUFU. {ECO:0000259|Pfam:PF05076}. SQ SEQUENCE 181 AA; 21206 MW; 304A97B642503947 CRC64; MIIVEHLEHY LGEIESGIKC LDRRYHLSVS VFPSQPYKGV TTFSTLGLNR YDLNYKSRFE LIFTCSEEWN KENIAAFLSG VAEYLIDNRQ PILRGEIIQL PRVIIEGSKM DALYVSAPFY FDDDFQVCYG EHYNIVFPLL VPLYKQEAEL VEKKGWNAFE QFLLNNEVDN LSDMKRKPFA W // ID Q5FAJ6_NEIG1 Unreviewed; 175 AA. AC Q5FAJ6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Diguanylate cyclase {ECO:0000313|EMBL:AAW88787.1}; GN ORFNames=NGO_0018 {ECO:0000313|EMBL:AAW88787.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88787.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88787.1; -; Genomic_DNA. DR RefSeq; WP_003696618.1; NC_002946.2. DR RefSeq; YP_207199.1; NC_002946.2. DR ProteinModelPortal; Q5FAJ6; -. DR EnsemblBacteria; AAW88787; AAW88787; NGO_0018. DR GeneID; 3283062; -. DR KEGG; ngo:NGO0018; -. DR PATRIC; 20332866; VBINeiGon24812_0018. DR HOGENOM; HOG000022909; -. DR KO; K07170; -. DR OMA; FQGQPAC; -. DR OrthoDB; EOG6QP15Z; -. DR BioCyc; NGON242231:GI2G-15-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 39 175 GAF. {ECO:0000259|SMART:SM00065}. SQ SEQUENCE 175 AA; 19093 MW; 097BE57AF8D0DBD1 CRC64; MYANMGDMMH ALHFSASDKA ALYREVLPQI ESVVADEADW VANLANTAAV LKEAFGWLWV GFYFVDTRSD ELVLAPFQGP LACTRIPFGR GVCGQAWAKG ETVVVKDVNA HPDHIACSSL SRSEIVVPLF SDGRCIGVLD ADSEHLAQFD EADALYLGEL AKILERRFEA SSQAA // ID Q5F727_NEIG1 Unreviewed; 49 AA. AC Q5F727; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=TonB dependent receptor family protein {ECO:0000313|EMBL:AAW90010.1}; GN ORFNames=NGO_1362 {ECO:0000313|EMBL:AAW90010.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90010.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90010.1; -; Genomic_DNA. DR RefSeq; WP_003698758.1; NC_002946.2. DR RefSeq; YP_208422.1; NC_002946.2. DR EnsemblBacteria; AAW90010; AAW90010; NGO_1362. DR GeneID; 3282437; -. DR KEGG; ngo:NGO1362; -. DR PATRIC; 20336109; VBINeiGon24812_1603. DR HOGENOM; HOG000027875; -. DR OrthoDB; EOG6C5RVS; -. DR BioCyc; NGON242231:GI2G-1275-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.40.170.20; -; 1. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Receptor {ECO:0000313|EMBL:AAW90010.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5620 MW; 2225ACAE384E529A CRC64; MTAHYKIGKS TRIGLDFENV FNKRCRTMPD IHVYGTPRSL TATVKHIVD // ID Q5F6N0_NEIG1 Unreviewed; 147 AA. AC Q5F6N0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Rrf2 family transcriptional regulator {ECO:0000313|EMBL:AAW90157.1}; GN ORFNames=NGO_1519 {ECO:0000313|EMBL:AAW90157.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90157.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90157.1; -; Genomic_DNA. DR RefSeq; WP_003689406.1; NC_002946.2. DR RefSeq; YP_208569.1; NC_002946.2. DR ProteinModelPortal; Q5F6N0; -. DR DNASU; 3281516; -. DR EnsemblBacteria; AAW90157; AAW90157; NGO_1519. DR GeneID; 3281516; -. DR KEGG; ngo:NGO1519; -. DR PATRIC; 20336520; VBINeiGon24812_1808. DR HOGENOM; HOG000249814; -. DR KO; K13771; -. DR OMA; GCEDDPP; -. DR OrthoDB; EOG6BGP3D; -. DR BioCyc; NGON242231:GI2G-1423-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 147 AA; 16055 MW; 0AB63AAB74A6810C CRC64; MYLTQHTDYG LRVLIYTAVN DDALVNIATI ASTYGISKSH LMKVVTALVK GGFLHSVRGK GGGLRLAAPP ERINIGAVVR HLEPMQLVEC MGPNNECLIT PSCRLTGILG GAMKSFFTYL DGFTLQDLLN KPTYDLLYES KIPIAVR // ID Q5F6T5_NEIG1 Unreviewed; 180 AA. AC Q5F6T5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90102.1}; GN ORFNames=NGO_1461 {ECO:0000313|EMBL:AAW90102.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90102.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90102.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90102; AAW90102; NGO_1461. DR PATRIC; 20336353; VBINeiGon24812_1725. DR HOGENOM; HOG000071351; -. DR OMA; HRREFRS; -. DR OrthoDB; EOG6V7BM7; -. DR BioCyc; NGON242231:GI2G-1367-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 180 AA; 20483 MW; 3707B1AAE7CB61F9 CRC64; MRRAEARPAT LSMHPLASPT LRNILRTHPV KNTRTVPIHR NPKTRHSRAG GNPVRSVSVI SKNCRSVKFL DSHFRRNDAV QVSVRTDSSF PHRQESGFVR AETYAPSFPH RREFRSVGIG TYRIKRLPQP CVLDSHFRGN DDSGIPNSNP PQPTYAHPTH LPYSPVPERA DKVRCRRRAS // ID Q5F4Z6_NEIG1 Unreviewed; 288 AA. AC Q5F4Z6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 77. 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 ORFNames=NGO_2144 {ECO:0000313|EMBL:AAW90741.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90741.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90741.1; -; Genomic_DNA. DR RefSeq; WP_010951415.1; NC_002946.2. DR RefSeq; YP_209153.1; NC_002946.2. DR ProteinModelPortal; Q5F4Z6; -. DR EnsemblBacteria; AAW90741; AAW90741; NGO_2144. DR GeneID; 3282777; -. DR KEGG; ngo:NGO2144; -. DR PATRIC; 20338141; VBINeiGon24812_2593. DR HOGENOM; HOG000253872; -. DR KO; K02108; -. DR OMA; VGHIIAG; -. DR OrthoDB; EOG6K4054; -. DR BioCyc; NGON242231:GI2G-2035-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01393, KW ECO:0000256|RuleBase:RU000483}; 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:UP000000535}; 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 144 164 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; 31389 MW; 3ED25FE2886C5FB7 CRC64; MAGETITAAD YIKHHLQSLT SLSDVTQGQG LKNIADFSFI NLDAVFFAVL LGVIGSFLLW RGAKKATAGV PGRFQAAVEI LFEFVDDMCK SIIHSEKSKK AVAPLGLTLF VWIFLMNAMD MLPVDLLPMV WQGITGNHHA LLRIVPTADL NTALALAVGV LLICIYYNIK IKGLGGWFHE LFSAPFGAKL APANFLLNLV EFLSKTVSHG MRLFGNMYAG ELVFLLIALL VGAWAASGSV EVMDPILFVF HIIAGLAWAI FHILVITLQA FIFMALAFVY IGQAHDAH // ID Q5F5Y5_NEIG1 Unreviewed; 330 AA. AC Q5F5Y5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 76. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028}; GN ORFNames=NGO_1783 {ECO:0000313|EMBL:AAW90402.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90402.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90402.1; -; Genomic_DNA. DR RefSeq; WP_003690001.1; NC_002946.2. DR RefSeq; YP_208814.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y5; -. DR SMR; Q5F5Y5; 96-326. DR EnsemblBacteria; AAW90402; AAW90402; NGO_1783. DR GeneID; 3282524; -. DR KEGG; ngo:NGO1783; -. DR PATRIC; 20337210; VBINeiGon24812_2141. DR HOGENOM; HOG000275914; -. DR KO; K06179; -. DR OMA; IVRVPPV; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NGON242231:GI2G-1681-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU362028}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 88 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 330 AA; 36662 MW; 4946A43F71165E10 CRC64; MKTHEISKGS VSLIGVAEHE AGQRLDNYLI KILKGVPKGY IHRIIRAGEV RLNKKRCKPD SRIAEGDTVR IPPVRVAEKE MPSERRAAVP ARAFEVVYED DALLVVNKPS GVAVHGGSGV SFGVIEQLRR ARPEAKYLEL VHRLDKDTSG LLMVAKKRSA LVKLHEAIRN DHPKKIYLAL GVGKLPDDNF HVKLPLFKYT GAQGEKMVRV SEDGQSAHTV FRVLSRFSDG ILHGVGLSHL TLVRATLKTG RTHQIRVHLQ SQGCPIAGDE RYGDYQANRR LQKLGLKRMF LHASELHLNH PLTGEPLVLK AEPPPDLAQF AVMLENGTKM // ID Q5F9M8_NEIG1 Unreviewed; 374 AA. AC Q5F9M8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 71. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_0365 {ECO:0000313|EMBL:AAW89109.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89109.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89109.1; -; Genomic_DNA. DR RefSeq; WP_003687777.1; NC_002946.2. DR RefSeq; YP_207521.1; NC_002946.2. DR ProteinModelPortal; Q5F9M8; -. DR REBASE; 5858; M.NgoAVII. DR EnsemblBacteria; AAW89109; AAW89109; NGO_0365. DR GeneID; 3283023; -. DR KEGG; ngo:NGO0365; -. DR PATRIC; 20333727; VBINeiGon24812_0441. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; FAGIVCK; -. DR OrthoDB; EOG6K13Q5; -. DR BioCyc; NGON242231:GI2G-344-MONOMER; -. DR Proteomes; UP000000535; 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; 1. 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417}. FT DOMAIN 17 337 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 374 AA; 42101 MW; B42B275FA91E8AD0 CRC64; MLSKQISNLN SSSNKPKILS LFSGCGGLDL GFHQAGCETV WANDFSHWAC ESFRKNIGDV IVEGDIEQIN PNDPTIPDCD IILGGFPCQD FSMIWKQPGL EGERGNLYKS FLRFVNAKKP KVFVAENVKG LLTANKKKAI QQIITDFENC GYYVQAKLYN FAEFGVPQFR ERVLIVGVRL DTGFDFRHPE PTHNETGENG LKPYVTAGQA ISNIPQNASN NELLKISDKT RRMLELIPEG GNFTDIPKDH PLYVKGMISH VYRRMHRNEP SKTIIAAGGG GTWGYHFPEP RAFTNRERAR LQSFPDDFEF VGSTTEVRRQ IGNAVPPQGV VELAKSILPI FSDNYEKVDL HEKLVEEKEI LFHDRLSKIR GGKQ // ID Q5F5N1_NEIG1 Unreviewed; 338 AA. AC Q5F5N1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90506.1}; GN ORFNames=NGO_1889 {ECO:0000313|EMBL:AAW90506.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90506.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90506.1; -; Genomic_DNA. DR RefSeq; WP_003690269.1; NC_002946.2. DR RefSeq; YP_208918.1; NC_002946.2. DR EnsemblBacteria; AAW90506; AAW90506; NGO_1889. DR GeneID; 3282301; -. DR KEGG; ngo:NGO1889; -. DR PATRIC; 20337478; VBINeiGon24812_2270. DR HOGENOM; HOG000218677; -. DR OMA; SFAHEDG; -. DR OrthoDB; EOG6HF5WM; -. DR BioCyc; NGON242231:GI2G-1790-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR009739; DUF1311. DR Pfam; PF07007; DUF1311; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 338 AA; 36836 MW; 8A11AE16449D9830 CRC64; MYRKLIALPF ALLLAACGRE EPPKALECAN PAVLQDIRGS IQETLTQEAR SFAREDGRQF VDADKIIAAA YGLAFSLEHA SETQEGGRTF CIADLNITVP SETLADAEAN SPLLYGETSL ADIVQQKTGG NVEFKDGVLT AAVRFLPAKD ARTAFIDNTV GMATQTLSAA LLPYGVKSIV MIDGKAVTKE DAVRVLSGKA REEEPSKPTP EDILEHNAAG GDAGVPQAAE GAPEPEILHP DDVERADTVT VSRGEVEEAR VQNQRAESEI TKLWGGLDTD VQKELVGEQR KWAQEKISNC RQAAAQADRQ EYAEYLKLQC DTRMTRERIQ YLRGYSID // ID Q5FAG2_NEIG1 Unreviewed; 231 AA. AC Q5FAG2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 54. DE SubName: Full=Mannose-1-phosphate guanylyltransferase {ECO:0000313|EMBL:AAW88825.1}; GN ORFNames=NGO_0060 {ECO:0000313|EMBL:AAW88825.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88825.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88825.1; -; Genomic_DNA. DR RefSeq; WP_003687300.1; NC_002946.2. DR RefSeq; YP_207237.1; NC_002946.2. DR ProteinModelPortal; Q5FAG2; -. DR EnsemblBacteria; AAW88825; AAW88825; NGO_0060. DR GeneID; 3282348; -. DR KEGG; ngo:NGO0060; -. DR PATRIC; 20332970; VBINeiGon24812_0069. DR HOGENOM; HOG000283478; -. DR KO; K00992; -. DR OMA; VAIMQPA; -. DR OrthoDB; EOG6XHC75; -. DR BioCyc; NGON242231:GI2G-54-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW88825.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88825.1}. FT DOMAIN 2 133 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 231 AA; 24335 MW; 2A57DA28B73E44CC CRC64; MKAMILAAGR GERMRPLTDT TPKPLLDVAG KPLIGWHLCR LKQAGFTEIV INHAWLGRQI ENALGDGSAY GVNIAYSPEP AGGLETAGGI AQALPLLGGQ PFLVANGDVL TDIDFTAAFQ TASSLPGHIS AHLWLVGNPP HNPDGDFSLL PDGSVRPEVS GGNGLTFSGV GIYRPEMFDG IEAGSVAKLA PVLLNEMRQN RVSGQKHTGL WLDVGTVCRL KEAQALAAAW K // ID Q5F6M9_NEIG1 Unreviewed; 206 AA. AC Q5F6M9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90158.2}; GN ORFNames=NGO_1520 {ECO:0000313|EMBL:AAW90158.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90158.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90158.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6M9; -. DR EnsemblBacteria; AAW90158; AAW90158; NGO_1520. DR PATRIC; 20336524; VBINeiGon24812_1810. DR HOGENOM; HOG000076162; -. DR OMA; RGCGDTA; -. DR OrthoDB; EOG6C5RT4; -. DR BioCyc; NGON242231:GI2G-1424-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 199 YrdC-like. {ECO:0000259|PROSITE:PS51163}. SQ SEQUENCE 206 AA; 22570 MW; DD70A760CC7CEEB3 CRC64; MAQFFAVHPD NPQERLIKQA VEIINQGGVV VYPTDSCYAL GCKLGDKAAM ERILSIRKID LKHHLTLMCA DLSELGTYAK IDNVQFRQLK AATPGPYTFI LQATKDAPAR ALHPKRKTIG LRIPDNAVAQ ALLEELGGPL LSCTLMLPED GEPLTDPYEI RERLEHAVDL VIDGGWCGTD PTTVIDMTDG TELVRRGFGD TAVFGL // ID Q5F6E5_NEIG1 Unreviewed; 88 AA. AC Q5F6E5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90242.1}; GN ORFNames=NGO_1614 {ECO:0000313|EMBL:AAW90242.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90242.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90242.1; -; Genomic_DNA. DR RefSeq; WP_003689557.1; NC_002946.2. DR RefSeq; YP_208654.1; NC_002946.2. DR EnsemblBacteria; AAW90242; AAW90242; NGO_1614. DR GeneID; 3281478; -. DR KEGG; ngo:NGO1614; -. DR PATRIC; 20336768; VBINeiGon24812_1929. DR OMA; HISFNAF; -. DR OrthoDB; EOG6716X2; -. DR BioCyc; NGON242231:GI2G-1511-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR020518; Tscrpt_reg_PrtN. DR Pfam; PF11112; PyocinActivator; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 88 AA; 10172 MW; 81EA272754002BEC CRC64; MNISKEQGLL IAYGGRPYIP PREVHKDFFA HIGFNAFKAS GVRCELPFPI FRLSDSRKSE YFVSVRELAK AIADKEEKAK SEYRKFRS // ID Q5F8F0_NEIG1 Unreviewed; 187 AA. AC Q5F8F0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89537.1}; GN ORFNames=NGO_0827 {ECO:0000313|EMBL:AAW89537.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89537.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89537.1; -; Genomic_DNA. DR RefSeq; WP_003706275.1; NC_002946.2. DR RefSeq; YP_207949.1; NC_002946.2. DR EnsemblBacteria; AAW89537; AAW89537; NGO_0827. DR GeneID; 3282243; -. DR KEGG; ngo:NGO0827; -. DR PATRIC; 20334812; VBINeiGon24812_0976. DR HOGENOM; HOG000218950; -. DR OMA; YLMKTVI; -. DR OrthoDB; EOG622PP9; -. DR BioCyc; NGON242231:GI2G-779-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 187 AA; 21489 MW; ACC9E3770BDD33AE CRC64; MRHLENNGYA NVAGLERILA VKTDNYKEKE NLLHEIFSKS RIGDTELFAV DENLVKRLFL SLRGEIVFPK NETAESEFEK SVHERRQEGN AGSGRKQLLD LVRRGHREYP YALPRLLADA ASYKPKKSKI RLFKEAYFGK SGTRLTDEIA DGIHIYTCFS RADLEKAYSE YLELFKSESD AGGRKPR // ID Q5FAE4_NEIG1 Unreviewed; 430 AA. AC Q5FAE4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Valine--pyruvate aminotransferase {ECO:0000313|EMBL:AAW88843.1}; GN ORFNames=NGO_0082 {ECO:0000313|EMBL:AAW88843.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88843.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88843.1; -; Genomic_DNA. DR RefSeq; WP_010359743.1; NC_002946.2. DR RefSeq; YP_207255.1; NC_002946.2. DR ProteinModelPortal; Q5FAE4; -. DR DNASU; 3282138; -. DR EnsemblBacteria; AAW88843; AAW88843; NGO_0082. DR GeneID; 3282138; -. DR KEGG; ngo:NGO0082; -. DR PATRIC; 20333051; VBINeiGon24812_0109. DR HOGENOM; HOG000269357; -. DR KO; K00835; -. DR OMA; HAHQCLR; -. DR OrthoDB; EOG6QCD62; -. DR BioCyc; NGON242231:GI2G-72-MONOMER; -. DR Proteomes; UP000000535; 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:AAW88843.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Pyruvate {ECO:0000313|EMBL:AAW88843.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88843.1}. FT DOMAIN 60 419 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 430 AA; 46846 MW; D0708A39C0CBEB18 CRC64; MQFSAFGEKF TQHSGILQLM DDLGDALKSD KPVNMLGGGN PARIPEIDRA FADIFSKLAA EHAVENIGNY SNPQGDAALI DALTAFPNRE YGWNLTVGNI ALTNGSQNAF FYLFNLFGGK FKLSDGTSAE KAILLPLAPE YIGYADVHVE GRHFVSVKPK IENVEHEGEA GFFKYRVDFD ALENLPELKA GKIGAICCSR PTNPTGNVLT DGEMARLDAL AREHGIPPII DNAYGMPFPN IIDSGVTLNW HENIILCFSL SKVGLPGVRT GIIVAAPEAV KAVSSLNAIV NLAPTRFGAA IAAPLLESGE MKRLADQVIR PFYRNQAQTA VSLLKRELGA YPMKIHKPEG AIFLWLWFEN LPVSSQTLYE MLKAEGTLII PGEHFFVGID TQDYPHAGEC IRMSIAQDAQ TLEKGIAAIG KTVRKPYDNV // ID Q5FA02_NEIG1 Unreviewed; 129 AA. AC Q5FA02; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Endoribonuclease {ECO:0000313|EMBL:AAW88985.1}; GN ORFNames=NGO_0232 {ECO:0000313|EMBL:AAW88985.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88985.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88985.1; -; Genomic_DNA. DR RefSeq; WP_003687566.1; NC_002946.2. DR RefSeq; YP_207397.1; NC_002946.2. DR ProteinModelPortal; Q5FA02; -. DR EnsemblBacteria; AAW88985; AAW88985; NGO_0232. DR GeneID; 3281362; -. DR KEGG; ngo:NGO0232; -. DR PATRIC; 20333409; VBINeiGon24812_0286. DR HOGENOM; HOG000267215; -. DR OMA; EIMERYF; -. DR OrthoDB; EOG6QVRPF; -. DR BioCyc; NGON242231:GI2G-216-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 129 AA; 13407 MW; 6B124669E9336729 CRC64; MSKTVIHTDK APAAIGAYSQ AVRAGGTVYM SGQIPLDPAT MTVVGNGDFH TEARQVFQNL QAVAEAAGGS LDDIVKLNAY LTDLGNFAVF NEVMAEFITE PFPARAAVGV ASLPKGVQVE AEAVLVLNA // ID Q5F8C8_NEIG1 Unreviewed; 118 AA. AC Q5F8C8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079}; DE EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079}; GN ORFNames=NGO_0857 {ECO:0000313|EMBL:AAW89559.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89559.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89559.1; -; Genomic_DNA. DR RefSeq; WP_003688545.1; NC_002946.2. DR RefSeq; YP_207971.1; NC_002946.2. DR ProteinModelPortal; Q5F8C8; -. DR EnsemblBacteria; AAW89559; AAW89559; NGO_0857. DR GeneID; 3282152; -. DR KEGG; ngo:NGO0857; -. DR PATRIC; 20334882; VBINeiGon24812_1011. DR HOGENOM; HOG000217627; -. DR KO; K01633; -. DR OMA; DYASVST; -. DR OrthoDB; EOG6ND0KG; -. DR BioCyc; NGON242231:GI2G-801-MONOMER; -. DR UniPathway; UPA00077; UER00154. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0016787; F:hydrolase activity; 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 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:UP000000535}; KW Folate biosynthesis {ECO:0000256|RuleBase:RU362079}; KW Hydrolase {ECO:0000313|EMBL:AAW89559.1}; KW Lyase {ECO:0000256|RuleBase:RU362079}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 113 FolB. {ECO:0000259|SMART:SM00905}. SQ SEQUENCE 118 AA; 13362 MW; AAE9D22614DCDCBC CRC64; MDKIFLHGMK ADTLIGVYGW ERERLQTLIV DLDIGVPEKA GSDDDIANTV HYAEVCETLR RHLKEQDFLL LEALAEYIAD LVLGYFGAVW VHVKIVKPGI LEGVREVGVE IERGKRED // ID Q5F7A6_NEIG1 Unreviewed; 393 AA. AC Q5F7A6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89931.1}; GN ORFNames=NGO_1274 {ECO:0000313|EMBL:AAW89931.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89931.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89931.1; -; Genomic_DNA. DR RefSeq; WP_003695921.1; NC_002946.2. DR RefSeq; YP_208343.1; NC_002946.2. DR ProteinModelPortal; Q5F7A6; -. DR MEROPS; S66.002; -. DR EnsemblBacteria; AAW89931; AAW89931; NGO_1274. DR GeneID; 3282079; -. DR KEGG; ngo:NGO1274; -. DR PATRIC; 20335881; VBINeiGon24812_1495. DR HOGENOM; HOG000025480; -. DR KO; K01297; -. DR OMA; PYMPNLK; -. DR OrthoDB; EOG6JTC7M; -. DR BioCyc; NGON242231:GI2G-1189-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 393 AA; 42261 MW; 82CE3F3F899B142B CRC64; MTEPTSRRRF LKTCTAAGAG LLQACGTSAT SVPPLPSSHS VVKARTVPLQ TPRRQSSDGN LLRVVASSGF AEDTNRVNTA LTRLYNAGFT VTNQQAGSRR FQRFAGTDAQ RAADFQEVAS GRVATPKVLM GLRGGYGAAR ILPHIDFASL GARMREHGTL FFGFSDVCAV QLALLAKGNM MSFAGPMAYS DFGKPAPGAF TMDAFIKGAT QNRLTVDVPY IQRADVETEG TLWGGNLSVL ASLAGTPYMP DIDGGILFLE DVGEQPYRIE RMLNTLYLSG ILGKQRAIVF GDFRMEKIRD LYDSSYDFSA VAKHISRTAK IPVLTGFPFG HIADKITFPL GAHTRIRMNG NGGYSVAFEG YPTLDASALT LDTLLPPPDL PIFPESGVAD ISE // ID Q5F8A0_NEIG1 Unreviewed; 86 AA. AC Q5F8A0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89587.1}; GN ORFNames=NGO_0888 {ECO:0000313|EMBL:AAW89587.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89587.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89587.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89587; AAW89587; NGO_0888. DR PATRIC; 20334951; VBINeiGon24812_1045. DR HOGENOM; HOG000218919; -. DR OMA; MTGAMFV; -. DR OrthoDB; EOG679TDC; -. DR BioCyc; NGON242231:GI2G-829-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 86 AA; 9000 MW; D0B387C60D0446F1 CRC64; MWGLGLGMTG AMFVLAVFAQ LVYGDTPATD SAFNVLGLAV SVWFGAKGNS LYARHLLSRG YTELPETVEA ANPQAALAQY FGRGGG // ID Q5F879_NEIG1 Unreviewed; 296 AA. AC Q5F879; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 78. 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 ORFNames=NGO_0912 {ECO:0000313|EMBL:AAW89608.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89608.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89608.1; -; Genomic_DNA. DR RefSeq; WP_003693285.1; NC_002946.2. DR RefSeq; YP_208020.1; NC_002946.2. DR ProteinModelPortal; Q5F879; -. DR SMR; Q5F879; 2-291. DR PRIDE; Q5F879; -. DR EnsemblBacteria; AAW89608; AAW89608; NGO_0912. DR GeneID; 3281099; -. DR KEGG; ngo:NGO0912; -. DR PATRIC; 20335007; VBINeiGon24812_1073. DR HOGENOM; HOG000239685; -. DR KO; K01902; -. DR OMA; FEQDPQT; -. DR OrthoDB; EOG644ZT0; -. DR BioCyc; NGON242231:GI2G-850-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Ligase {ECO:0000256|RuleBase:RU000677, ECO:0000313|EMBL:AAW89608.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000699}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 30549 MW; 01F447EC8834C9DF CRC64; MSVLINKDTK VLVQGFTGKN GTFHSEQALA YGTKVVGGVT PGKGGQTHLD LPVFNTMKEA VKETGADASV IYVPAPFVLD SIVEAVDSGV GLVVVITEGV PTLDMLKAKR YLETNGNGTR LVGPNCPGVI TPGECKIGIM PGHIHTPGRI GIISRSGTLT YEAVAQTTNL GLGQSTCIGI GGDPIPGMNQ IDALKLFQED PDTDAIIMIG EIGGTAEEEA AEYIQSNVTK PVVGYIAGVT APKGKRMGHA GAIISGGKGT AEEKFAAFEK AGIAYTRSPA ELGTTMLEVL KAKGLA // ID Q5F9A2_NEIG1 Unreviewed; 385 AA. AC Q5F9A2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Caudovirus prohead protease family protein {ECO:0000313|EMBL:AAW89235.1}; GN ORFNames=NGO_0497 {ECO:0000313|EMBL:AAW89235.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89235.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89235.1; -; Genomic_DNA. DR RefSeq; WP_010951062.1; NC_002946.2. DR RefSeq; YP_207647.1; NC_002946.2. DR EnsemblBacteria; AAW89235; AAW89235; NGO_0497. DR GeneID; 3282952; -. DR KEGG; ngo:NGO0497; -. DR PATRIC; 20334036; VBINeiGon24812_0590. DR HOGENOM; HOG000071317; -. DR OMA; AVREMHG; -. DR OrthoDB; EOG6RRKJW; -. DR BioCyc; NGON242231:GI2G-475-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR006433; Prohead_protease. DR Pfam; PF04586; Peptidase_S78; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89235.1}; KW Protease {ECO:0000313|EMBL:AAW89235.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 301 335 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 385 AA; 40168 MW; 8078DB257DE18F84 CRC64; MTKLYAQIAK TEAQDDGTVK VWGYASSEAV DSDGEVVAAE AMKAAIPDYM KFGAVREMHG SNAAGTAIEI NVEDDGRTFF GAHIVDPVAV TKVKTGVYKG FSIGGSVTAR NDLNKSQITG LKLTEISLVD RPANPDAVFT CFKADKPKDE AGAADKDGKP SDKPTEEEDE NPKDGDKGPK TEDKGDKDAG KKDEAGKSAS VNLSESEIAA LKAVLAKADK PKGGPAAKSM YQVKSPADVL MSLKWLVEDA SYDNIDEAVT AQIKESAAGL AESLKALAAS EADKPADGLA AKAGKSGDLA KAESADELAK AQDALKKSND ALAKAQAEIE SLKKQAVPPK GSTKAISKAE DNGEDPLKGF QPIVKNDGTL DDVATLIKAK QTGRL // ID Q5F966_NEIG1 Unreviewed; 327 AA. AC Q5F966; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Periplasmic protein {ECO:0000313|EMBL:AAW89271.1}; GN ORFNames=NGO_0533 {ECO:0000313|EMBL:AAW89271.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89271.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89271.1; -; Genomic_DNA. DR RefSeq; WP_003689032.1; NC_002946.2. DR RefSeq; YP_207683.1; NC_002946.2. DR ProteinModelPortal; Q5F966; -. DR EnsemblBacteria; AAW89271; AAW89271; NGO_0533. DR GeneID; 3282914; -. DR KEGG; ngo:NGO0533; -. DR PATRIC; 20334112; VBINeiGon24812_0628. DR HOGENOM; HOG000218983; -. DR KO; K09795; -. DR OMA; PPNMRQK; -. DR OrthoDB; EOG62NX13; -. DR BioCyc; NGON242231:GI2G-511-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 327 AA; 36244 MW; 57E403F5076827D3 CRC64; MKNFLSLFAS ILMSALIAVW FSQNPINAYW QQTYHRNSPL EPLAAYGWWR SGAALQENAY ALSDGIKTFL SGETPPTAQD GGSADMPPEA AASEAAPPAG GTEWKQGTEA AAVRSGDKVF FAGDSLMQGV APFVQKSLKQ QYGIESANLS KQSTGLSYPS FFDWPKTIEE TLKKHPEISV LAVFLGPNDP WDFPVGKRYL KFASDEWAQE YLKRVDRILE AAHTHRVQVV WLGIPYMKKV KLDGQMRYLD KLLSEHLKGK IILIPTAQTL SGGKGRYTDS VNVNGKPVRY RSKDGIHFTA EGQKLLAEKI MEKIVFEPST QPSSTQP // ID Q5F7I0_NEIG1 Unreviewed; 500 AA. AC Q5F7I0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89857.2}; GN ORFNames=NGO_1197 {ECO:0000313|EMBL:AAW89857.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89857.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89857.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89857; AAW89857; NGO_1197. DR PATRIC; 20335693; VBINeiGon24812_1405. DR HOGENOM; HOG000219227; -. DR OMA; NPYGSVY; -. DR OrthoDB; EOG61ZTG1; -. DR BioCyc; NGON242231:GI2G-1109-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011202; UCP014677. DR PIRSF; PIRSF014677; UCP014677; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 500 AA; 58339 MW; 60531A436D59EA15 CRC64; MNIKEFMSNY TNHPVLFIGT GMSLRYLDNS YTWDGLLSKI AIDLFGDDRE YLNIKSRYCE DGRFQYEEIA EELQSKFDKV LENDPDGRFK EINDKFFENM RAGNTLSRFK IYISTLLSQL NYKDNSNTEL SELKKARKNV GSIITTNYDK LAQDIFEFNP LIGNDILLSN PYGSVYKIHG CVDDPSKIII TKKDYEKFKE KYELIRAQLL SLFIHNPIIF LGYNVGDENI KEILKTIFTY VEQNSPSANK IRRNFLLVEY EPESNNEDIV EHDIDITGFS TIRINKIKTD NFSQIYKALA ELTLPISAMD VRKFQSIAKE IYTGGNIKVS FTEDMDNLNN SDKVVAIGST KTISYNFQTT SEMMSNYFKI IEEENSQLLK LIDKHSIAST QYFPIYGFSR ICSDIHKEAV LKRQQKEKLD HFIEEINRRC KNNHSSIQSI LDDENISDTY KNDAIAWGIW NNQLSEDEVE NYLKNFVNKK NTHYKRLLCM FDYKKYADTV // ID Q5F8E9_NEIG1 Unreviewed; 48 AA. AC Q5F8E9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89538.1}; GN ORFNames=NGO_0828 {ECO:0000313|EMBL:AAW89538.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89538.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89538.1; -; Genomic_DNA. DR RefSeq; WP_003691144.1; NC_002946.2. DR RefSeq; YP_207950.1; NC_002946.2. DR EnsemblBacteria; AAW89538; AAW89538; NGO_0828. DR GeneID; 3282148; -. DR KEGG; ngo:NGO0828; -. DR PATRIC; 20334814; VBINeiGon24812_0977. DR HOGENOM; HOG000027809; -. DR OrthoDB; EOG625K3R; -. DR BioCyc; NGON242231:GI2G-780-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 48 AA; 5205 MW; 3EC340E51B31B82F CRC64; MEKSGIVYSM KTVIKGVYSE LNLNRYGVGS PCRTICTVCG SPPCPDFC // ID Q5F6N5_NEIG1 Unreviewed; 270 AA. AC Q5F6N5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 64. DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:AAW90152.2}; GN ORFNames=NGO_1514 {ECO:0000313|EMBL:AAW90152.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90152.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90152.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6N5; -. DR EnsemblBacteria; AAW90152; AAW90152; NGO_1514. DR PATRIC; 20336510; VBINeiGon24812_1803. DR HOGENOM; HOG000222700; -. DR OMA; REYRKIH; -. DR OrthoDB; EOG6CVV93; -. DR BioCyc; NGON242231:GI2G-1418-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. 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 Acyltransferase {ECO:0000313|EMBL:AAW90152.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90152.2}. FT DOMAIN 4 270 CN hydrolase. FT {ECO:0000259|PROSITE:PS50263}. SQ SEQUENCE 270 AA; 29280 MW; 77722EE3C8873C2F CRC64; MDKIRVAAVQ MVSGVSPETN VAAMKRLVAR AAEQGADWVL LPEYWVLMGA NDTGKLALAE PLGGGRFQTA LSETAKECGV VLFGGTVPLQ SPEAGKVMNT LLVYGCDGVR TGLYHKMHLF GFSGLGERYA EADTIRAGRE VPHLSAEGMP VAAGICYDVR FPEFFRRQLP FDVLMLPAAF THTTGKAHWE LLLRARAVEN QCYVVAAAQG GLHENGRRTF GHSMIVDPWG DVLDVLPEGE GIVTADIDAN RLNSVRNRLP ALKHRVLDAV // ID Q5F955_NEIG1 Unreviewed; 287 AA. AC Q5F955; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 67. DE SubName: Full=tRNA-modifying protein {ECO:0000313|EMBL:AAW89282.2}; GN ORFNames=NGO_0548 {ECO:0000313|EMBL:AAW89282.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89282.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89282.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F955; -. DR EnsemblBacteria; AAW89282; AAW89282; NGO_0548. DR PATRIC; 20334148; VBINeiGon24812_0646. DR HOGENOM; HOG000261299; -. DR OMA; TRILPIV; -. DR OrthoDB; EOG6QP0ZT; -. DR BioCyc; NGON242231:GI2G-522-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 70 GCV_T. {ECO:0000259|Pfam:PF01571}. SQ SEQUENCE 287 AA; 31022 MW; 52A1C8DD6A7C6214 CRC64; MKTLLPFFGV ARVSGEDRQT FLHGQLSNDI NNLQTGQACY ATYNTPKGRV IANMIVVNRG DDLLLIMAQD LLEATVKRLQ MFVLRAKAVF EILEDYAVGA ELAASAEPLA AQEPSLAFTS ECVSDGICSV ILHHRGILHI APETALPPYD AAAENAWRLH EIRSGYPWIC AATKETAVAQ MLNQHIIGGV HFKKGCYPGQ EIIARAQYRG QVKRGLAVLS GNSAAEAGIL LTADGEEAGI VLDSVQDSEN FTALAVIKFS AAQKELTVPN GGIFKAVHLF FKTKNAE // ID Q5FAG6_NEIG1 Unreviewed; 359 AA. AC Q5FAG6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000256|HAMAP-Rule:MF_02040}; GN ORFNames=NGO_0056 {ECO:0000313|EMBL:AAW88821.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88821.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88821.1; -; Genomic_DNA. DR RefSeq; WP_010950984.1; NC_002946.2. DR RefSeq; YP_207233.1; NC_002946.2. DR ProteinModelPortal; Q5FAG6; -. DR EnsemblBacteria; AAW88821; AAW88821; NGO_0056. DR GeneID; 3282337; -. DR KEGG; ngo:NGO0056; -. DR PATRIC; 20332960; VBINeiGon24812_0065. DR HOGENOM; HOG000079914; -. DR KO; K03593; -. DR OMA; ENNCLVP; -. DR OrthoDB; EOG64XXQJ; -. DR BioCyc; NGON242231:GI2G-49-MONOMER; -. DR Proteomes; UP000000535; 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 ECO:0000313|EMBL:AAW88821.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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 ECO:0000313|EMBL:AAW88821.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT NP_BIND 104 111 ATP. {ECO:0000256|HAMAP-Rule:MF_02040}. SQ SEQUENCE 359 AA; 38138 MW; 2CBC83E1F196DD6B CRC64; MNIQNIRTLL DTVAVPNTAR TLGGEKAVRS VGQRSDGIHI ALHFGFPVAH IAAALADAVQ ETLMPETGGA HIHLGIDTEI GTHKVRPGVT TIKGVKNIIA VASGKGGVGK STTTANLAAA MARMGARVGV LDADLYGPSQ PTMLGVHDRK PDQKNQKLIP VESSDGIQVM SIGFLVDTGQ AVVWRGPMVS QALQQLMFQS EWDEVDYLFI DLPPGTGDIQ LTLSQRIPVT GSVIVTTPQD IALIDARKAV DMFRKVNIPI LGVLENMSVH ICSNCGHSEA LFGTDGGKDL AARLNVPLLG QLPLSLPVRE AMDGGTPARL FDEHPAIARI YTDAAFQIAL GIADKGKDFS SRFPKIVVE // ID Q5F511_NEIG1 Unreviewed; 558 AA. AC Q5F511; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90726.1}; GN ORFNames=NGO_2128 {ECO:0000313|EMBL:AAW90726.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90726.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90726.1; -; Genomic_DNA. DR RefSeq; WP_010361207.1; NC_002946.2. DR RefSeq; YP_209138.1; NC_002946.2. DR EnsemblBacteria; AAW90726; AAW90726; NGO_2128. DR GeneID; 3282792; -. DR KEGG; ngo:NGO2128; -. DR PATRIC; 20338105; VBINeiGon24812_2575. DR HOGENOM; HOG000261088; -. DR OMA; LPYWLGA; -. DR OrthoDB; EOG6Z9B0S; -. DR BioCyc; NGON242231:GI2G-2020-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 558 AA; 62052 MW; 02E2F0B630470B4A CRC64; MLTYTPPDAR PPAKTHEKPW LLLLMAFAWL WPGVFSHDLW NPAEPAVYTA VEALAGSPTP LVAHLFGQTD FGIPPVYLWV AAAFKHLLSP WAADPYDAAR FAGVFFAVIG LTSCGFAGFN FLGRHHGRSV VLIHIGCIGL IPVAHFLNPA AAAFAAAGLV LHGYSLARRR VIAASFLLGT GWTLMSLAAA YPAAFALMLP LPVLMFFRPW QSRRLMLTAV ASLAFALPLM TVYPLLLAKT QPALFAQWLN YHVFGTFGGV RHIQTAFSLF YYLKNLLWFA LPALPLAVWT VCRTRLFSTD WGILGIVWML AVLVLLAFNP QRFQDNLVWL LPPLALFGAA QLDSLRRGAA AFVNWFGIMA FGLFAVFLWT GFFAMNYGWP AKLAERAAYF SPYYVPDIDP IPMAVAVLFT PLWLWAITRK NIRGRQAVTN WAAGVTLTWA LLMTLFLPWL DAAKSHAPVV RSMEASFSPE LKRELSDGIE CIGIGGGDLH TRIVWTQYGT LPHRVGDVRC RYRIVRLPQN ADAPQGWQTV WQGARPRNKD SKFALIRKIG ENILKTTD // ID Q5F9N5_NEIG1 Unreviewed; 140 AA. AC Q5F9N5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=Chitinase {ECO:0000313|EMBL:AAW89102.2}; GN ORFNames=NGO_0358 {ECO:0000313|EMBL:AAW89102.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89102.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89102.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89102; AAW89102; NGO_0358. DR PATRIC; 20333711; VBINeiGon24812_0433. DR HOGENOM; HOG000218861; -. DR OrthoDB; EOG66MQQT; -. DR BioCyc; NGON242231:GI2G-337-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 140 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364418. SQ SEQUENCE 140 AA; 15711 MW; 8B997ACFD8A20D83 CRC64; MKKMFLSAAL LLSAAAQTVW ADTVFSCKTD NNKYIEVQKI NRNLYEYSFG SAAKKEIAIR NSKADLLGRS DRWQGMGSGR RATMKFQNGE FMYTVWTGFD SVTHTESSGV VVERRGKEVA RVGCTPKTAQ ANFNDDDFSR // ID Q5F9V0_NEIG1 Unreviewed; 512 AA. AC Q5F9V0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Apolipoprotein N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148}; DE Short=ALP N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01148}; DE EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_01148}; GN Name=lnt {ECO:0000256|HAMAP-Rule:MF_01148}; GN ORFNames=NGO_0289 {ECO:0000313|EMBL:AAW89037.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89037.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Transfers the fatty acyl group on membrane lipoproteins. CC {ECO:0000256|HAMAP-Rule:MF_01148}. CC -!- PATHWAY: Protein modification; lipoprotein biosynthesis (N-acyl CC transfer). {ECO:0000256|HAMAP-Rule:MF_01148, CC ECO:0000256|SAAS:SAAS00088954}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01148}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01148}. CC -!- SIMILARITY: Belongs to the CN hydrolase family. Apolipoprotein N- CC acyltransferase subfamily. {ECO:0000256|HAMAP-Rule:MF_01148}. CC -!- SIMILARITY: Contains 1 CN hydrolase domain. {ECO:0000256|HAMAP- CC Rule:MF_01148}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89037.1; -; Genomic_DNA. DR RefSeq; WP_003687663.1; NC_002946.2. DR RefSeq; YP_207449.1; NC_002946.2. DR ProteinModelPortal; Q5F9V0; -. DR DNASU; 3281662; -. DR EnsemblBacteria; AAW89037; AAW89037; NGO_0289. DR GeneID; 3281662; -. DR KEGG; ngo:NGO0289; -. DR PATRIC; 20333557; VBINeiGon24812_0359. DR HOGENOM; HOG000264279; -. DR KO; K03820; -. DR OMA; DWILQIT; -. DR OrthoDB; EOG6VTJXM; -. DR BioCyc; NGON242231:GI2G-269-MONOMER; -. DR UniPathway; UPA00666; -. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_01148, KW ECO:0000256|SAAS:SAAS00461391, ECO:0000313|EMBL:AAW89037.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01148}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01148}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01148}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01148, KW ECO:0000256|SAAS:SAAS00461428}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01148, KW ECO:0000256|SAAS:SAAS00461391, ECO:0000313|EMBL:AAW89037.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01148, KW ECO:0000256|SAAS:SAAS00461428}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01148, KW ECO:0000256|SAAS:SAAS00461428}. FT TRANSMEM 5 25 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 56 76 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 92 112 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 118 138 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 169 189 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 200 220 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT TRANSMEM 487 507 Helical. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT DOMAIN 228 512 CN hydrolase. FT {ECO:0000259|PROSITE:PS50263}. FT ACT_SITE 271 271 Proton acceptor. {ECO:0000256|HAMAP- FT Rule:MF_01148}. FT ACT_SITE 339 339 {ECO:0000256|HAMAP-Rule:MF_01148}. FT ACT_SITE 389 389 Nucleophile. {ECO:0000256|HAMAP- FT Rule:MF_01148}. SQ SEQUENCE 512 AA; 56983 MW; 8B9A7B424F193733 CRC64; MFSKLDKYWQ HPALYWPLLI LFAAATPFAF APYYHFWLMP LIFGAFVRLI ELRPRFAASS AYLFGLTAYT AQFYWIHTAL HDVSGLPDLY AVPLTFLLPA YLALYPALCF WLWKKFTLPQ GIKTGLVLPI LWTLTEFARE RFLTGFGWGA IGYSQITPDS PLAGFAPLGG IHMVTLATAF LGVWLVLAID NTARSGKRLL PAILIAALLA AGYTAQQTDF TRPDGSRSTV ALLQGNIAQT LKWREDQVIP TIQKYYEQVG KTTADIVILP ETAIPIMRQN LPENILAQFA EQAQNNGSAL AVGISQYTSD GNGYENAVIN LTGYQENNQD GIPYYAKNHL VPFGEYKPLP LLTTPLYKMM DMPLSDFRKG GGKQSAMMMK NQKIAFNICY EDGFGDELIA AAKDATLLAN VSNMAWYGKS NAMYQHLQQS QARAMELGRY MVRATNTGAT AIISPKGNII AQAQPDTETV LEGHIKGYIG ETPYMKTGSS WWLMGILTLA ALILFIFRNK EH // ID Q5F671_NEIG1 Unreviewed; 141 AA. AC Q5F671; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 52. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90316.2}; GN ORFNames=NGO_1692 {ECO:0000313|EMBL:AAW90316.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90316.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90316.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90316; AAW90316; NGO_1692. DR PATRIC; 20336948; VBINeiGon24812_2018. DR HOGENOM; HOG000219492; -. DR OMA; QGWMHAK; -. DR OrthoDB; EOG67DPNK; -. DR BioCyc; NGON242231:GI2G-1586-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 52 74 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 99 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 138 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 141 AA; 16385 MW; C0C99C95D4BB7BD7 CRC64; MFSWFKLFHL FFVISWFAGL FYLPRIFVNM AMIDAPRGNP EYVRLSGMAV RLYRFMSPLG FGAVVFGAAI PFAAGRWGSG WVHVKLCLGL MLLAYQLYCG VLLRRFQDYS NAFSHRWYRV FNEIPVLLMV AALYLVVFKP F // ID Q5F8C2_NEIG1 Unreviewed; 72 AA. AC Q5F8C2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89565.1}; GN ORFNames=NGO_0863 {ECO:0000313|EMBL:AAW89565.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89565.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89565.1; -; Genomic_DNA. DR RefSeq; WP_003688536.1; NC_002946.2. DR RefSeq; YP_207977.1; NC_002946.2. DR ProteinModelPortal; Q5F8C2; -. DR EnsemblBacteria; AAW89565; AAW89565; NGO_0863. DR GeneID; 3282160; -. DR KEGG; ngo:NGO0863; -. DR PATRIC; 20334896; VBINeiGon24812_1018. DR HOGENOM; HOG000275055; -. DR KO; K09794; -. DR OMA; FERHNEL; -. DR OrthoDB; EOG63VC4F; -. DR BioCyc; NGON242231:GI2G-807-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007420; DUF465. DR Pfam; PF04325; DUF465; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 72 AA; 8222 MW; 3D0F1363C306311C CRC64; MFPEYRDLIS KLKQENSRFA RLFDEHNELD DKITGLANNP VTSGAETIDE LKKAKLKLKD ELYAILQKAA GK // ID Q5F5M3_NEIG1 Unreviewed; 288 AA. AC Q5F5M3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 70. DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|RuleBase:RU003706}; DE EC=2.7.7.24 {ECO:0000256|RuleBase:RU003706}; GN ORFNames=NGO_1898 {ECO:0000313|EMBL:AAW90514.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90514.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and CC glucose 1-phosphate, as well as its pyrophosphorolysis. CC {ECO:0000256|RuleBase:RU003706}. CC -!- CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate = CC diphosphate + dTDP-alpha-D-glucose. CC {ECO:0000256|RuleBase:RU003706}. CC -!- SIMILARITY: Belongs to the glucose-1-phosphate CC thymidylyltransferase family. {ECO:0000256|RuleBase:RU003706}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90514.1; -; Genomic_DNA. DR RefSeq; WP_010359534.1; NC_002946.2. DR RefSeq; YP_208926.1; NC_002946.2. DR ProteinModelPortal; Q5F5M3; -. DR SMR; Q5F5M3; 1-286. DR EnsemblBacteria; AAW90514; AAW90514; NGO_1898. DR GeneID; 3282292; -. DR KEGG; ngo:NGO1898; -. DR PATRIC; 20337500; VBINeiGon24812_2281. DR HOGENOM; HOG000283473; -. DR KO; K00973; -. DR OMA; PHDAEQF; -. DR OrthoDB; EOG6RC3RN; -. DR BioCyc; NGON242231:GI2G-1798-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Magnesium {ECO:0000256|RuleBase:RU003706}; KW Metal-binding {ECO:0000256|RuleBase:RU003706}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003706}. FT DOMAIN 2 238 NTP_transferase. FT {ECO:0000259|Pfam:PF00483}. SQ SEQUENCE 288 AA; 32008 MW; 0CB4F7B64E867EA4 CRC64; MKGIILAGGS GTRLYPITRG VSKQLLPVYD KPMIYYPLSV LMLAGIRDIL VITAPEDNAA FQRLLGDGSD FGIRLQYAVQ PSPDGLAQAF IIGEEFIGNG NVCLILGDNI FYGQSFTQTL KQAAAKTHGA TVFGYRVKDP ERFGVVEFDE NFNALSIEEK PQQPKSDWAV TGLYFHDNRA VEFAKQLKPS ARGELEISDL NRMYLEDGSL SVQILGRGFA WLDTGTQESL HEAASFVQTV QNIQNLHIAC LEEIAWRNGW LTKKDVETRA KPLEKTAYGQ YLLRLIGK // ID Q5F9R0_NEIG1 Unreviewed; 77 AA. AC Q5F9R0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Glutaredoxin {ECO:0000313|EMBL:AAW89077.1}; GN ORFNames=NGO_0331 {ECO:0000313|EMBL:AAW89077.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89077.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89077.1; -; Genomic_DNA. DR RefSeq; WP_003687723.1; NC_002946.2. DR RefSeq; YP_207489.1; NC_002946.2. DR ProteinModelPortal; Q5F9R0; -. DR EnsemblBacteria; AAW89077; AAW89077; NGO_0331. DR GeneID; 3283039; -. DR KEGG; ngo:NGO0331; -. DR PATRIC; 20333655; VBINeiGon24812_0405. DR HOGENOM; HOG000250076; -. DR OMA; CHYHLDE; -. DR OrthoDB; EOG6RZB9Q; -. DR BioCyc; NGON242231:GI2G-312-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 77 AA; 9256 MW; BF55D5B8EFDF967E CRC64; MKLTLMFREY CSLCHKMRDA LKPFQDEYGF GLEVVDVDEN PVLEEKYNEL IPVLLAGDEE ICHWFLDEDR LKQFLER // ID Q5F626_NEIG1 Unreviewed; 674 AA. AC Q5F626; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE SubName: Full=NADH:ubiquinone oxidoreductase subunit L {ECO:0000313|EMBL:AAW90361.1}; GN ORFNames=NGO_1740 {ECO:0000313|EMBL:AAW90361.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90361.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90361.1; -; Genomic_DNA. DR RefSeq; WP_010951337.1; NC_002946.2. DR RefSeq; YP_208773.1; NC_002946.2. DR EnsemblBacteria; AAW90361; AAW90361; NGO_1740. DR GeneID; 3281182; -. DR KEGG; ngo:NGO1740; -. DR PATRIC; 20337078; VBINeiGon24812_2079. DR HOGENOM; HOG000100570; -. DR KO; K00341; -. DR OMA; PESMEGP; -. DR OrthoDB; EOG6FZ48R; -. DR BioCyc; NGON242231:GI2G-1636-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AAW90361.1}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 56 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 87 108 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 120 137 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 202 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 222 241 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 280 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 292 313 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 320 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 367 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 387 408 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 428 445 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 487 508 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 552 569 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 650 673 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 67 125 Proton_antipo_N. FT {ECO:0000259|Pfam:PF00662}. FT DOMAIN 137 419 Proton_antipo_M. FT {ECO:0000259|Pfam:PF00361}. SQ SEQUENCE 674 AA; 74117 MW; 3D394C75CF5DB738 CRC64; MNDMTLYLII ALVPLAGSLI AGLFGNKIGR AGAHTVTILG VAVSAVLSAY VLWGFLNGSR TKFDENVYTW 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 LKKYMPITWL TMLIGNLSLI GTPFFSGFYS KDSIIEAVKY STLPGSGVAY FAVLASVFVT AFYAFRQYFM VFHGEEKWRS LPEHHSDGHG EEHHGLGKND NPHESPLVVT LPLILLAIPS VIIGYIAIEP MLYGDFFKDV IFVNADAHPT MHIMKEEFHG ALAMVSHSLT SPVLYLAAAG VAAAWLLYVK LPHLPAKIAQ AFRPVYVLFE NKYYLDALYF NVFAKGTRAL GNFFWKVGDT AIIDNGIVNG SAKLVGAIAA QVRKAQTGFI YTYAAAMVFG VLVLLGMTFW GLFR // ID Q5F9N0_NEIG1 Unreviewed; 629 AA. AC Q5F9N0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=DEAD/DEAH box helicase {ECO:0000313|EMBL:AAW89107.1}; GN ORFNames=NGO_0363 {ECO:0000313|EMBL:AAW89107.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89107.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89107.1; -; Genomic_DNA. DR RefSeq; WP_003687775.1; NC_002946.2. DR RefSeq; YP_207519.1; NC_002946.2. DR REBASE; 103508; H.NgoAVII. DR EnsemblBacteria; AAW89107; AAW89107; NGO_0363. DR GeneID; 3283030; -. DR KEGG; ngo:NGO0363; -. DR PATRIC; 20333723; VBINeiGon24812_0439. DR HOGENOM; HOG000027903; -. DR OMA; VPNIKLP; -. DR OrthoDB; EOG6M6JNX; -. DR BioCyc; NGON242231:GI2G-342-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018310; Put_endonuclease_Z1-dom. DR Pfam; PF10593; Z1; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAW89107.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Helicase {ECO:0000313|EMBL:AAW89107.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89107.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW89107.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 257 447 Z1. {ECO:0000259|Pfam:PF10593}. SQ SEQUENCE 629 AA; 71101 MW; A62A9EB8603117AB CRC64; MLRTYLNQLT PPELADSVKN TVDGFMEKLS QTEPKIAQNV LLLGNVQSGK TAQVLGVLSA LADDGDHKVF LYLTTDSVDL QDQTVKRAKA NLKNFIVLSE ADDRSFMEVM KAENPILVVI KKNARVLKRW RNLFASQSSL KGYPLVIVDD EADAASLNTN SDKPAKDAST INKLLNDIKN SCCQSLFIQL TATPQSLLLQ HEESDWQPEF IHFFEAGEKY IGGNFVFSDP PSYIVRFIDS ELDDMKDESG EIAEGAKQAL LSFLITCAEF ALCDKANCNF ALHPSYKIQD HQAFSKKIQA FLNDLVQAVN NGEDLAGSFK ESYLDLQKTK PDIHHFDEIY EKLTALLENK QISTLVVNSQ TETDFDLEKG FNIIIGGNVI GRGLTIPKLQ TVYYSRTAKK PNADTFWQHS RIFGYDRDKS LLRLYIPFDV YYFFVQLNQA NNLIIGQAKN SGGNIQVIYP KNINPTRKNV LKFDSINQIV GGVNYFPLHP NEDNLSEINK ILPSILKDEI QSDLYQIDIE DLFLVLDKLG RYVPDDWNKE KFIAGVEALK AQRPSFKTYV LIKTGRKLSR ATGTMLSEDD RKLGEKYPND LFLTLYQVVG NKDKGWQGKD FWLPNIKLPH NGLVYQSAK // ID Q5F8J3_NEIG1 Unreviewed; 123 AA. AC Q5F8J3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89494.1}; GN ORFNames=NGO_0780 {ECO:0000313|EMBL:AAW89494.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89494.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89494.1; -; Genomic_DNA. DR RefSeq; WP_003688636.1; NC_002946.2. DR RefSeq; YP_207906.1; NC_002946.2. DR ProteinModelPortal; Q5F8J3; -. DR EnsemblBacteria; AAW89494; AAW89494; NGO_0780. DR GeneID; 3281841; -. DR KEGG; ngo:NGO0780; -. DR PATRIC; 20334706; VBINeiGon24812_0925. DR HOGENOM; HOG000218960; -. DR OMA; SAGLSKW; -. DR OrthoDB; EOG6G20P3; -. DR BioCyc; NGON242231:GI2G-734-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 123 AA; 13719 MW; 51F00B4AC31F8C99 CRC64; MLFEENPIDG QFAEYECGAG GIRLAGQSFH KPVLVHKDSV CLPQCRTLSD LTPENLLSDI KPVDYPEILI IGTGAAQEFI HPKIMADFSR IGISVECMNT DSAFRTLVFL HSEGRRAWAW LQP // ID Q5F8S0_NEIG1 Unreviewed; 122 AA. AC Q5F8S0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAW89417.1}; GN ORFNames=NGO_0690 {ECO:0000313|EMBL:AAW89417.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89417.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89417.1; -; Genomic_DNA. DR RefSeq; WP_003691259.1; NC_002946.2. DR RefSeq; YP_207829.1; NC_002946.2. DR EnsemblBacteria; AAW89417; AAW89417; NGO_0690. DR GeneID; 3281888; -. DR KEGG; ngo:NGO0690; -. DR PATRIC; 20334476; VBINeiGon24812_0810. DR HOGENOM; HOG000218973; -. DR OMA; GCVSEQA; -. DR OrthoDB; EOG60W7XD; -. DR BioCyc; NGON242231:GI2G-657-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000313|EMBL:AAW89417.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 122 AA; 13031 MW; FAAACD2DAD18B405 CRC64; MNKTLSILPA AILLGGCAAG GNTFGSLDGG TGMGGSIVKM TVESQCRAEL DRRSEWRLTA LAMSAEKQAE WENKICGCAT EEAPNQLTGN DVMQMLNQST RNQALAALTV KTVSACFKRL YR // ID Q5F573_NEIG1 Unreviewed; 282 AA. AC Q5F573; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Transporter {ECO:0000313|EMBL:AAW90664.1}; GN ORFNames=NGO_2057 {ECO:0000313|EMBL:AAW90664.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90664.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90664.1; -; Genomic_DNA. DR RefSeq; WP_003687000.1; NC_002946.2. DR RefSeq; YP_209076.1; NC_002946.2. DR ProteinModelPortal; Q5F573; -. DR EnsemblBacteria; AAW90664; AAW90664; NGO_2057. DR GeneID; 3282739; -. DR KEGG; ngo:NGO2057; -. DR PATRIC; 20337915; VBINeiGon24812_2480. DR HOGENOM; HOG000110051; -. DR KO; K03442; -. DR OMA; WEVEREI; -. DR OrthoDB; EOG61GG69; -. DR BioCyc; NGON242231:GI2G-1958-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 30708 MW; 449654CCB5CF490D CRC64; MDFKQFDFLH LISVSGWGHL AEKAWAFGLN LAAALLIFLV GKWAAKRIVA VMRAAMTRAQ VDATLISFLC NVANIGLLIL VIIAALGRLG VSTTSVTALI GGAGLAVALS LKDQLSNFAA GALIILFRPF KVGDFIRVGG FEGYVREIKM VQTSLRTTDN EEVVLPNSVV MGNSIVNRSS LPLCRAQVIV GVDYNCDLKV AKEAVLKAAA EHPLSVQNEE RQPAAYITAL GDNAIEITLW AWANEADRWT LQCDLNEQVV ENLRKVNINI PFPQRDIHII NS // ID Q5F6V3_NEIG1 Unreviewed; 346 AA. AC Q5F6V3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 20-JAN-2016, entry version 87. DE SubName: Full=Ethanol-active dehydrogenase/acetaldehyde-active reductase {ECO:0000313|EMBL:AAW90084.2}; GN Name=adhP {ECO:0000313|EMBL:AAW90084.2}; GN ORFNames=NGO_1442 {ECO:0000313|EMBL:AAW90084.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90084.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90084.2; -; Genomic_DNA. DR RefSeq; WP_010951267.1; NC_002946.2. DR RefSeq; YP_208496.2; NC_002946.2. DR ProteinModelPortal; Q5F6V3; -. DR PRIDE; Q5F6V3; -. DR EnsemblBacteria; AAW90084; AAW90084; NGO_1442. DR GeneID; 3281729; -. DR KEGG; ngo:NGO1442; -. DR PATRIC; 20336303; VBINeiGon24812_1700. DR HOGENOM; HOG000294685; -. DR KO; K13953; -. DR OMA; ATHCIVS; -. DR OrthoDB; EOG6BPDJN; -. DR BioCyc; NGON242231:GI2G-1349-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Metal-binding {ECO:0000256|RuleBase:RU361277}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Zinc {ECO:0000256|RuleBase:RU361277}. FT DOMAIN 12 334 PKS_ER. {ECO:0000259|SMART:SM00829}. SQ SEQUENCE 346 AA; 36349 MW; 02E552818C185E5F CRC64; MQAVVVNKNV AGDVEVVERE VRPLEYGEAL VEVEYCGVCH TDLHVAAGDY GEKPGRVLGH EGIGLVKEVA DGVKNLKVGD RVSIAWLFQS CGSCEYCNTG RETLCRSVLN AGYTADGGMA THCIVSADYA VKVPEGLDPA QASSITCAGV TTYKAIKVSG VRPGQWIAIY GAGGLGNLGV QYAKKVFGTH VVAIDINDDK LAFAKETGAD LVVNAAKEDA AKVIQEKTGG AHAAVVTAVS AAAFNSAVNC VRAGGRVVAV GLPPESMDLS IPRLVLDGIE VVGSLVGTRK DLEEAFQFGA EGLVVPKVQL RALDEAPAIF QEMREGKITG RMVIDMKKEC GCDHHH // ID Q5F773_NEIG1 Unreviewed; 262 AA. AC Q5F773; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 64. DE SubName: Full=Hydrolase {ECO:0000313|EMBL:AAW89964.2}; GN ORFNames=NGO_1312 {ECO:0000313|EMBL:AAW89964.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89964.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89964.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F773; -. DR EnsemblBacteria; AAW89964; AAW89964; NGO_1312. DR PATRIC; 20335985; VBINeiGon24812_1543. DR HOGENOM; HOG000184780; -. DR OMA; INGQYNF; -. DR OrthoDB; EOG6DRPKW; -. DR BioCyc; NGON242231:GI2G-1227-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89964.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 6 254 HAD-like_dom. {ECO:0000259|Pfam:PF08282}. SQ SEQUENCE 262 AA; 28278 MW; 871E02CC15233FA7 CRC64; MNPKIVFFDI DDTLYRKYTD TLRPSVKTAV AALRGKGILT ALATGRSLAT IPEKVRDMMA ETGMDAVVTI NGQFALLHGK TVREVPMDTG LMGRVCAHLD GLGMDYAFVG GEGIAVSALS ECVCRALQHI ASDFFADKDY FSSKPVYQML VFAEENEMPL WSDIVEREGL KTVRWHEEAV DLLPAGMSKT DGIRSVVEAL GLEMADVMAF GDGLNDVEML SEVGFGVAMG NGEQAAKEAA KYVCPGVDED GVLRGLQDLG VI // ID Q5F8N9_NEIG1 Unreviewed; 70 AA. AC Q5F8N9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89448.1}; GN ORFNames=NGO_0729 {ECO:0000313|EMBL:AAW89448.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89448.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89448.1; -; Genomic_DNA. DR RefSeq; WP_002243493.1; NC_002946.2. DR RefSeq; YP_207860.1; NC_002946.2. DR EnsemblBacteria; AAW89448; AAW89448; NGO_0729. DR GeneID; 3282071; -. DR KEGG; ngo:NGO0729; -. DR PATRIC; 20334600; VBINeiGon24812_0872. DR HOGENOM; HOG000071294; -. DR OrthoDB; EOG6SNF2F; -. DR BioCyc; NGON242231:GI2G-688-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 70 AA; 8379 MW; D9A2B3BB29F4E9D4 CRC64; MELGYTPYNL RTLRNRCKLT QAELAQIVGV KHYIQVGRWE AEPDTETRRA DMPLEKWRQF LDWIEKTNAV // ID Q5FAC9_NEIG1 Unreviewed; 199 AA. AC Q5FAC9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Pilus assembly protein PilP {ECO:0000313|EMBL:AAW88858.1}; GN ORFNames=NGO_0097 {ECO:0000313|EMBL:AAW88858.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88858.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88858.1; -; Genomic_DNA. DR RefSeq; WP_010356666.1; NC_002946.2. DR RefSeq; YP_207270.1; NC_002946.2. DR EnsemblBacteria; AAW88858; AAW88858; NGO_0097. DR GeneID; 3282268; -. DR KEGG; ngo:NGO0097; -. DR PATRIC; 20333091; VBINeiGon24812_0129. DR HOGENOM; HOG000218781; -. DR KO; K02663; -. DR OMA; LFNFTIR; -. DR OrthoDB; EOG6W45SQ; -. DR BioCyc; NGON242231:GI2G-87-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 22256 MW; EFFBEC63F50E43E5 CRC64; MNNLIKINLL PYREEMNKRK QQQFKTLMYG AVLTGVAAVA ATYLFIDNMI NKQSEKNTLL EISIAHLDTE LSEIQKLKQE KDAFLIKKNK IEELQIKRLQ AAKILDSLNE AVPGSTYLTS LDAVTADSYR LSGRTSSDNR VAAMMRAMPN TGIFKQPELL SIKKNNSHQE FTLQATLQPI VKAAESKENP ASGNAQEAN // ID Q5F6W4_NEIG1 Unreviewed; 405 AA. AC Q5F6W4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=TonB-dependent receptor {ECO:0000313|EMBL:AAW90073.2}; GN ORFNames=NGO_1430 {ECO:0000313|EMBL:AAW90073.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90073.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90073.2; -; Genomic_DNA. DR PRIDE; Q5F6W4; -. DR EnsemblBacteria; AAW90073; AAW90073; NGO_1430. DR PATRIC; 20336279; VBINeiGon24812_1688. DR HOGENOM; HOG000071347; -. DR OMA; NGERNTH; -. DR OrthoDB; EOG61S2V1; -. DR BioCyc; NGON242231:GI2G-1338-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004872; F:receptor activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.40.170.20; -; 2. DR InterPro; IPR000531; TonB-dep_rcpt_b-brl. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Receptor {ECO:0000313|EMBL:AAW90073.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 405 AA; 45859 MW; 528C95AC481635A4 CRC64; MTVFSVAPSW AEQPANTEEI QPVKTFSPPK PIAPTAAQGY FPENQFDRSD RSDYYFVTEN IDQAFRPLKA NSSFYGKSFY NSVTAQALGA KVYGVANLNR TKANGYKDGG GRDTDWKYSR FNQALVLGFV PSENQEYRLT YLHDDINNDR QPQVVNDALD TERHISKLNV RWGNADLSNT VSAEAGVIKL KRHADNYSLR PNNTPQQVFV ELDRKVYDFS LKHDADFGKF HNTAAVSYRN DSQNGERNTH TAMCDFLNGY RFADVHIDRW CIADTLSYKF DDRHKLGLGL SYELNEADIR KNTAQPENPI KPGFPFASSQ QIWKTHYGYD FNGKVRRHAL SGELKYDFTP SETQKYSVSL AHLERIGDNT ERFNSLAAIV QNRMSGMLMN QNPAAAIAGN PPAEN // ID Q5F9W1_NEIG1 Unreviewed; 759 AA. AC Q5F9W1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Competence protein ComA {ECO:0000313|EMBL:AAW89026.2}; GN ORFNames=NGO_0276 {ECO:0000313|EMBL:AAW89026.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89026.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89026.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9W1; -. DR EnsemblBacteria; AAW89026; AAW89026; NGO_0276. DR PATRIC; 20333525; VBINeiGon24812_0343. DR HOGENOM; HOG000262043; -. DR OMA; EMFPEQS; -. DR OrthoDB; EOG647TTM; -. DR BioCyc; NGON242231:GI2G-258-MONOMER; -. DR Proteomes; UP000000535; 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; IPR025405; DUF4131. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF03772; Competence; 1. DR Pfam; PF13567; DUF4131; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 48 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 308 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 329 350 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 356 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 386 405 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 417 435 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 462 484 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 523 701 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 759 AA; 82298 MW; 32820B5D3DFC9BAD CRC64; MTVLWLCFII VCFLYREWGD VFRRWFLPCW VVGVAVSFAL SVVPHWPFWL AAFAVLAVLA RRFAFAGLML CVLAGAAYGV FRTEAALSSQ WRAEAVSGVP LTVEVTDMPR SDGRRVQFAA KAVDSGGRTF DLLLSDYKRR EWAVGSRWRI TARVHPVVGE LNLRGLNREA WALSNGVGGV GTVGADRVLL HGGSGWGIAV WRSRISRNWR QADADGGLSD GIGLMRALSV GEQSALRPEL WQAFRPLGLT HLVSISGLHV TMVAVLFAWL AKRLLACSPR LPARPRAWVL AAGCAGALFY ALLAGFSVPT QRSVLMLAAF AWAWRRGRLS AWATWWQALA AVLLFDPLAV LGVGTWLSFG LVAALIWACA GCLYEGKRQT AVRGQWAASV LSLVLLGYLF ASLPLVSPLV NAVSIPWFSW VLTPLALLGS VVPFAPLQQA GAFLAEYTLR FLVWLADVSP EFAVAAAPLP LLVLAVCAAL LLLLPRGLGL RPWAVLLLAG FVSYRPEAVP ENEAAVTVWD AGQGLSVLVR TANRHLLFDT GTVAAAQTGI VPSLNAAGVR RLDKLVLSHH DSDHDGGFQA VGKIPNGGIY AGQPEFYEGA RHCAEQRWQW DGVDFEFLRP SERKNIDDNG KSCVLRVVAG GAALLVTGDL DTKGEESLVG KYGGNLYSQV LVLGHHGSNT SSSGVFLNAV SPEYAVASSG YANAYKHPTE AVQNRVRAHG IKLLRTDLSG ALQFGLGRGG VKAQRLRVYK FYWQKKPFE // ID Q5F7C7_NEIG1 Unreviewed; 165 AA. AC Q5F7C7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 48. DE SubName: Full=Prokaryotic membrane lipolipid attachment site family protein {ECO:0000313|EMBL:AAW89910.2}; GN ORFNames=NGO_1251 {ECO:0000313|EMBL:AAW89910.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89910.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89910.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89910; AAW89910; NGO_1251. DR PATRIC; 20335835; VBINeiGon24812_1472. DR HOGENOM; HOG000219036; -. DR OMA; APSHWAD; -. DR OrthoDB; EOG6M9DVZ; -. DR BioCyc; NGON242231:GI2G-1168-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 165 AA; 18613 MW; 0EB282FBF1941EED CRC64; MAGMKKYLIP LSIAAVLSGC QSIYVPTLTE IPVNPINTVK TEAPAKGFRL APSHWADVAK ISDEATRLGY QVGIGKMTKV QAAQYLNNFR KRLVGRNAVD DSMYEIYLRS AVDSQRGEIN TEQSKLYIEN ALRGWQQRWK NMDAKPDNPA FTNFLMEVMK MQPLK // ID Q5FAL2_NEIG1 Unreviewed; 107 AA. AC Q5FAL2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Cupin {ECO:0000313|EMBL:AAW88791.1}; GN ORFNames=NGO_0022 {ECO:0000313|EMBL:AAW88791.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88791.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88791.1; -; Genomic_DNA. DR RefSeq; WP_010950973.1; NC_002946.2. DR RefSeq; YP_207203.1; NC_002946.2. DR ProteinModelPortal; Q5FAL2; -. DR SMR; Q5FAL2; 4-102. DR EnsemblBacteria; AAW88791; AAW88791; NGO_0022. DR GeneID; 3283065; -. DR KEGG; ngo:NGO0022; -. DR PATRIC; 20332874; VBINeiGon24812_0022. DR HOGENOM; HOG000031295; -. DR OMA; MIGEMND; -. DR OrthoDB; EOG6K6VBF; -. DR BioCyc; NGON242231:GI2G-19-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 41 99 Cupin_2. {ECO:0000259|Pfam:PF07883}. SQ SEQUENCE 107 AA; 12038 MW; C9F79A05346CEFF7 CRC64; MQNETINLKQ HLAAIKEYWQ PEIINRHGFQ FRLVKLLVDY GWHTHGYSDK VLFAVEGDMA VDFADGGNMT IREGEMAVVP KSVSHRPRSE NGCSVVLIDL PDPSEAA // ID Q5F8W2_NEIG1 Unreviewed; 184 AA. AC Q5F8W2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89375.1}; GN ORFNames=NGO_0648 {ECO:0000313|EMBL:AAW89375.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89375.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89375.1; -; Genomic_DNA. DR RefSeq; WP_003688863.1; NC_002946.2. DR RefSeq; YP_207787.1; NC_002946.2. DR EnsemblBacteria; AAW89375; AAW89375; NGO_0648. DR GeneID; 3281772; -. DR KEGG; ngo:NGO0648; -. DR PATRIC; 20334384; VBINeiGon24812_0764. DR HOGENOM; HOG000219000; -. DR OMA; RTHMKKI; -. DR OrthoDB; EOG6DNT9S; -. DR BioCyc; NGON242231:GI2G-615-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 19 46 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 184 AA; 20296 MW; 4F31D60FD69D7FC9 CRC64; MKKIIASALI ATFALTACQD DTQARLERQQ KQIEALQQQL AQQADDTVYQ LTPEAVKDTI PAQAQANGNN GQPVTGKDGQ QYIYDQSTGS WLLQSLIGAA AGAFIGNALA NKFTRAGNQD SPVARRARAA YHQSARPNAR TSRDLNTRSL RAKQQAAQAQ RYRPTTRPPV NYRRPAMRGF GRRR // ID Q5F711_NEIG1 Unreviewed; 220 AA. AC Q5F711; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 65. DE SubName: Full=Biopolymer transporter ExbB {ECO:0000313|EMBL:AAW90026.2}; GN ORFNames=NGO_1378 {ECO:0000313|EMBL:AAW90026.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90026.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU004057}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU004057}. CC -!- SIMILARITY: Belongs to the exbB/tolQ family. CC {ECO:0000256|RuleBase:RU004057}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90026.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90026; AAW90026; NGO_1378. DR PATRIC; 20336145; VBINeiGon24812_1621. DR HOGENOM; HOG000134792; -. DR OMA; SQAINHQ; -. DR OrthoDB; EOG6JDWB5; -. DR BioCyc; NGON242231:GI2G-1291-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protein transport {ECO:0000256|RuleBase:RU004057}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU004057}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 151 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 192 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 72 203 MotA_ExbB. {ECO:0000259|Pfam:PF01618}. SQ SEQUENCE 220 AA; 24132 MW; 0247734B36123FB5 CRC64; MNLKLVFESG DPVLIGVFVL MLLMSTVTWC LVVLRCIKLY RARKGNAAVK RHMRDTLSLN DAVEKVRAVD APLSKLAQEA LQSYRNYRRN EASELAQALP LNEYLVIQIR NSMAQIMRRF DYGMTALASI GATAPFIGLF GTVWGIYHAL INIGQSGQMS IAAVAGPIGE ALVATAAGLF VAIPAVLAYN FLNRGTKILT QDLDAMAHDL HVRLLNQKDS // ID Q5F743_NEIG1 Unreviewed; 700 AA. AC Q5F743; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=AsmA family protein {ECO:0000313|EMBL:AAW89994.1}; GN ORFNames=NGO_1344 {ECO:0000313|EMBL:AAW89994.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89994.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89994.1; -; Genomic_DNA. DR RefSeq; WP_003693786.1; NC_002946.2. DR RefSeq; YP_208406.1; NC_002946.2. DR EnsemblBacteria; AAW89994; AAW89994; NGO_1344. DR GeneID; 3282014; -. DR KEGG; ngo:NGO1344; -. DR PATRIC; 20336061; VBINeiGon24812_1580. DR HOGENOM; HOG000219074; -. DR OMA; PTALKQN; -. DR OrthoDB; EOG67Q964; -. DR BioCyc; NGON242231:GI2G-1258-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007844; AsmA. DR Pfam; PF05170; AsmA; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 611 AsmA. {ECO:0000259|Pfam:PF05170}. SQ SEQUENCE 700 AA; 77174 MW; F716AAFB80BA3F60 CRC64; MDLLSVFHKY RLKYAVAVLT MLLLAAVGLH ASVYRTFTPE NIRSRLQQSI AHTHRKISFD ADIRRRLLPR PTVILKNLTI TEPDGGRVAV SVKETKIGLS WKNLWSDRIQ VEKWVVSGAD LALTRDRNGA WNIQDLFDGA KHSASVNRII VENSTVRLNF LQQQLILKEI SLNLQSPDSS GQQFESSGIL VWRKLSVPWK SRGLFLSDGI GTPEISPFHF EASTSLDGHG ITISTTGSPS VRFNAGGADA AGLGLRADTS FRNLHLTAQI PALALKNNSI KTGTVNGTFT AGGEYARWDG SFKLDKANLH SGIANIGNAE ISGSFKTPRL QTNFSLGSPL VWSRDNGLDA PRLHISTLQD TVDRLPQPRF ISRLDGSLSI PNLQNWNAEL NGTFDRQPVA AKFKYTREGA PHLEAAAALQ KLNLAPYLDE FRQQNGKIFP DILGRLSGNV EAHLKIGSIQ LPGLQLDDME TYLHADKDHI ALSRFKSGLY GGHTEGGISI ANTRPATYRL QQNASNIQIQ PLLQDLFGFH SFSGNGDAVI DLTASGENRK QLIRSLQGSL SLNISNGAWH GIDMDSILKN GLSGKISGST PFYRFTLNSE ISDGISRHID TELFSDSLYV TSNGYTNLDT QELSEDVLIR NAVHPKNKPI PLKITGTVDK PSITVDYGRL TGGINSRKEK QKILEDTLLE QWQWLKPKEP // ID Q5F9V3_NEIG1 Unreviewed; 171 AA. AC Q5F9V3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=RDD family protein {ECO:0000313|EMBL:AAW89034.2}; GN ORFNames=NGO_0285 {ECO:0000313|EMBL:AAW89034.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89034.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89034.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89034; AAW89034; NGO_0285. DR PATRIC; 20333545; VBINeiGon24812_0353. DR HOGENOM; HOG000262647; -. DR OMA; PRRQFLH; -. DR OrthoDB; EOG63VC0G; -. DR BioCyc; NGON242231:GI2G-266-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 40 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 148 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 7 161 RDD. {ECO:0000259|Pfam:PF06271}. SQ SEQUENCE 171 AA; 18968 MW; ADBF9D2A688E4238 CRC64; MMILKTAPLK RRFAAILYEM LLVGAATCLA ALLAGIAAIF LNPVSIAVSA LVTSILIMGA WWLYFRANWH GQGQTLAMRT WKIGLCDLNG IQPSLHLLRL RFIWACIFIV FIPMLAYAGL RHFLGIPPKG AAGAALVWLI LPWGFALLNP DRQFLYDFLA GTRLVDVKEQ S // ID Q5FA48_NEIG1 Unreviewed; 107 AA. AC Q5FA48; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=HIT family hydrolase {ECO:0000313|EMBL:AAW88939.1}; GN ORFNames=NGO_0184 {ECO:0000313|EMBL:AAW88939.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88939.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88939.1; -; Genomic_DNA. DR RefSeq; WP_003687490.1; NC_002946.2. DR RefSeq; YP_207351.1; NC_002946.2. DR ProteinModelPortal; Q5FA48; -. DR EnsemblBacteria; AAW88939; AAW88939; NGO_0184. DR GeneID; 3281428; -. DR KEGG; ngo:NGO0184; -. DR PATRIC; 20333295; VBINeiGon24812_0230. DR HOGENOM; HOG000061064; -. DR KO; K02503; -. DR OMA; CNPYPDG; -. DR OrthoDB; EOG69GZSV; -. DR BioCyc; NGON242231:GI2G-169-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW88939.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 107 HIT. {ECO:0000259|PROSITE:PS51084}. SQ SEQUENCE 107 AA; 11612 MW; 1315960D0912F86B CRC64; MDNCIFCKIA AKEIPAQTVY EDGEMVCFKD INPAAPLHLL LIPKVHFDSL AHAAPEHQPL LGKMMLKVPE IAKASGLTDG FKTLINTGKG GGQEVFHLHI HIMGTPV // ID Q5F6G8_NEIG1 Unreviewed; 125 AA. AC Q5F6G8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90219.1}; GN ORFNames=NGO_1591 {ECO:0000313|EMBL:AAW90219.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90219.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90219.1; -; Genomic_DNA. DR RefSeq; WP_003689514.1; NC_002946.2. DR RefSeq; YP_208631.1; NC_002946.2. DR EnsemblBacteria; AAW90219; AAW90219; NGO_1591. DR GeneID; 3281774; -. DR KEGG; ngo:NGO1591; -. DR PATRIC; 20336708; VBINeiGon24812_1900. DR HOGENOM; HOG000219105; -. DR OMA; KDIVNVQ; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NGON242231:GI2G-1487-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 125 AA; 15299 MW; 111ADFAC32F3F0F3 CRC64; MCEFKDIIRN VPYFEGYDEN SFIGKWYDDG VWDDEEYWKL ENDLIEVRRK YPYPMDIPRD IVIGIGTIIE FLMVPNWKLF EIKASPWLPD SVGINERYER LKTMLRYIFT EKDIVNVQFD YYNKK // ID Q5F5F8_NEIG1 Unreviewed; 119 AA. AC Q5F5F8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90579.1}; GN ORFNames=NGO_1970 {ECO:0000313|EMBL:AAW90579.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90579.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90579.1; -; Genomic_DNA. DR RefSeq; WP_002218298.1; NC_002946.2. DR RefSeq; YP_208991.1; NC_002946.2. DR EnsemblBacteria; AAW90579; AAW90579; NGO_1970. DR GeneID; 3282653; -. DR KEGG; ngo:NGO1970; -. DR PATRIC; 20337705; VBINeiGon24812_2379. DR HOGENOM; HOG000218645; -. DR OMA; WQPELIR; -. DR OrthoDB; EOG6GTZM7; -. DR BioCyc; NGON242231:GI2G-1869-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028964; Imm8. DR Pfam; PF15586; Imm8; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 14143 MW; 632CDBDA7D460314 CRC64; MRLKLKNYDC SDFDLEDFPQ DKLENFCILL TLSIGFDESN GADYFYVYIY STEWLLSNIH RPMSLKNSIV TNRFNIEHIL KLINDILEIC NSTSEDKSIS NLAKYFDWEF DDYNLNIQD // ID Q5F823_NEIG1 Unreviewed; 601 AA. AC Q5F823; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 83. DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399}; DE EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399}; DE AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399}; DE Flags: Precursor; GN Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399}; GN ORFNames=NGO_0978 {ECO:0000313|EMBL:AAW89664.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89664.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein CC disulfide + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00399}. CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00399}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000256|HAMAP- CC Rule:MF_00399}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89664.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F823; -. DR EnsemblBacteria; AAW89664; AAW89664; NGO_0978. DR PATRIC; 20335156; VBINeiGon24812_1147. DR HOGENOM; HOG000254982; -. DR OMA; YISQTRD; -. DR OrthoDB; EOG69D3B9; -. DR BioCyc; NGON242231:GI2G-906-MONOMER; -. DR Proteomes; UP000000535; 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; -; 2. 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 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00399}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00399}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464105}; NAD {ECO:0000256|HAMAP-Rule:MF_00399}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399}; KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|HAMAP-Rule:MF_00399}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464105}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399, KW ECO:0000256|SAAS:SAAS00464105}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00399}. FT SIGNAL 1 20 {ECO:0000256|HAMAP-Rule:MF_00399}. FT CHAIN 21 601 Thiol:disulfide interchange protein DsbD. FT {ECO:0000256|HAMAP-Rule:MF_00399}. FT /FTId=PRO_5005388627. FT TRANSMEM 192 212 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 243 263 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 267 287 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 311 331 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 347 367 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 381 401 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 407 427 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT TRANSMEM 438 458 Helical. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT DOMAIN 482 601 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. FT DISULFID 120 126 Redox-active. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT DISULFID 207 328 Redox-active. {ECO:0000256|HAMAP- FT Rule:MF_00399}. FT DISULFID 519 522 Redox-active. {ECO:0000256|HAMAP- FT Rule:MF_00399}. SQ SEQUENCE 601 AA; 64942 MW; 98E42A956315FADB CRC64; MKKLICLFAV FLMLCGRAFA LDANDLLPPE KAFVPELTVA DDGVNVRFRI ADGYYMYQAK IVGKTDPADL LGQPSFSKGE EKEDEFFGRQ TVHHHEAQVA FPYAKAVGEP YKLVLTYQGC AEAGVCYPPV DTEFDISGNG TYHPQTDEPA SAKDRFLQPS SQNGSGALPP PKGDEGGDGR 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 FALGSILLIG GAWFGWQGAN GKTTALHHFL TLNPPAEAGK FSEHGKMFAD TAALKAAMDT ALKEHPDKPV VLDFYADWCI SCKEMAVYTL NQPEVHQAVD MERFFQIDVT ANTPEHQALL KEYGLFGPPG VFVVRADGSR SEPLLGFVKA DKFIEWYEQN R // ID Q5F7L3_NEIG1 Unreviewed; 422 AA. AC Q5F7L3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89824.1}; GN ORFNames=NGO_1158 {ECO:0000313|EMBL:AAW89824.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89824.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89824.1; -; Genomic_DNA. DR RefSeq; WP_010951204.1; NC_002946.2. DR RefSeq; YP_208236.1; NC_002946.2. DR EnsemblBacteria; AAW89824; AAW89824; NGO_1158. DR GeneID; 3282228; -. DR KEGG; ngo:NGO1158; -. DR PATRIC; 20335585; VBINeiGon24812_1357. DR HOGENOM; HOG000071330; -. DR OMA; ITANHYG; -. DR OrthoDB; EOG6MWNK1; -. DR BioCyc; NGON242231:GI2G-1070-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 422 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256052. SQ SEQUENCE 422 AA; 45360 MW; 2DB6AB5A8315EF64 CRC64; MKQKKTVQCI LLGFAAASMH AQGAAAANSG TIEKTDKYTL VLAKQGQENN YTLNGGTEVK PLNSLIIAAN GGTNNITIKG KLADGPADAP PTIDNNSIER NINKNGYTYA WQNWSGAVML VDQSYEGENK VTFENVTIAA HNAPAGILSD DRHKSSSLAP AMLAFKGRNT INMDADSNAN SSNEGILLLN NGEKMGEYRL VSEEGSTLNI NIKSGKDKGQ GITANHYGNS DINFNKASPN ITTMEFKGDV NIKIDRNGQE EAESNGFGFY SSRKLGNKKQ IPEGSKMEAI FRGNVDIVAT PVYDEQGRPK SIGSAFAIDG KYSKVEVVGG EGKVVKIKGD IFAYNGGSVS VNLANKDSYF EGEAHIGKRS FAKGKDMFAL TVDADGYELT PDTKSIEKKK KELNVRGCTR LSLNSTPIPQ DF // ID Q5F9T4_NEIG1 Unreviewed; 102 AA. AC Q5F9T4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89053.1}; GN ORFNames=NGO_0306 {ECO:0000313|EMBL:AAW89053.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89053.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89053.1; -; Genomic_DNA. DR RefSeq; WP_003690777.1; NC_002946.2. DR RefSeq; YP_207465.1; NC_002946.2. DR EnsemblBacteria; AAW89053; AAW89053; NGO_0306. DR GeneID; 3281604; -. DR KEGG; ngo:NGO0306; -. DR PATRIC; 20333593; VBINeiGon24812_0376. DR HOGENOM; HOG000218853; -. DR OMA; AQWQHNH; -. DR OrthoDB; EOG62RSGG; -. DR BioCyc; NGON242231:GI2G-286-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 102 AA; 11319 MW; E4FE8C1239E683EF CRC64; MTNNVDLTIP AKRYFTLDEL CGLLQISPYG FAQWQHDHGV VVGYGGERYT RLDVVKLLKL KSTFAPYAEG AESGSDGNRP VTLQEIGDGL KDLLEDLDKE LC // ID Q5F5N7_NEIG1 Unreviewed; 196 AA. AC Q5F5N7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:AAW90500.1}; GN ORFNames=NGO_1879 {ECO:0000313|EMBL:AAW90500.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90500.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90500.1; -; Genomic_DNA. DR RefSeq; WP_003696417.1; NC_002946.2. DR RefSeq; YP_208912.1; NC_002946.2. DR ProteinModelPortal; Q5F5N7; -. DR EnsemblBacteria; AAW90500; AAW90500; NGO_1879. DR GeneID; 3282326; -. DR KEGG; ngo:NGO1879; -. DR PATRIC; 20337456; VBINeiGon24812_2259. DR HOGENOM; HOG000218674; -. DR KO; K06992; -. DR OMA; FHISEIN; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NGON242231:GI2G-1784-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 31 154 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 196 AA; 22540 MW; 265F4E16D9F02134 CRC64; MLGLCLLTPA SYQNIHVRSW KARRDSGIVK QDLDFSCGAA SIATLLNNFY GRHYSEAEIL DKMDKTQMRT SFDDMQRIMP ELGFEAQGYA LPFEQLVQLK IPVIVYLKYR KNNHFSVLNG INGETVLLAD PSLGHVSTSK SQFLSAWKTR DGEMEGKILA IVPKNTDFVR NQMFFNKNPV RQTRFTVEQI QMRQKR // ID Q5F9X2_NEIG1 Unreviewed; 165 AA. AC Q5F9X2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Colicin V production protein {ECO:0000313|EMBL:AAW89015.1}; GN ORFNames=NGO_0264 {ECO:0000313|EMBL:AAW89015.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89015.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89015.1; -; Genomic_DNA. DR RefSeq; WP_003687616.1; NC_002946.2. DR RefSeq; YP_207427.1; NC_002946.2. DR EnsemblBacteria; AAW89015; AAW89015; NGO_0264. DR GeneID; 3281544; -. DR KEGG; ngo:NGO0264; -. DR PATRIC; 20333497; VBINeiGon24812_0329. DR HOGENOM; HOG000162044; -. DR KO; K03558; -. DR OMA; DYAVVFI; -. DR OrthoDB; EOG6W4609; -. DR BioCyc; NGON242231:GI2G-247-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 17550 MW; 664009D83687FA05 CRC64; MNSLPIADLL ASAVIAACIV ISTMRGVIAE AGSMVAWVVS FFFAKLFAAP FADLAFASFQ PRLFALALSF ISLFVIACLI QKMLRSLLTG AVSAVGLGFA NRILGGVFGA LKGVLIVTLL IMLASKTDLP DTEEWQQSYT VPFFVSLSEA VLNHTDNAPE SLDDD // ID Q5F6D5_NEIG1 Unreviewed; 66 AA. AC Q5F6D5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90252.1}; GN ORFNames=NGO_1624 {ECO:0000313|EMBL:AAW90252.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90252.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90252.1; -; Genomic_DNA. DR RefSeq; WP_003695499.1; NC_002946.2. DR RefSeq; YP_208664.1; NC_002946.2. DR EnsemblBacteria; AAW90252; AAW90252; NGO_1624. DR GeneID; 3281170; -. DR KEGG; ngo:NGO1624; -. DR PATRIC; 20336788; VBINeiGon24812_1939. DR HOGENOM; HOG000071222; -. DR BioCyc; NGON242231:GI2G-1521-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 7296 MW; F40CCAB196548BD6 CRC64; MNELISKINR VGAREKDGQS LLLKVGEICR DAGATFTTRK SESLNHTAFT FTVKKDGLKD KAMIVL // ID Q5F9D2_NEIG1 Unreviewed; 163 AA. AC Q5F9D2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89205.1}; GN ORFNames=NGO_0467 {ECO:0000313|EMBL:AAW89205.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89205.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89205.1; -; Genomic_DNA. DR RefSeq; WP_010951052.1; NC_002946.2. DR RefSeq; YP_207617.1; NC_002946.2. DR EnsemblBacteria; AAW89205; AAW89205; NGO_0467. DR GeneID; 3282980; -. DR KEGG; ngo:NGO0467; -. DR PATRIC; 20333972; VBINeiGon24812_0558. DR HOGENOM; HOG000071216; -. DR OMA; KEVHEYQ; -. DR OrthoDB; EOG6HQSQB; -. DR BioCyc; NGON242231:GI2G-445-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008840; Sipho_Gp157. DR Pfam; PF05565; Sipho_Gp157; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 163 AA; 18230 MW; 7D4598DF8CCE54E7 CRC64; MTALALYRCA ADVQAALDYY FDSETEREDT LEAVIGQFEV KAQSVIAYIK NQEITEKMLE GHIRRMTGKL KAVKAQNQSL KDYLARNMQA AGITEIKADD GTFKASFRKS EAVVILDEAQ IPAEFMREAV KTEPDKTAIR KAIESGRQVA GAKIEGRKNL QIR // ID Q5F9V2_NEIG1 Unreviewed; 294 AA. AC Q5F9V2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89035.1}; GN ORFNames=NGO_0286 {ECO:0000313|EMBL:AAW89035.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89035.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89035.1; -; Genomic_DNA. DR RefSeq; WP_003687657.1; NC_002946.2. DR RefSeq; YP_207447.1; NC_002946.2. DR EnsemblBacteria; AAW89035; AAW89035; NGO_0286. DR GeneID; 3281649; -. DR KEGG; ngo:NGO0286; -. DR PATRIC; 20333547; VBINeiGon24812_0354. DR HOGENOM; HOG000037752; -. DR OMA; QEMILLA; -. DR OrthoDB; EOG61KBKV; -. DR BioCyc; NGON242231:GI2G-267-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 158 YicC_N. {ECO:0000259|Pfam:PF03755}. FT DOMAIN 209 294 DUF1732. {ECO:0000259|Pfam:PF08340}. SQ SEQUENCE 294 AA; 33289 MW; F14D88D7B1432535 CRC64; MSSGNIRIHS MTGFANAAAE CGSKRINLDI RAVNHRFLDI QIRMPDDLRH LENGIREQIS SHLARGKVEC KIQIQDAENG NQSLELNRVL VGQLAEINKN LRKHYDLAKL GVADILRFPG VLASQKENTE ALAKTIVELA DKALKDFTAA RRREGKKLGE HLLQRIKNME EIIDALSEIF PALVEAHKEK IRTRLAEAVG SIDNDRLQQE FALFIQKSDI DEEFSRLRTH IAEVRRIVTE HKGSSGKRLD FLMQELNREA NTLGSKSIAT ECTQASVELK VLIEQMREQV QNIE // ID Q5F6H0_NEIG1 Unreviewed; 225 AA. AC Q5F6H0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=MafB alternative C-terminus {ECO:0000313|EMBL:AAW90217.1}; GN ORFNames=NGO_1589 {ECO:0000313|EMBL:AAW90217.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90217.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90217.1; -; Genomic_DNA. DR RefSeq; WP_003705658.1; NC_002946.2. DR RefSeq; YP_208629.1; NC_002946.2. DR ProteinModelPortal; Q5F6H0; -. DR EnsemblBacteria; AAW90217; AAW90217; NGO_1589. DR GeneID; 3282550; -. DR KEGG; ngo:NGO1589; -. DR PATRIC; 20336704; VBINeiGon24812_1898. DR HOGENOM; HOG000219103; -. DR OrthoDB; EOG60GRTJ; -. DR BioCyc; NGON242231:GI2G-1485-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 158 225 Ntox21. {ECO:0000259|Pfam:PF15526}. SQ SEQUENCE 225 AA; 25128 MW; A5B9A30047AA8938 CRC64; MVKTADGYKA IARIRVGDHV FAKDEASGET GYKPVTAQYG NPYRETVYIE ISDGIGNNQT LISNRIHPFY SDGKWIKAED LKAGSRLLSE SGRTQTVRNI IVKPTPLKAY NLTVADWHTY FVKGNQAETE GVWVHNACPP RKTPSTPVYG NDSEAYAAAK KLGYRKIKER TRNDAAIFKK GKSYISRDVD SHNGGAWKEA SSPKNLNRKE TRNGTFDKNL NRIGD // ID Q5F5M5_NEIG1 Unreviewed; 338 AA. AC Q5F5M5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 71. DE SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:AAW90512.1}; GN ORFNames=NGO_1896 {ECO:0000313|EMBL:AAW90512.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90512.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90512.1; -; Genomic_DNA. DR RefSeq; WP_003694383.1; NC_002946.2. DR RefSeq; YP_208924.1; NC_002946.2. DR ProteinModelPortal; Q5F5M5; -. DR SMR; Q5F5M5; 1-338. DR EnsemblBacteria; AAW90512; AAW90512; NGO_1896. DR GeneID; 3282314; -. DR KEGG; ngo:NGO1896; -. DR PATRIC; 20337496; VBINeiGon24812_2279. DR HOGENOM; HOG000168001; -. DR KO; K01784; -. DR OMA; SDPSWNI; -. DR OrthoDB; EOG6WHNS9; -. DR BioCyc; NGON242231:GI2G-1796-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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; -; 1. DR InterPro; IPR005886; GalE. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR008089; Nuc_sugar_epim. DR Pfam; PF16363; GDP_Man_Dehyd; 1. DR PRINTS; PR01713; NUCEPIMERASE. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01179; galE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 324 NAD(P)-bd_dom. FT {ECO:0000259|Pfam:PF16363}. SQ SEQUENCE 338 AA; 36885 MW; C6A905035A083984 CRC64; MTVLITGGTG FIGSHTAVSL VQSGYDAVIL DNLCNSSAAV LPRLRQITGR NIPFYQGDIR DCQILRQIFS EHEIESVIHF AGLKAVGESV AEPTKYYGNN VYGSLVLAEE MARAGVLKIV FSSSATVYGD AEKVPYTEDM RPGDTANPYG ASKAMVERML TDIQKADPRW SVILLRYFNP IGAHESGLIG EQPNGVPNNL LPYICQVASG RLPQLSVFGG DYPTPDGTGM RDYIHVMDLA EGHIAAMKAK GGVAGVHLFN LGSGRAYSVL EIIRAFEAAS GLHIPYRIQP RRAGDLACSY ADPSHTKQQT GWETKRGLQQ MMEDSWRWVS RNPGRYGD // ID Q5F668_NEIG1 Unreviewed; 351 AA. AC Q5F668; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 67. 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 ORFNames=NGO_1695 {ECO:0000313|EMBL:AAW90319.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90319.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90319.1; -; Genomic_DNA. DR RefSeq; WP_003689853.1; NC_002946.2. DR RefSeq; YP_208731.1; NC_002946.2. DR ProteinModelPortal; Q5F668; -. DR SMR; Q5F668; 4-346. DR EnsemblBacteria; AAW90319; AAW90319; NGO_1695. DR GeneID; 3281208; -. DR KEGG; ngo:NGO1695; -. DR PATRIC; 20336954; VBINeiGon24812_2021. DR HOGENOM; HOG000220501; -. DR KO; K01626; -. DR OMA; DGCIDWA; -. DR OrthoDB; EOG63JR9W; -. DR BioCyc; NGON242231:GI2G-1589-MONOMER; -. DR UniPathway; UPA00053; UER00084. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC. 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361}; KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR001361, KW ECO:0000256|SAAS:SAAS00456513}. FT DOMAIN 43 336 DAHP_synth_1. {ECO:0000259|Pfam:PF00793}. SQ SEQUENCE 351 AA; 38655 MW; 022BA6594232719F CRC64; MTHHYPTDDI KIKEVKELLP PIAHLYELPI SKEASGLVHR TRQEISDLVH GRDRRLLVII GPCSIHDPKA ALEYAERLLK LRKRYENELL IVMRVYFEKP RTTVGWKGLI NDPHLDGTFD INFGLRQARS LLLSLNNMGM PASTEFLDMI TPQYYADLIS WGAIGARTTE SQVHRELASG LSCPVGFKNG TDGNLKIAID AIGAASHSHH FLSVTKAGHS AIVHTGGNPD CHVILRGGKE PNYDAGHVSE AVEQLRAAGV TDKLMIDCSH ANSRKDYTRQ MEVAQDIADQ LEQDGGNIMG VMVESHLVEG RQDKPEVYGK SITDACIGWG ATEELLALLA GANTKRMARA G // ID Q5F6V9_NEIG1 Unreviewed; 204 AA. AC Q5F6V9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 49. DE SubName: Full=Cadmium transporter {ECO:0000313|EMBL:AAW90078.2}; GN ORFNames=NGO_1435 {ECO:0000313|EMBL:AAW90078.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90078.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90078.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90078; AAW90078; NGO_1435. DR PATRIC; 20336289; VBINeiGon24812_1693. DR HOGENOM; HOG000099674; -. DR OMA; ANTRKEY; -. DR OrthoDB; EOG6RG02S; -. DR BioCyc; NGON242231:GI2G-1343-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 62 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 68 87 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 108 134 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 140 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 174 192 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 204 AA; 22639 MW; 842034D2AB719EDE CRC64; MFSTVITAAV LYIATAVDLL VILLIFFARA NTRKEYRDIY IGQYLGSVIL ILVSLFLAFV LNYVPEKWVL GLLGLIPIYL GIKVAIYDDC EGEKRAKKEL DEKGLSKLVG IVALVTVASC GADNIGLFVP YFVTLDLVDL LVTLLVFLIL IFVLVYTAQR LANISGVGEI VEKFSRWIMA VIYIGLGLFI IIENNTIRTI ISII // ID Q5F9Q6_NEIG1 Unreviewed; 222 AA. AC Q5F9Q6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89081.1}; GN ORFNames=NGO_0336 {ECO:0000313|EMBL:AAW89081.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89081.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89081.1; -; Genomic_DNA. DR RefSeq; WP_003687733.1; NC_002946.2. DR RefSeq; YP_207493.1; NC_002946.2. DR EnsemblBacteria; AAW89081; AAW89081; NGO_0336. DR GeneID; 3281777; -. DR KEGG; ngo:NGO0336; -. DR PATRIC; 20333663; VBINeiGon24812_0409. DR HOGENOM; HOG000277976; -. DR KO; K09792; -. DR OMA; QHWLMGH; -. DR OrthoDB; EOG6DNT6V; -. DR BioCyc; NGON242231:GI2G-316-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 84 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 128 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 222 AA; 24150 MW; CA378DC282F4AC88 CRC64; MNHDITFLTL FLLGFFGGTH CIGMCGGLSS AFALQLPPHI NRFWLILLLN TGRISSYTAI GLMLGLIGQL GISLDQTRVL QNILYTASNL LLLFLGLYLS GISSLAAKIE KIGKPIWRNL NPILNRLLPI KSIPACLAVG ILWGWLPCGL VYSASLYALG SGSATTGGLY MLAFALGTLP NLLAIGIFSL QLKKIMQNRY IRLCTGLSVS LWALWKLAVL WL // ID Q5F8F3_NEIG1 Unreviewed; 65 AA. AC Q5F8F3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89534.1}; GN ORFNames=NGO_0823 {ECO:0000313|EMBL:AAW89534.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89534.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89534.1; -; Genomic_DNA. DR RefSeq; WP_003688584.1; NC_002946.2. DR RefSeq; YP_207946.1; NC_002946.2. DR ProteinModelPortal; Q5F8F3; -. DR SMR; Q5F8F3; 1-64. DR EnsemblBacteria; AAW89534; AAW89534; NGO_0823. DR GeneID; 3282209; -. DR KEGG; ngo:NGO0823; -. DR PATRIC; 20334800; VBINeiGon24812_0970. DR HOGENOM; HOG000262066; -. DR OMA; AIQQAWI; -. DR OrthoDB; EOG6ZD6DN; -. DR BioCyc; NGON242231:GI2G-776-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7633 MW; 91A91AAD85258181 CRC64; MKWTDTRRIA EELYDLHGEA IDPKTVRFTQ LRDLIMALPE FDDDPARCGE RILEAVQQAW IDEAE // ID Q5F526_NEIG1 Unreviewed; 507 AA. AC Q5F526; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90711.2}; GN ORFNames=NGO_2111 {ECO:0000313|EMBL:AAW90711.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90711.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90711.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90711; AAW90711; NGO_2111. DR PATRIC; 20338063; VBINeiGon24812_2554. DR HOGENOM; HOG000218740; -. DR OMA; YAIEGHH; -. DR OrthoDB; EOG6R2GVK; -. DR BioCyc; NGON242231:GI2G-2005-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007655; DUF560. DR Pfam; PF04575; DUF560; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 507 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364409. SQ SEQUENCE 507 AA; 55500 MW; 90D2BC029E2A6020 CRC64; MYRVCRLCAA LCVWGAVGAY AAGLPDVRDD AAALRAQRAA AEGWAGMPPE GDSAANGGSR VIDGDFLLSR PQLLEHVLRD ALNGNQADLI ASLADLYAKL PDYDAVLYGR ARALLAKLAG RPAEAVARYR ALHRDNAADE RVLLDLAAAE FDDFRLKSAG LHFAEAAKLD LPAPVLENVG RFRKKTEGLT GWHFSGGISP SVNKNANNAA PQYCLQGGGS RICSVTGPVR AAGLDYEAGA EKLTALADNH YLLFRANVGG TSYYFSRKSA YDDAFGRAYL GWQYKNARQT VGVLPFYQAQ LSGSDGFDAK TKPPADRRLA PYMLAHGAGV QLAHSYRLSR RSQLSVSLER YRQRYREQGR AERNDGWQDG LYVSLARRLG GSATVFGGWQ FARFVPKRET VGGAVNNAAY RRNAVHIGWA QEWGGTGGLN SRIAASYAHR NYKGIAAFST EAQRNREWNV SLALSHDKLS YKGIVPTLNY RFGKTESNVP YAKRRNSEVF VSADWRF // ID Q5F751_NEIG1 Unreviewed; 332 AA. AC Q5F751; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 73. DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:AAW89986.1}; DE EC=1.1.1.28 {ECO:0000313|EMBL:AAW89986.1}; GN ORFNames=NGO_1336 {ECO:0000313|EMBL:AAW89986.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89986.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89986.1; -; Genomic_DNA. DR RefSeq; WP_003691673.1; NC_002946.2. DR RefSeq; YP_208398.1; NC_002946.2. DR ProteinModelPortal; Q5F751; -. DR EnsemblBacteria; AAW89986; AAW89986; NGO_1336. DR GeneID; 3282039; -. DR KEGG; ngo:NGO1336; -. DR PATRIC; 20336041; VBINeiGon24812_1570. DR HOGENOM; HOG000136695; -. DR KO; K03778; -. DR OMA; VIVTAHQ; -. DR OrthoDB; EOG61VZ8G; -. DR BioCyc; NGON242231:GI2G-1250-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003720, KW ECO:0000313|EMBL:AAW89986.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 36634 MW; 45727B4AC7264FC4 CRC64; MKIAIYGTKS YDREHFTRAN RHFGFELEFF DFMLDAKTAK MAEGAEAACI FVNDDASRPV LEKLAQIGVK TVALRCAGFN NVDLKAAEEL GLKVVRVPAY SPESVAEHTV GLMLTLNRRI HKAYQRTRDA NFSLEGLTGF NMYGKTAGVI GTGKIGIATM RILKGFGMNL LAYDPFCNPE VEKLGGRYVD LDELYARSDI ITLHCPATPE NHYMLNEAAF DKMKDGVMII NTSRGGLIDS AAAIEALKCR KIGALGMDVY ENERELFFED KSNDVITDDV FRRLSSCHNV LFTGHQAFLT EEALGNISEV TLSNIREVGQ TGDCGNAVRA DG // ID Q5F5I2_NEIG1 Unreviewed; 70 AA. AC Q5F5I2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90555.2}; GN ORFNames=NGO_1943 {ECO:0000313|EMBL:AAW90555.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90555.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90555.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90555; AAW90555; NGO_1943. DR PATRIC; 20337631; VBINeiGon24812_2342. DR HOGENOM; HOG000027918; -. DR OMA; KPEVNVM; -. DR OrthoDB; EOG63VC55; -. DR BioCyc; NGON242231:GI2G-1845-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR027383; Znf_put. DR Pfam; PF13490; zf-HC2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 15 49 zf-HC2. {ECO:0000259|Pfam:PF13490}. SQ SEQUENCE 70 AA; 8268 MW; 01BA08103D55647C CRC64; MVQPRKPEVN VMKKCRDIAL LLSKHQDRET TPGEKISIYM HLLFCPHCRE YKRQLQTIKI SLAKTTRTSK // ID Q5F873_NEIG1 Unreviewed; 427 AA. AC Q5F873; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369}; GN Name=gltA {ECO:0000313|EMBL:AAW89614.1}; GN ORFNames=NGO_0918 {ECO:0000313|EMBL:AAW89614.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89614.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89614.1; -; Genomic_DNA. DR RefSeq; WP_003688402.1; NC_002946.2. DR RefSeq; YP_208026.1; NC_002946.2. DR ProteinModelPortal; Q5F873; -. DR SMR; Q5F873; 6-421. DR EnsemblBacteria; AAW89614; AAW89614; NGO_0918. DR GeneID; 3281236; -. DR KEGG; ngo:NGO0918; -. DR PATRIC; 20335019; VBINeiGon24812_1079. DR HOGENOM; HOG000021224; -. DR KO; K01647; -. DR OMA; NKEDGVR; -. DR OrthoDB; EOG6P8TP4; -. DR BioCyc; NGON242231:GI2G-856-MONOMER; -. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000000535; 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:AAW89614.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89614.1}; 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; A9B577F228559BD7 CRC64; MSKSIKLNVP GRAGLELPVL EASIGHDVVD IRGLTKNTGL FAFDPGFVST ASCESKITYI DGDQGLLYYR GYPIEQLAEK SDYLEVCYLL IYGELPTPEQ KAEFDNTVRR HTMVHEQLTW FFRGFRRDAH PMAMMVGVVG ALSAFYQDSL DITNPEHRKI 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 YVPAGER // ID Q5F5I9_NEIG1 Unreviewed; 249 AA. AC Q5F5I9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=EtfB protein {ECO:0000313|EMBL:AAW90548.1}; GN ORFNames=NGO_1935 {ECO:0000313|EMBL:AAW90548.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90548.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90548.1; -; Genomic_DNA. DR RefSeq; WP_010951372.1; NC_002946.2. DR RefSeq; YP_208960.1; NC_002946.2. DR ProteinModelPortal; Q5F5I9; -. DR SMR; Q5F5I9; 1-242. DR EnsemblBacteria; AAW90548; AAW90548; NGO_1935. DR GeneID; 3282684; -. DR KEGG; ngo:NGO1935; -. DR PATRIC; 20337610; VBINeiGon24812_2332. DR HOGENOM; HOG000247877; -. DR KO; K03521; -. DR OMA; KGQDKAY; -. DR OrthoDB; EOG65TRQZ; -. DR BioCyc; NGON242231:GI2G-1838-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 23 211 ETF. {ECO:0000259|SMART:SM00893}. SQ SEQUENCE 249 AA; 26988 MW; 9131C6D14B956C66 CRC64; MKALVAVKRV VDYNVKVRVK ADGSDVDIGN VKMSMNPFDE IAVEEAVRLK EAGKVSEIVA VSLGEKKCEE TLRTALAMGA DRAIHIETDV KLEPLAVAKL LKAVADKENP QIFFLGKQAI DDDANQVAQM LAALLNAAQG TFVSKVQIEG DEVQIVREID GGEETIALKL PAVISADLRL NEPRFVKLPN IMVAKKKPLE KLDSADLATD ISPRLKTVKF AEPKARQAGV KVASVAELVE KLKNEAKVI // ID Q5F992_NEIG1 Unreviewed; 284 AA. AC Q5F992; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89245.1}; GN ORFNames=NGO_0507 {ECO:0000313|EMBL:AAW89245.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89245.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89245.1; -; Genomic_DNA. DR RefSeq; WP_010951065.1; NC_002946.2. DR RefSeq; YP_207657.1; NC_002946.2. DR EnsemblBacteria; AAW89245; AAW89245; NGO_0507. DR GeneID; 3282942; -. DR KEGG; ngo:NGO0507; -. DR PATRIC; 20334056; VBINeiGon24812_0600. DR HOGENOM; HOG000057732; -. DR OMA; YGAHELV; -. DR OrthoDB; EOG69KTSR; -. DR BioCyc; NGON242231:GI2G-485-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011928; Phage_phiJL001_Gp84. DR InterPro; IPR018964; Phage_phiJL001_Gp84_C. DR InterPro; IPR019228; Phage_phiJL001_Gp84_N. DR Pfam; PF09931; DUF2163; 1. DR Pfam; PF09356; Phage_BR0599; 1. DR TIGRFAMs; TIGR02218; phg_TIGR02218; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 174 DUF2163. {ECO:0000259|Pfam:PF09931}. FT DOMAIN 203 281 Phage_BR0599. {ECO:0000259|Pfam:PF09356}. SQ SEQUENCE 284 AA; 30789 MW; 7C377DADD041CD69 CRC64; MKAATKELIG LLHGGDEFQM ADLYTITLSG GRVLRHTGAD MPVVWDGQAY GAHELVIKRG ATRTAVGLEV DSNTLQISAA PDYRLEGLQW AEAALGGVLD GARVKIDRVF FDAGLRPVGA VNIFSGRVSD VSGGRSSVKV DVKSDIELLN VSSPRNIYQA GCMRTLYDDG CKVNREKFTV NGRVTENSRT GTVLKHNLTQ PDGWFSQGVI KFAGGRNAGL SRTVKAHGGN TFELALRLPY PPQAGDAFKV YPGCDKRRDT CKDKFDNIVH FRGFPFIPSA DTVV // ID Q5F6N4_NEIG1 Unreviewed; 290 AA. AC Q5F6N4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW90153.1}; GN ORFNames=NGO_1515 {ECO:0000313|EMBL:AAW90153.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90153.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90153.1; -; Genomic_DNA. DR RefSeq; WP_003695549.1; NC_002946.2. DR RefSeq; YP_208565.1; NC_002946.2. DR ProteinModelPortal; Q5F6N4; -. DR EnsemblBacteria; AAW90153; AAW90153; NGO_1515. DR GeneID; 3281521; -. DR KEGG; ngo:NGO1515; -. DR PATRIC; 20336512; VBINeiGon24812_1804. DR HOGENOM; HOG000043493; -. DR KO; K00210; -. DR OMA; MWRDICL; -. DR OrthoDB; EOG6B8XMB; -. DR BioCyc; NGON242231:GI2G-1419-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 290 Prephenate/arogenate dehydrogenase. FT {ECO:0000259|PROSITE:PS51176}. SQ SEQUENCE 290 AA; 31585 MW; C858A848A83F9348 CRC64; MPILNHIALI GVGLIGGSFV LDLKRQGLVR TVTGIDTDRD NLERALERGV IDRASVVIDA DSIGGADLVL IATPVATVPA VLTALRPVLP EHTWISDVGS TKSSVIEAFR RCLPGRLHRC IAAHPIAGSD RNGAQAAQFG LFRHRKLIIT PHGGEDSDGI ALVENLWRAV GADIFTMDAQ HHDAVFAAVS HMPHLTAFAY VHQILDHPDG QEYLKFAATG FRDFTRIASG HPAVWADICL ANKDSLLQLV QGLGKQLDVL ADILTADDRE ALYRYFEEAK TTRDRWLDGN // ID Q5F5F2_NEIG1 Unreviewed; 77 AA. AC Q5F5F2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90585.1}; GN ORFNames=NGO_1976 {ECO:0000313|EMBL:AAW90585.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90585.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90585.1; -; Genomic_DNA. DR RefSeq; WP_003686864.1; NC_002946.2. DR RefSeq; YP_208997.1; NC_002946.2. DR EnsemblBacteria; AAW90585; AAW90585; NGO_1976. DR GeneID; 3282647; -. DR KEGG; ngo:NGO1976; -. DR PATRIC; 20337717; VBINeiGon24812_2385. DR HOGENOM; HOG000218709; -. DR OrthoDB; EOG6JDWJK; -. DR BioCyc; NGON242231:GI2G-1875-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 47 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 77 AA; 8855 MW; 569D4EC820AC7249 CRC64; MWHIVAIGYL FVAVMYSAAQ PSIARALIYL VFWVVLPTVF TVFAVTVRRR NRLMGQQEQA ESEQQRAQRQ KDSGTKP // ID Q5F705_NEIG1 Unreviewed; 151 AA. AC Q5F705; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90032.2}; GN ORFNames=NGO_1384 {ECO:0000313|EMBL:AAW90032.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90032.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90032.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90032; AAW90032; NGO_1384. DR PATRIC; 20336157; VBINeiGon24812_1627. DR HOGENOM; HOG000219104; -. DR OMA; KEKSMVD; -. DR OrthoDB; EOG690MM7; -. DR BioCyc; NGON242231:GI2G-1297-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 151 AA; 17574 MW; 25ADFF93102C760E CRC64; MVDAVVKTPE FLPFTSVGIF RFGADITQYK NILETFMYEP PDEFGTEYYE SPDSNLLISV EKNKIISIFC YQELYFMGVN IIGLNFEDFK QLFHHPKSYG VDKYYLSNES YPTYVYEFDE IGVQAWEAKG KIVTIIAGGK DNYSTEPYYD E // ID Q5F8G5_NEIG1 Unreviewed; 100 AA. AC Q5F8G5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89522.1}; GN ORFNames=NGO_0810 {ECO:0000313|EMBL:AAW89522.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89522.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89522.1; -; Genomic_DNA. DR RefSeq; WP_010951129.1; NC_002946.2. DR RefSeq; YP_207934.1; NC_002946.2. DR EnsemblBacteria; AAW89522; AAW89522; NGO_0810. DR GeneID; 3281846; -. DR KEGG; ngo:NGO0810; -. DR PATRIC; 20334778; VBINeiGon24812_0959. DR HOGENOM; HOG000071285; -. DR OMA; RILPERN; -. DR OrthoDB; EOG62K24V; -. DR BioCyc; NGON242231:GI2G-764-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 100 AA; 10969 MW; 02A4A471DD2CFC3A CRC64; MIINKFTWAM AVFSAILALV IGSGFTALEY VKEPPAAPYA VSAPKTAGVK PRRILPERNP PCCRLTVQTP RPFQTPAMRT DRIRLTERQQ IPFPSSGSAA // ID Q5F7H9_NEIG1 Unreviewed; 524 AA. AC Q5F7H9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 61. DE SubName: Full=Protein DcaA {ECO:0000313|EMBL:AAW89858.1}; GN ORFNames=NGO_1198 {ECO:0000313|EMBL:AAW89858.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89858.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89858.1; -; Genomic_DNA. DR RefSeq; WP_003706709.1; NC_002946.2. DR RefSeq; YP_208270.1; NC_002946.2. DR ProteinModelPortal; Q5F7H9; -. DR EnsemblBacteria; AAW89858; AAW89858; NGO_1198. DR GeneID; 3281951; -. DR KEGG; ngo:NGO1198; -. DR PATRIC; 20335695; VBINeiGon24812_1406. DR HOGENOM; HOG000218728; -. DR OMA; WLMLKEI; -. DR OrthoDB; EOG6B35XZ; -. DR BioCyc; NGON242231:GI2G-1110-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 53 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 110 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 154 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 213 464 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 524 AA; 59048 MW; D567F41685B1210D CRC64; MKKSLFVLFL YSSLLTASEI AYRFVFGIET LPAAKMAETF ALTFMIAALY LFARYKASRL LIAVFFAFSM IANNVHYAVY QSWMTGINYW LMLKEVTEVG SAGASMLDKL WLPALWGVAE VMLFCSLAKF RRKTHFSADI LFAFLMLMIF VRSFDTKQEH GISPKPTYSR IKANYFSFGY FVGRVLPYQL FDLSKIPVFK QPAPSKIGQG SIQNIVLIMG ESESAAHLKL FGYGRETSPF LTRLSQADFK PIVKQSYSAG FMTAVSLPSF FNVIPHANGL EQISGGDTNM FRLAKEQGYE TYFYSAQAEN QMAILNLIGK KWIDHLIQPT QLGYGNGDNM PDEKLLPLFD KINLQQGRHF IVLHQRGSHA PYGALLQPQD KVFGEADIVD KYDNTIHKTD QMIQTVFEQL QKQPDGNWLF AYTSDHGQYV RQDIYNQGTV QPDSYIVPLV LYSPDKAVQQ AANQAFAPCE IAFHQQLSTF LIHTLGYDMP VSGCREGSVT GNLITGDAGS LNIRNGKAEY VYPQ // ID Q5F6K5_NEIG1 Unreviewed; 406 AA. AC Q5F6K5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 58. DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase family protein {ECO:0000313|EMBL:AAW90182.2}; GN ORFNames=NGO_1546 {ECO:0000313|EMBL:AAW90182.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90182.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90182.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6K5; -. DR EnsemblBacteria; AAW90182; AAW90182; NGO_1546. DR PATRIC; 20336590; VBINeiGon24812_1843. DR HOGENOM; HOG000265464; -. DR OMA; QHEMGEL; -. DR OrthoDB; EOG6716MX; -. DR BioCyc; NGON242231:GI2G-1448-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Methyltransferase {ECO:0000313|EMBL:AAW90182.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90182.2}. SQ SEQUENCE 406 AA; 44745 MW; D52EAD21DD79E1B1 CRC64; MSGNPINLHK LTFIMLLPSP EARQSSLNLQ TLIAEEIGKH GNWIPFSRFM ELVLYAPQYG YYTGGSHKIG NTGDFITAPT LTPLFAQTLA RQLQELLPQT AGNIYEFGAG TGQLAADLLG SVSDSINCYY IIEISPELAA RQKNLIQARA PEASQKVVHL TALPEAFDGI IIGNELLDAI PVEIVRKNEG GLLEHIGVCT DNGRFAYSAR PLHDPSLSTS ASLYFPQTDY PYTSELHPQQ YAFIRTLASR LERGGMIFID YGFDAAQYYH PQRNQGTLIG HYRHHVIHNP FDFIGLADLT AHVNFTDIAQ AGTDAGLDLT GYLPQSHFLL NLGITELLAQ TGKTDSAAYI REAAAVQKLI DQHEMGELFK VIAFGKNIGI DWAGFRFGDI CHKLQPSCRL NPLQTA // ID Q5F961_NEIG1 Unreviewed; 158 AA. AC Q5F961; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Cation uptake regulator {ECO:0000313|EMBL:AAW89276.1}; GN ORFNames=NGO_0542 {ECO:0000313|EMBL:AAW89276.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89276.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89276.1; -; Genomic_DNA. DR RefSeq; WP_010357704.1; NC_002946.2. DR RefSeq; YP_207688.1; NC_002946.2. DR ProteinModelPortal; Q5F961; -. DR EnsemblBacteria; AAW89276; AAW89276; NGO_0542. DR GeneID; 3282910; -. DR KEGG; ngo:NGO0542; -. DR PATRIC; 20334134; VBINeiGon24812_0639. DR HOGENOM; HOG000014146; -. DR KO; K09823; -. DR OMA; DHSHCVH; -. DR OrthoDB; EOG6N6839; -. DR BioCyc; NGON242231:GI2G-516-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 158 AA; 17576 MW; 32F3D70E32756E46 CRC64; MKTNFKQKII EQARREDLQV TALREQVLDI VLQQSGVIKA YNVLSQMQQQ SEGVLAPPTA YRALDFWADQ GVLHKVAAVN GYILCSHAQH ECNDHCHDHE EAEAHHSAFI LVCTECGAAD EQTLSHEWAA LRAGVAESGF ALKEEHVVLT GICKKCQK // ID Q5FAK0_NEIG1 Unreviewed; 103 AA. AC Q5FAK0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=DNA-binding protein {ECO:0000313|EMBL:AAW88783.1}; GN ORFNames=NGO_0011 {ECO:0000313|EMBL:AAW88783.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88783.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88783.1; -; Genomic_DNA. DR RefSeq; WP_003700847.1; NC_002946.2. DR RefSeq; YP_207195.1; NC_002946.2. DR ProteinModelPortal; Q5FAK0; -. DR EnsemblBacteria; AAW88783; AAW88783; NGO_0011. DR GeneID; 3283058; -. DR KEGG; ngo:NGO0011; -. DR PATRIC; 20332854; VBINeiGon24812_0013. DR HOGENOM; HOG000265487; -. DR KO; K07726; -. DR OMA; ETMRNFD; -. DR OrthoDB; EOG6ZPSZQ; -. DR BioCyc; NGON242231:GI2G-10-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000313|EMBL:AAW88783.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 48 102 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 103 AA; 11139 MW; 0E4A4377BA656A4C CRC64; MKYKSGIFAA IHETMQGLHD IGAIDKKTMR GFDKSCLTEI KPLSGGDIKA IREKEALSQA AFAIYLNVGK NHVSAWERGV KKPSGAALKL LTIVKNKGIE AIA // ID Q5F5F7_NEIG1 Unreviewed; 498 AA. AC Q5F5F7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Septum formation inhibitor Maf {ECO:0000313|EMBL:AAW90580.1}; GN ORFNames=NGO_1971 {ECO:0000313|EMBL:AAW90580.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90580.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90580.1; -; Genomic_DNA. DR RefSeq; WP_010951374.1; NC_002946.2. DR RefSeq; YP_208992.1; NC_002946.2. DR EnsemblBacteria; AAW90580; AAW90580; NGO_1971. DR GeneID; 3282652; -. DR KEGG; ngo:NGO1971; -. DR PATRIC; 20337707; VBINeiGon24812_2380. DR HOGENOM; HOG000218708; -. DR OMA; VRYDINI; -. DR OrthoDB; EOG6FFS2K; -. DR BioCyc; NGON242231:GI2G-1870-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 498 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256572. SQ SEQUENCE 498 AA; 53927 MW; 7BAB8FADDF192F30 CRC64; MNLPIQKFMM LFAAAISLLQ IPISHANGLD ARLRDDMQAK HYEPGGKYHL FGNARGSVKN RVCAVQTFDA TAVGPILPIT HERTGFEGVI GYETHFSGHG HEVHSPFDNH DSKSTSDFSG GVDGGFTVYQ LHRTGSEIHP ADGYDGPQGG GYPEPQGARD IYSYHIKGTS TKTKINTVPQ APFSDRWLKE NAGAASGFLS RADEAGKLIW ENDPDKNWRA NRMDDIRGIV QGAVNPFLTG FQGVGIGAIT DSAVSPVTDT AAQQTLQGIN DLGNLSPEAQ LAAASLLQDS AFAVKDGINS ARQWADAHPN ITATAQTALA VAEAAGTVWR GKKVELNPTK WDWVKNTGYK KPAARHMQTV DGEMAGGNRP PKSITSEGKA NAATYPKLVN QLNEQNLNNI AAQDPRLSLA IHEGKKNFPI GTATYEEADR LGKIWVGEGA RQTSGGGWLS RDGTRQYRPP TEKKSQFATT GIQANFETYT IDSNEKRNKI KNGHLNIR // ID Q5F8C1_NEIG1 Unreviewed; 80 AA. AC Q5F8C1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89566.1}; GN ORFNames=NGO_0865 {ECO:0000313|EMBL:AAW89566.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89566.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89566.1; -; Genomic_DNA. DR RefSeq; WP_003704095.1; NC_002946.2. DR RefSeq; YP_207978.1; NC_002946.2. DR EnsemblBacteria; AAW89566; AAW89566; NGO_0865. DR GeneID; 3282878; -. DR KEGG; ngo:NGO0865; -. DR PATRIC; 20334902; VBINeiGon24812_1021. DR HOGENOM; HOG000027803; -. DR OMA; NLPFNVL; -. DR OrthoDB; EOG66B43D; -. DR BioCyc; NGON242231:GI2G-808-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 8911 MW; F7BE6788C62C63CC CRC64; MAGQEELSWQ VVYQRVMADK DVVGAGYLID FAQTAENLPF DVLPLISLVL NKGDETLKTG MLNKLPDNAK ENLRIMGYLP // ID Q5F7V6_NEIG1 Unreviewed; 477 AA. AC Q5F7V6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 70. DE SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AAW89731.1}; DE EC=1.2.1.16 {ECO:0000313|EMBL:AAW89731.1}; GN Name=gabD {ECO:0000313|EMBL:AAW89731.1}; GN ORFNames=NGO_1061 {ECO:0000313|EMBL:AAW89731.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89731.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89731.1; -; Genomic_DNA. DR RefSeq; WP_003693417.1; NC_002946.2. DR RefSeq; YP_208143.1; NC_002946.2. DR ProteinModelPortal; Q5F7V6; -. DR EnsemblBacteria; AAW89731; AAW89731; NGO_1061. DR GeneID; 3281280; -. DR KEGG; ngo:NGO1061; -. DR PATRIC; 20335356; VBINeiGon24812_1244. DR HOGENOM; HOG000271509; -. DR KO; K00135; -. DR OMA; PVAKMLY; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NGON242231:GI2G-976-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003344, KW ECO:0000313|EMBL:AAW89731.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 22 470 Aldedh. {ECO:0000259|Pfam:PF00171}. SQ SEQUENCE 477 AA; 51010 MW; 52B6C6AA59ACD189 CRC64; MNEYSQLIKH PDISLSPISD GIGVGNPATG EILAYVRNTG SDKLKNLIQK AAAAQKLWAA KTALERADIL WRWYFLVKEN KEALARLMTM EQGKSLTEAR GEIDYAASFV RWFAEEARRI DGDVLTSVKA SQKLVVLKQP VGVTAAITPW NFPSAMIARK AAPALAVGCA MIVKPASLTP LSAYALAVLA YEAGVPQDLL PVVSGRASEI SHEFATNPTV RKISFTGSTE VGAKIFAGSA ADIKKLSLEL GGNAPFIVFD DADLDKAVEG ALASKFRNSG QTCVCTNRVY VQSGIYDVFC RKLSEKAAAL KLGDGLDEGV NQGPLIEEKA VEKVEQHIAD ALSKGAVCLT GGKRSALGGT FFEPTVLSGV TAQMAVAREE TFGPLCPVFR FETEAEVIEA ANNTEYGLAA YLFTSDTARQ WRVGEVLEYG MVGINTGLIS NEAAPFGGVK RSGLGREGSK YGADEYLELK YLCIDAG // ID Q5F8A4_NEIG1 Unreviewed; 135 AA. AC Q5F8A4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89583.1}; GN ORFNames=NGO_0884 {ECO:0000313|EMBL:AAW89583.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89583.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89583.1; -; Genomic_DNA. DR RefSeq; WP_010951142.1; NC_002946.2. DR RefSeq; YP_207995.1; NC_002946.2. DR EnsemblBacteria; AAW89583; AAW89583; NGO_0884. DR GeneID; 3281475; -. DR KEGG; ngo:NGO0884; -. DR PATRIC; 20334943; VBINeiGon24812_1041. DR OrthoDB; EOG6KQ6GP; -. DR BioCyc; NGON242231:GI2G-825-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 135 AA; 15351 MW; 9178175441FAF9AC CRC64; MPPNRIGKNR LDMSGGIRMP VCMKSPNILI VRQPPFAMRP NRCGWRAKKT AAYKGQDPAK VTHYLTRPAG FSDCQRVCPD ETGFDRRLFR PYARSLKGQM AKARISGKRY RRLSAEHAEG FSKGCGCRYI TKSNR // ID Q5F9I1_NEIG1 Unreviewed; 237 AA. AC Q5F9I1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89156.1}; GN ORFNames=NGO_0413 {ECO:0000313|EMBL:AAW89156.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89156.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89156.1; -; Genomic_DNA. DR RefSeq; WP_003706625.1; NC_002946.2. DR RefSeq; YP_207568.1; NC_002946.2. DR EnsemblBacteria; AAW89156; AAW89156; NGO_0413. DR GeneID; 3283003; -. DR KEGG; ngo:NGO0413; -. DR PATRIC; 20333837; VBINeiGon24812_0496. DR HOGENOM; HOG000218871; -. DR OMA; QTITRKH; -. DR OrthoDB; EOG6H1PZZ; -. DR BioCyc; NGON242231:GI2G-391-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 237 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256082. FT TRANSMEM 212 232 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 237 AA; 26080 MW; D70F844EFA0FCF76 CRC64; MLFRKTTAAV LAATLILNGC TMMLRGMNNP VSQTITRKHV DKDQIRAFGV VAEDNAQLEK GSLVMMGGKY WFAVNPEDSA KLTGLLKAGL DKPFQIVEDT PSYARHQALP VKFEAPGSQN FSTGGLCLRY DTGRPDDIAK LKQLEFKAVK LDNRTIYTRC VSAKGKYYAT PQKLNADYHF EQSVPADIYY TVTEKHTDKS KLFGNILYTP PLLILDAAAA VLVLPMALIA AANSSDK // ID Q5F696_NEIG1 Unreviewed; 261 AA. AC Q5F696; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 81. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|PIRNR:PIRNR000094}; DE EC=1.3.1.9 {ECO:0000256|PIRNR:PIRNR000094}; GN ORFNames=NGO_1666 {ECO:0000313|EMBL:AAW90291.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90291.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a CC trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH. CC {ECO:0000256|PIRNR:PIRNR000094}. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|PIRNR:PIRNR000094}. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. FabI subfamily. {ECO:0000256|PIRNR:PIRNR000094}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90291.1; -; Genomic_DNA. DR RefSeq; WP_002223367.1; NC_002946.2. DR RefSeq; YP_208703.1; NC_002946.2. DR ProteinModelPortal; Q5F696; -. DR SMR; Q5F696; 2-258. DR PRIDE; Q5F696; -. DR EnsemblBacteria; AAW90291; AAW90291; NGO_1666. DR GeneID; 3281284; -. DR KEGG; ngo:NGO1666; -. DR PATRIC; 20336882; VBINeiGon24812_1986. DR KO; K00208; -. DR OMA; GILDMIH; -. DR OrthoDB; EOG6HF644; -. DR BioCyc; NGON242231:GI2G-1560-MONOMER; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000094}; KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000094}; KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000094}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000094}; KW NAD {ECO:0000256|PIRNR:PIRNR000094}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000094}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT ACT_SITE 147 147 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000094-1}. FT ACT_SITE 157 157 Proton acceptor. FT {ECO:0000256|PIRSR:PIRSR000094-1}. FT BINDING 95 95 Substrate; via amide nitrogen and FT carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR000094-2}. 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 Q5F5B3_NEIG1 Unreviewed; 462 AA. AC Q5F5B3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 61. DE SubName: Full=Sodium:proton antiporter {ECO:0000313|EMBL:AAW90624.1}; GN ORFNames=NGO_2016 {ECO:0000313|EMBL:AAW90624.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90624.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90624.1; -; Genomic_DNA. DR RefSeq; WP_003686927.1; NC_002946.2. DR RefSeq; YP_209036.1; NC_002946.2. DR EnsemblBacteria; AAW90624; AAW90624; NGO_2016. DR GeneID; 3282696; -. DR KEGG; ngo:NGO2016; -. DR PATRIC; 20337815; VBINeiGon24812_2431. DR HOGENOM; HOG000279369; -. DR KO; K07084; -. DR OMA; NHIYDTC; -. DR OrthoDB; EOG6D5G41; -. DR BioCyc; NGON242231:GI2G-1917-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 109 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 153 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; 48067 MW; 993E23C4CF3D99B3 CRC64; MNAVVVAVIV MLVLSLSRVH VVLSLTVGAF VGGAVAGMPL QNIADAAGQV SQAGIIPVFN KGLEGGAKIA LSYAMLGAFA MAITHSGLPQ QLAGAVVRKL NRGGMPDSVR SGEGAVKWLL LSIILVMGIM SQNVIPIHIA FIPMIVPPLL LVFNRLKIDR RLIACVITFG LVTTYMFLPY GFGAIFLNEI LLGNIHSAAP QLDVKNINVM AAMAIPALGM LAGLLLAFVH YRKPRLYQSN NADTAGNADA ANRPQPSAYR SLVAAAAIAV CFAIQLMYED SLVLGAMLGF AVFMMLGVIN RDKANDVFGE GIKMMAMVGF IMIAAQGFAA VMNATGHIQP LVESSMAIFG NSKGMAALAM LVVGLLVTMG IGSSFSTLPI IAAIYVPLCT GLGFSPLATA AIVGTAGALG DAGSPASDST LGPTMGLNAD GRHDHIRDSV IPTFIHYNIP LLIAGWIAAM VL // ID Q5F7J8_NEIG1 Unreviewed; 149 AA. AC Q5F7J8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Pilin {ECO:0000313|EMBL:AAW89839.1}; GN ORFNames=NGO_1177 {ECO:0000313|EMBL:AAW89839.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89839.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89839.1; -; Genomic_DNA. DR RefSeq; WP_002214937.1; NC_002946.2. DR RefSeq; YP_208251.1; NC_002946.2. DR ProteinModelPortal; Q5F7J8; -. DR EnsemblBacteria; AAW89839; AAW89839; NGO_1177. DR GeneID; 3281950; -. DR KEGG; ngo:NGO1177; -. DR PATRIC; 20335637; VBINeiGon24812_1382. DR HOGENOM; HOG000218724; -. DR OrthoDB; EOG6NWBPW; -. DR BioCyc; NGON242231:GI2G-1086-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Methylation {ECO:0000256|RuleBase:RU000388}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F728_NEIG1 Unreviewed; 95 AA. AC Q5F728; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90009.1}; GN ORFNames=NGO_1361 {ECO:0000313|EMBL:AAW90009.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90009.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90009.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90009; AAW90009; NGO_1361. DR PATRIC; 20336107; VBINeiGon24812_1602. DR HOGENOM; HOG000219080; -. DR OMA; FFLALTK; -. DR OrthoDB; EOG6NKR31; -. DR BioCyc; NGON242231:GI2G-1274-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 87 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 95 AA; 10624 MW; CC8C2763B7F6300A CRC64; MQRCFNWFDH YCRRLEKYFR RCSIMETWVQ NYTAIGGSLY LTAAAALLPI VFFFAALTVL KLKGYQAGLI ALAVAVFGFG MPTGMAVSSL SPQPD // ID Q5F5B0_NEIG1 Unreviewed; 256 AA. AC Q5F5B0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Adenylyltransferase {ECO:0000313|EMBL:AAW90627.1}; GN ORFNames=NGO_2019 {ECO:0000313|EMBL:AAW90627.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90627.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90627.1; -; Genomic_DNA. DR RefSeq; WP_010951383.1; NC_002946.2. DR RefSeq; YP_209039.1; NC_002946.2. DR ProteinModelPortal; Q5F5B0; -. DR EnsemblBacteria; AAW90627; AAW90627; NGO_2019. DR GeneID; 3282728; -. DR KEGG; ngo:NGO2019; -. DR PATRIC; 20337819; VBINeiGon24812_2433. DR HOGENOM; HOG000281217; -. DR OMA; EVACATM; -. DR OrthoDB; EOG628F8J; -. DR BioCyc; NGON242231:GI2G-1920-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW90627.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90627.1}. FT DOMAIN 16 249 ThiF. {ECO:0000259|Pfam:PF00899}. SQ SEQUENCE 256 AA; 27075 MW; 7F8DCBDD51F3BBB1 CRC64; MTATEHDNDD ALLLRYSRHI LLDEIGIEGQ QKLSAAHILV VGCGGLGAAA LPYLAASGVG TLTIADSDTV ELHNLQRQVA FDEGDVGKPK AETLAGRLKR INHTVDVRAV NEKLDGCRLT GLVQTADIVL DCCDNYATRQ AVNRACVQTK TPLVSGAAVR FEGQLAAYRP DLPDSPCYAC LFDGGSASDG ICSLFGVLSP LVGIVGCTQA AEALKILLEA GEPSHGRLAV YRALEGGWQY FDLPRNPECP VCGAAR // ID Q5F5A7_NEIG1 Unreviewed; 109 AA. AC Q5F5A7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90630.1}; GN ORFNames=NGO_2022 {ECO:0000313|EMBL:AAW90630.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90630.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90630.1; -; Genomic_DNA. DR RefSeq; WP_003686940.1; NC_002946.2. DR RefSeq; YP_209042.1; NC_002946.2. DR EnsemblBacteria; AAW90630; AAW90630; NGO_2022. DR GeneID; 3282725; -. DR KEGG; ngo:NGO2022; -. DR PATRIC; 20337827; VBINeiGon24812_2437. DR HOGENOM; HOG000218720; -. DR OrthoDB; EOG6GTZMF; -. DR BioCyc; NGON242231:GI2G-1923-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 19 53 {ECO:0000256|SAM:Coils}. FT COILED 59 100 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 109 AA; 12717 MW; DAF529F6CAB81D00 CRC64; MKQNIEKLES SVYTLVQKFE TLVSENRRLK ETVAELERAH ERQKLEHETA VDELSEALLV QVGKLKEDLQ NKIDSLTEEN ARYRALLEQS REKISALAAR LPQRQETQQ // ID Q5F610_NEIG1 Unreviewed; 104 AA. AC Q5F610; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90377.1}; GN ORFNames=NGO_1756 {ECO:0000313|EMBL:AAW90377.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90377.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90377.1; -; Genomic_DNA. DR RefSeq; WP_010951340.1; NC_002946.2. DR RefSeq; YP_208789.1; NC_002946.2. DR EnsemblBacteria; AAW90377; AAW90377; NGO_1756. DR GeneID; 3281377; -. DR KEGG; ngo:NGO1756; -. DR BioCyc; NGON242231:GI2G-1652-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 104 AA; 10860 MW; AEF1607F1D5FA251 CRC64; MSENGKGNFA AAAAVIPANL HSVIPTKVGI RNAKSKETVL SDKFPHRQVW IPAYAGMTAA GIGGFGGVGG FGGLKPALVY RNFRIIATNR PAATRARPRQ TTVA // ID Q5F988_NEIG1 Unreviewed; 101 AA. AC Q5F988; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89249.1}; GN ORFNames=NGO_0511 {ECO:0000313|EMBL:AAW89249.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89249.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89249.1; -; Genomic_DNA. DR RefSeq; WP_003689058.1; NC_002946.2. DR RefSeq; YP_207661.1; NC_002946.2. DR EnsemblBacteria; AAW89249; AAW89249; NGO_0511. DR GeneID; 3282937; -. DR KEGG; ngo:NGO0511; -. DR PATRIC; 20334066; VBINeiGon24812_0605. DR OMA; FQEAVIT; -. DR OrthoDB; EOG6N684F; -. DR BioCyc; NGON242231:GI2G-489-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 101 AA; 11014 MW; A6F329DCAE58DBD5 CRC64; MIEDKKIVAL NFAVEDGMTG ASAAYHVVEH IGADYRNGYV TATLNGYVSE NAFKSGKRYL LARTLDFQET DITAPDPGWV YRKALEGAAG IPKDAQPVYA E // ID Q5F643_NEIG1 Unreviewed; 433 AA. AC Q5F643; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 43. DE SubName: Full=Gliding motility protein {ECO:0000313|EMBL:AAW90344.1}; GN ORFNames=NGO_1723 {ECO:0000313|EMBL:AAW90344.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90344.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90344.1; -; Genomic_DNA. DR RefSeq; WP_010951333.1; NC_002946.2. DR RefSeq; YP_208756.1; NC_002946.2. DR EnsemblBacteria; AAW90344; AAW90344; NGO_1723. DR GeneID; 3281319; -. DR KEGG; ngo:NGO1723; -. DR PATRIC; 20337040; VBINeiGon24812_2060. DR HOGENOM; HOG000071358; -. DR OMA; KPEWLAQ; -. DR OrthoDB; EOG615VF4; -. DR BioCyc; NGON242231:GI2G-1619-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.80.10.10; -; 1. DR InterPro; IPR032675; L_dom-like. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 433 AA; 49188 MW; 409076520190170F CRC64; MYWERGLHMY KASAVVPTGY VRVGNTAPLC GEDTQRYASF WGDGYDVYRQ LRWRQIPEKQ RKAFKKAAKS KNTVMFAGRE YGISKQNLSD VWDDFEDAME LKAFPCLSSL FLTKWHKNLY EYLEEYPFIT RLCLENHGQT VLDFSNTRIT DLSVDMTGVE SLYLNEGLDS LNLKGEIKEN CKVCTAGKGA GLILEVGKSV PKVRGLENLT AVNVMGIADF DMQNLSETYP KLKTIRLWGK PGNIANFSAV SGFEDLEVFT AVDLFGFGAD DIPHPDRLPK LHRLWMSSLP EEAAKAVKKL YKKRKEDGLD PWIEKARKPE WLAQNFDNPF RDWDGAEHIP KSHAKKAAEL YRKTRAGVVK LLGNPPENIG EGLAEAVKAY TGGFNKMDKK HFIDTVERED IAEALETILD LIPDGSCADK EKLFEIFDKN RNF // ID Q5F959_NEIG1 Unreviewed; 185 AA. AC Q5F959; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 87. 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 ORFNames=NGO_0544 {ECO:0000313|EMBL:AAW89278.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89278.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89278.1; -; Genomic_DNA. DR RefSeq; WP_010951078.1; NC_002946.2. DR RefSeq; YP_207690.1; NC_002946.2. DR ProteinModelPortal; Q5F959; -. DR SMR; Q5F959; 23-182. DR EnsemblBacteria; AAW89278; AAW89278; NGO_0544. DR GeneID; 3282908; -. DR KEGG; ngo:NGO0544; -. DR PATRIC; 20334138; VBINeiGon24812_0641. DR HOGENOM; HOG000065978; -. DR KO; K03767; -. DR OMA; NLDYPQP; -. DR OrthoDB; EOG6S26C3; -. DR BioCyc; NGON242231:GI2G-518-MONOMER; -. DR Proteomes; UP000000535; 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; 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; PS50072; CSA_PPIASE_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU363019}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5006528989. FT DOMAIN 29 183 PPIase cyclophilin-type. FT {ECO:0000259|PROSITE:PS50072}. SQ SEQUENCE 185 AA; 20043 MW; ADD330D3466B5522 CRC64; MKPKFKTVLT ALLLAVSLPS MAATRVLMET DMGNIRLVLD ESKASKTVAN FVRYARKGFY DNTIFHRVIG GFVIQGDGLT EDLVQKATDK AVANESGNGL KNTVGTIAMA RTAAPDSAAA QFFINLADNG SLDYKNGQYG YTVFGRVESG MDTVSKIARV KTATRGFYQN VPVQPVKIRR VVVGQ // ID Q5F8W9_NEIG1 Unreviewed; 756 AA. AC Q5F8W9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Restriction endonuclease subunit M {ECO:0000313|EMBL:AAW89368.1}; GN ORFNames=NGO_0641 {ECO:0000313|EMBL:AAW89368.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89368.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89368.1; -; Genomic_DNA. DR RefSeq; WP_010951099.1; NC_002946.2. DR RefSeq; YP_207780.1; NC_002946.2. DR ProteinModelPortal; Q5F8W9; -. DR REBASE; 10855; M.NgoAXII. DR EnsemblBacteria; AAW89368; AAW89368; NGO_0641. DR GeneID; 3281459; -. DR KEGG; ngo:NGO0641; -. DR PATRIC; 20334366; VBINeiGon24812_0755. DR HOGENOM; HOG000220748; -. DR KO; K07316; -. DR OMA; IHSEEFQ; -. DR OrthoDB; EOG65F8SN; -. DR BioCyc; NGON242231:GI2G-608-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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; IPR002295; D21N6_MeTrfase. 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 InterPro; IPR022221; TypeIII_RM_meth. DR Pfam; PF01555; N6_N4_Mtase; 1. DR Pfam; PF12564; TypeIII_RM_meth; 1. DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89368.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89368.1}; KW Nuclease {ECO:0000313|EMBL:AAW89368.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 41 95 TypeIII_RM_meth. FT {ECO:0000259|Pfam:PF12564}. FT DOMAIN 269 612 N6_N4_Mtase. {ECO:0000259|Pfam:PF01555}. SQ SEQUENCE 756 AA; 86038 MW; 1D20FAFD16D7BDF3 CRC64; MKTGIQTELA QALLSHEKIW ANEEKTILAK NILLDLVEKT DPSIIGLLLN NDELKRHFFV EVNGVLVFKL QDFRFFLDKH SINNSYTKYA NRIGLTDGNR FLKDNSDIVL DFPFKDCVLN GGQSTEEGEE IYFKRNNSQP ASQPASQPAS QPASQPASQP ASQPASQPAS QPASQPASQP ASQPASQLYT KLTRKRQEIF FNQTLAFDEI DRLFDAKAFS KFSRHTADGK QPVGEIKRRS DGTPAENLII KGNNLIAMHS LAKQFKGKVK LIYIDPPYNT ETDSFAYNDK FSHSTWLTFM KNRLEIAKEL LKDDGLIFVQ CDDKEQAYLK VLLDETFTRE NFINCIAVKM SEPSGNKMAH TSHRLPKIKE YILIYKNKNI KLNPIREQKS EWDNEYNIFL ENFTQEDKKF IDLIVNSQTE NKEINGNTLK EIDILLKKIS PISVNQKLAQ LNIKDNEVIK WKLDNAYRIV RTAASSSVKK LADEKKEICQ QQFFSVISKR DKLLYIVKSD YSKDAKAPRV QVLFAEDYLS ISLCDLWTNI NTTGLEAEGN VELKNGKKPE SLIETIIKLA TNENDIVLDY HLGSGTTAAV AHKMNRQYIG IEQMDYIETL AVERMKKVID GEQGGISKAV NWQGGGEFVY AELSPFNETA KQQILACENS DGIKTLFEGL CERHFLKYNV SVNEFSQIIE EPEFQSLALD EQKQMMLEML DLNQMYISLS EMDDEQFAGC LNDDDKALSR AFYQSVKHQA EKKDGE // ID Q5F7S9_NEIG1 Unreviewed; 132 AA. AC Q5F7S9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Putative phage associated protein {ECO:0000313|EMBL:AAW89758.1}; GN ORFNames=NGO_1091 {ECO:0000313|EMBL:AAW89758.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89758.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89758.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89758; AAW89758; NGO_1091. DR PATRIC; 20335434; VBINeiGon24812_1283. DR HOGENOM; HOG000071258; -. DR OMA; VIGAFDM; -. DR OrthoDB; EOG6NGW12; -. DR BioCyc; NGON242231:GI2G-1003-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 132 AA; 14296 MW; 49551EFBF9A1FC3E CRC64; MKRQEAAKAH YREIYTAHPD ADSIVESREL EEWLAGQNPL VRKAFNDALK DGTAAEVIGA FDMFKAAKSA AEPEKPAEKP PAGKNTPNTL SDIPAGRDHT ASDGPPDYLS GNALAEKLAS MTEEQVEKFL NS // ID Q5F871_NEIG1 Unreviewed; 235 AA. AC Q5F871; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 79. 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:AAW89616.2}; GN ORFNames=NGO_0920 {ECO:0000313|EMBL:AAW89616.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89616.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89616.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F871; -. DR EnsemblBacteria; AAW89616; AAW89616; NGO_0920. DR PATRIC; 20335023; VBINeiGon24812_1081. DR HOGENOM; HOG000160590; -. DR OMA; DGQYFGP; -. DR OrthoDB; EOG6CK7MG; -. DR BioCyc; NGON242231:GI2G-858-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Iron {ECO:0000256|RuleBase:RU361237}; KW Iron-sulfur {ECO:0000256|RuleBase:RU361237}; KW Metal-binding {ECO:0000256|RuleBase:RU361237}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 27144 MW; 9D0E4D1EDF795D0F CRC64; MEKMSFEIYR YNPDVDAKPY MQRYELELEP TDVKLLDALV RLKAQDDTLS FRRSCREGIC GSDGMNINGK NGLACLTDLR SLKQPVKIRP LPGLPVIRDL IVDMTQFFKQ YHSVKPYVVN DNPIDADKER LQTQEERKEL DGLYECILCA CCSTACPSFW WNPDKFVGPS GLLNAYRFIA DSRDTITNER LDNLNDPYRL FRCHTIMNCV DVCPKHLNPT RAIGKIKEIM LKRVV // ID Q5F5J6_NEIG1 Unreviewed; 163 AA. AC Q5F5J6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AAW90541.1}; GN ORFNames=NGO_1928 {ECO:0000313|EMBL:AAW90541.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90541.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90541.1; -; Genomic_DNA. DR RefSeq; WP_003688081.1; NC_002946.2. DR RefSeq; YP_208953.1; NC_002946.2. DR ProteinModelPortal; Q5F5J6; -. DR EnsemblBacteria; AAW90541; AAW90541; NGO_1928. DR GeneID; 3282691; -. DR KEGG; ngo:NGO1928; -. DR PATRIC; 20337594; VBINeiGon24812_2324. DR HOGENOM; HOG000218687; -. DR OMA; TIWHEVL; -. DR OrthoDB; EOG6GJC0M; -. DR BioCyc; NGON242231:GI2G-1831-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90541.1}. FT DOMAIN 18 161 N-acetyltransferase. FT {ECO:0000259|PROSITE:PS51186}. SQ SEQUENCE 163 AA; 18678 MW; 294E680BFA8E5E9F CRC64; MNSLFVDNTV FITRLKAGHI GRLVQALFEE WHGFEPWSSV DKIRAYYGRC LKDDELPLAF AAVDDSGTLL GSAAVKRHDM ENFPQYEYWL GDVFVLPEYR GKGIGRRLVA HCIGAARSLG IKFLYLYTPD VQIFYESFGW AVVGRHFHNG EWVTVMRLDV DKV // ID Q5F5X6_NEIG1 Unreviewed; 159 AA. AC Q5F5X6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 49. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90411.2}; GN ORFNames=NGO_1792 {ECO:0000313|EMBL:AAW90411.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90411.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90411.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90411; AAW90411; NGO_1792. DR PATRIC; 20337230; VBINeiGon24812_2151. DR HOGENOM; HOG000218657; -. DR OMA; HDAFACA; -. DR OrthoDB; EOG6742XQ; -. DR BioCyc; NGON242231:GI2G-1690-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 59 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 125 141 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 159 AA; 17245 MW; AA4BEAF53F40EAFE CRC64; MFVNEKYPYA TLFAGLVFLT LPFALAVHDA FACAFGRAGL LVSVSDGGFG RRGGWDGTVW FVFGVFAFLN VVVSAGLTKL AYKKMMRRHS RYALFLSGVA ACAAVAWIFK LLLGSAALGG LSGEAVSEYA FAVWLVSMLT LPKRLTRAPV QPVVFHRKK // ID Q5F903_NEIG1 Unreviewed; 456 AA. AC Q5F903; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Transporter {ECO:0000256|RuleBase:RU003732}; GN ORFNames=NGO_0606 {ECO:0000313|EMBL:AAW89334.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89334.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89334.1; -; Genomic_DNA. DR RefSeq; WP_003692969.1; NC_002946.2. DR RefSeq; YP_207746.1; NC_002946.2. DR ProteinModelPortal; Q5F903; -. DR EnsemblBacteria; AAW89334; AAW89334; NGO_0606. DR GeneID; 3281535; -. DR KEGG; ngo:NGO0606; -. DR PATRIC; 20334292; VBINeiGon24812_0718. DR HOGENOM; HOG000033129; -. DR KO; K03308; -. DR OMA; TLTIWHT; -. DR OrthoDB; EOG6PGK51; -. DR BioCyc; NGON242231:GI2G-574-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 102 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 177 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 189 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 252 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 311 340 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 352 374 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 394 414 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 435 455 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 456 AA; 49880 MW; 8A8131698E5C4B49 CRC64; MSSPSNTNRQ TWSSRLTYIL TVAGATVGFG ATWRFPYLVG ENGGGAYVFL FCIAMLVIGI PMILVENVIG RRKGVNALDA FGGPMNGKPV AKIWKLVGRM GLLGAFGIMA YYMVLGGWVI SYIVNIIGGN LNISSPVDGV VTKGFFTEHI ENSPWEIASY TLLFVAVNQW ILVKGVIGGI EKTAKYLMPL LFLFLIAMVV RNVTLPGAME GVAFYLKPDF SKITAELFVF VLGQVFFALS LGFGVMITLS SYLDKNENLV QTAVITAITN TIIAVLAGFM IFPSLFSFGV APNSGPTLVF QSLPIVFSHM WAGPVFAVIF FSLLLIAALT TSLTIYEVLI TTIQEKTKIR RTAAITIVLS VIFVFGNIPS ILSYGPWKDV SVFGKNIFDA FDYISGNILF MLTALGSALF VGFVMKDEAK EELLYKGNHT TVNIWFAYVK YLVPLVILLI FVSNLF // ID Q5F7Q2_NEIG1 Unreviewed; 119 AA. AC Q5F7Q2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89785.1}; GN ORFNames=NGO_1118 {ECO:0000313|EMBL:AAW89785.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89785.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89785.1; -; Genomic_DNA. DR RefSeq; WP_003691733.1; NC_002946.2. DR RefSeq; YP_208197.1; NC_002946.2. DR EnsemblBacteria; AAW89785; AAW89785; NGO_1118. DR GeneID; 3281899; -. DR KEGG; ngo:NGO1118; -. DR PATRIC; 20335490; VBINeiGon24812_1311. DR HOGENOM; HOG000071223; -. DR OMA; ARENHLW; -. DR OrthoDB; EOG6J74X7; -. DR BioCyc; NGON242231:GI2G-1030-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 13785 MW; 2FE69CF52A27127B CRC64; MQVLLGEDFK RALKNYPKED RRKIAEFIAH VQQNGLSGLP GRNKSSDNVP ADDPQWLEKV RFAQRHNLWH YHIGIPKYNG GRYGDLTSAY ILHYTLCDGF IKIIGFDRHP PFILPDIPK // ID Q5F9V9_NEIG1 Unreviewed; 374 AA. AC Q5F9V9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 73. DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028}; DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028}; GN ORFNames=NGO_0278 {ECO:0000313|EMBL:AAW89028.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89028.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89028.1; -; Genomic_DNA. DR RefSeq; WP_003692709.1; NC_002946.2. DR RefSeq; YP_207440.1; NC_002946.2. DR ProteinModelPortal; Q5F9V9; -. DR SMR; Q5F9V9; 98-334. DR EnsemblBacteria; AAW89028; AAW89028; NGO_0278. DR GeneID; 3281614; -. DR KEGG; ngo:NGO0278; -. DR PATRIC; 20333529; VBINeiGon24812_0345. DR HOGENOM; HOG000275919; -. DR KO; K06180; -. DR OMA; TYGGRPR; -. DR OrthoDB; EOG6P070X; -. DR BioCyc; NGON242231:GI2G-260-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU362028}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 39 112 S4 RNA-binding. FT {ECO:0000259|PROSITE:PS50889}. SQ SEQUENCE 374 AA; 41295 MW; DA58166BF30D79CE CRC64; MQNTSFDNES DYSDDSDFAS ASGTENRIGL TVPLELAGGR LDAVLAKLLP DYSRSRLTSW IKEGAVIVND KPSQPKDKMI GGEQICVTVR PSEENLAFVP EPMDLDIVYE DDTVIVVNKP AGLVVHPAAG NWTGTLLNGL LAHCPELSQI PRAGIVHRLD KETSGLMVVA KTLPAQNSLV RQLQERTVKR IYRAVANGIV PFDGKIETQI GRDPHNRLKM AAVKFGGKPA VTHVKVLERY LAHSYIECSL GTGRTHQIRV HMREANHPLA GDPVYGNPRH PCGDTVKEAV KSLGARQALH AYRLSFTHPE SGETVSFEAP IPDDIYHLLS VLRLEAGLDS SLSNEEEWQD KFGADDDDDW NEDDYDVEVV YVRE // ID Q5F6A7_NEIG1 Unreviewed; 58 AA. AC Q5F6A7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90280.1}; GN ORFNames=NGO_1653 {ECO:0000313|EMBL:AAW90280.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90280.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90280.1; -; Genomic_DNA. DR RefSeq; WP_003689785.1; NC_002946.2. DR RefSeq; YP_208692.1; NC_002946.2. DR EnsemblBacteria; AAW90280; AAW90280; NGO_1653. DR GeneID; 3281331; -. DR KEGG; ngo:NGO1653; -. DR PATRIC; 20336852; VBINeiGon24812_1971. DR OrthoDB; EOG63RGXV; -. DR BioCyc; NGON242231:GI2G-1549-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 58 AA; 6979 MW; 4B4E8AB633CDA36F CRC64; MNPTKQSKKS YESKRVLKHV SFNTEKEANL LEFSNNLDFS KWVKEKLKHE LELEKLKK // ID Q5F9B1_NEIG1 Unreviewed; 49 AA. AC Q5F9B1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89226.1}; GN ORFNames=NGO_0488 {ECO:0000313|EMBL:AAW89226.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89226.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89226.1; -; Genomic_DNA. DR RefSeq; WP_010951059.1; NC_002946.2. DR RefSeq; YP_207638.1; NC_002946.2. DR TCDB; 1.E.22.1.1; the neisserial phage-associated holin (np-holin) family. DR EnsemblBacteria; AAW89226; AAW89226; NGO_0488. DR GeneID; 3282959; -. DR KEGG; ngo:NGO0488; -. DR PATRIC; 20334014; VBINeiGon24812_0579. DR HOGENOM; HOG000071251; -. DR OrthoDB; EOG661HK0; -. DR BioCyc; NGON242231:GI2G-466-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5275 MW; 926DCB991B45F6CC CRC64; MDTLLSIITA LSFAGAATLA VWLLVEAADA VLRRKREGKG EDDFDGFGY // ID Q5F5L7_NEIG1 Unreviewed; 135 AA. AC Q5F5L7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=RNA-binding protein {ECO:0000313|EMBL:AAW90520.1}; GN ORFNames=NGO_1906 {ECO:0000313|EMBL:AAW90520.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90520.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90520.1; -; Genomic_DNA. DR RefSeq; WP_003690202.1; NC_002946.2. DR RefSeq; YP_208932.1; NC_002946.2. DR EnsemblBacteria; AAW90520; AAW90520; NGO_1906. DR GeneID; 3282272; -. DR KEGG; ngo:NGO1906; -. DR PATRIC; 20337532; VBINeiGon24812_2293. DR HOGENOM; HOG000218680; -. DR OMA; FTVAGCQ; -. DR OrthoDB; EOG61ZTGT; -. DR BioCyc; NGON242231:GI2G-1809-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 135 AA; 15518 MW; BD3B31EC7FE54BD9 CRC64; MEIRVIKYTA TAALFAFTVA GCRLAGWYEC SSLSGWCKPR KPAAIDFWDI GGESPLSLED YEIPLSDGNR SVRANEYESA QKSYFYRKIG KFEACGLDWR TRDGKPLVER FKQEGFDCLE KQGLRRNGLS ERVRW // ID Q5F596_NEIG1 Unreviewed; 210 AA. AC Q5F596; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Metallo-beta-lactamase {ECO:0000313|EMBL:AAW90641.1}; GN ORFNames=NGO_2033 {ECO:0000313|EMBL:AAW90641.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90641.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90641.1; -; Genomic_DNA. DR RefSeq; WP_010951386.1; NC_002946.2. DR RefSeq; YP_209053.1; NC_002946.2. DR ProteinModelPortal; Q5F596; -. DR EnsemblBacteria; AAW90641; AAW90641; NGO_2033. DR GeneID; 3282714; -. DR KEGG; ngo:NGO2033; -. DR PATRIC; 20337849; VBINeiGon24812_2448. DR HOGENOM; HOG000058039; -. DR OMA; QSTRFGF; -. DR OrthoDB; EOG69GZQ4; -. DR BioCyc; NGON242231:GI2G-1934-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 194 Lactamase_B. {ECO:0000259|SMART:SM00849}. SQ SEQUENCE 210 AA; 23576 MW; C235CD7E9518D848 CRC64; MTLRYEILPV TPFRQNCTLI WDDESGEAVL TDVGGDVPFL LQALANRKLT LTAIWLTHGH LDHAGGVVEM LETHKVPVLG PHREDEFLLQ SLPQTTAQYG FPVSPAFAPN RWLEEGETLT VGRYAFQVLH IPGHTPGHVV FYCAEAELLI AGDVLFYETI GRTDFPRGNH ADLINNIRNK LFAFPETVQV VAGHERMTSI GHEKRHNPFF // ID Q5F667_NEIG1 Unreviewed; 268 AA. AC Q5F667; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Signal transduction protein {ECO:0000313|EMBL:AAW90320.1}; GN ORFNames=NGO_1699 {ECO:0000313|EMBL:AAW90320.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90320.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90320.1; -; Genomic_DNA. DR RefSeq; WP_003689873.1; NC_002946.2. DR RefSeq; YP_208732.1; NC_002946.2. DR EnsemblBacteria; AAW90320; AAW90320; NGO_1699. DR GeneID; 3281214; -. DR KEGG; ngo:NGO1699; -. DR PATRIC; 20336990; VBINeiGon24812_2035. DR HOGENOM; HOG000255939; -. DR OMA; FTLAAFH; -. DR OrthoDB; EOG69SKBK; -. DR BioCyc; NGON242231:GI2G-1595-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 29842 MW; 971E9AD1AB2E0A40 CRC64; MPTVFIFLTA VYAGLGAFAW HCQQQGRGRD YPWKTELPVL GAALTVHGAA LLMPVIQDKI IIMGFGYSGS LIVWMMLFIY FAGSFFYPLR GVQLLLYPCA ALMLLSGLVF PGKFSGYEIT DFPFMLHIGT SLLAYGLFGI ATLLSVLSLL LHRSLHRRNF SKLAGFLPSL LSLEKLMFQA MWAGFILLTY SVVSGTFFAE AVFGKPMTFT HKTVFGILSW LIYGGLLLKH SMTAWRGKKA AVWTIIGFVS LMIAYMGSKF VLEIILKR // ID Q5F9I7_NEIG1 Unreviewed; 1032 AA. AC Q5F9I7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 78. DE SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:AAW89150.1}; GN ORFNames=NGO_0407 {ECO:0000313|EMBL:AAW89150.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89150.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89150.1; -; Genomic_DNA. DR RefSeq; WP_003706627.1; NC_002946.2. DR RefSeq; YP_207562.1; NC_002946.2. DR ProteinModelPortal; Q5F9I7; -. DR REBASE; 5504; NgoAV. DR EnsemblBacteria; AAW89150; AAW89150; NGO_0407. DR GeneID; 3282183; -. DR KEGG; ngo:NGO0407; -. DR PATRIC; 20333825; VBINeiGon24812_0490. DR HOGENOM; HOG000003518; -. DR KO; K01153; -. DR OMA; NFKQKTH; -. DR OrthoDB; EOG6JTCB4; -. DR BioCyc; NGON242231:GI2G-385-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89150.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89150.1}; KW Nuclease {ECO:0000313|EMBL:AAW89150.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 294 439 Helicase ATP-binding. FT {ECO:0000259|PROSITE:PS51192}. FT COILED 51 74 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 1032 AA; 118500 MW; A2B501A1D04AEA00 CRC64; MNLETKPIAE TPNFIVLDQY EKIEQSGSYQ SENRLEAELI ADLQNQGYEY RKDLNSQSRL LENLRAQLQR LNDVAFSDGE WARFLTEYLD RPAENITDKT RKIHDDHIYD FAFDDGRLKN IYLLDKKNLA RNHVQLINQF EQTGTHANRY DVTVLVNGLP LVQIELKKRG VAVREAFNQV HRYSKESFNS GNSLFKFLQI FVISNGTDTR YFANTTKRDK NSFDFTMNWA RSDNHPIKDL KDFTATFLQK SVLLSVLLHY SVFDANDTLL IMRPYQIAAA ERILWKINSS AQAKNWSGPE SGGYVWHTTG SGKTLTGFKA ARLATESAFI DKVFFVVDRK DLDYQTMKEY QRFSPDSVNG SESTAGLKRN LEKDGNKIIV TTIQKLNNLM KSEDNLPVYH RQVVFIFDEC HRSQFGEAQK NLKKKFKKFC QFGFTGTPIF PENALGAETT AGVFGRELHS YVITDAIRDE KVLKFKVDYN DVRPQFKAVE AEQDEKELSA AENRQALLHP ERIREITQYI LSRFRQKTHR LNAGGKGFNA MFAVSSVDAA KCYYEAFKTQ QAGSLHPLKT ATIFSFAANE EQNAVGEIVD ETFEPEAMDS SAKEFLQAAI NDYNACFKTN FGTDSKAFQN YYRDLAKRVK NREVDLLIVV GMFLTGFDAP TLNTLFVDKN LRYHGLMQAF SRTNRIYDAT KTFGNIVCFR DLEQATIDAI TLFGDKNTKN VVLEKSYEEY MNGYTDSQTG EARRGYLDVA KELHERFPDP DKIETEKDKK DFAKLFGEYL RAENVLQNYD EFAALRELQN VDAADEDAMK AFQEKYYLSD EDVQEMRKVP MPSERAVQDY RSAYNDIRDW LRRQKAGEQK EQSKIDWDDV VFEVDLLKSQ EINLDYILQL VFEHHKKIKG KAELVEEIRR IIRASIGHRA KEGLIVDFIN DTDLDKVPDV PAILETFYTY AQEVMRHEAA GLIAAEGLNE TAAKRYLTGS LKRGYASENG TELTETLPKM SPLNPQYLTK KQSVFQKIAA FVEKFAGIGA DI // ID Q5F994_NEIG1 Unreviewed; 88 AA. AC Q5F994; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89243.1}; GN ORFNames=NGO_0505 {ECO:0000313|EMBL:AAW89243.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89243.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89243.1; -; Genomic_DNA. DR RefSeq; WP_003689070.1; NC_002946.2. DR RefSeq; YP_207655.1; NC_002946.2. DR EnsemblBacteria; AAW89243; AAW89243; NGO_0505. DR GeneID; 3282944; -. DR KEGG; ngo:NGO0505; -. DR PATRIC; 20334052; VBINeiGon24812_0598. DR OMA; ASYMGIK; -. DR OrthoDB; EOG6TTVRX; -. DR BioCyc; NGON242231:GI2G-483-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 88 AA; 9597 MW; 8CD35614C6821E5D CRC64; MIAHVCASTG WTWDYVADNL DLPRIKHLNE YWREHPPVHI LAASYMGVKP SSGSVQSEAD EAEAVGMLGG GELSEDEFDA LLKAKGII // ID Q5F664_NEIG1 Unreviewed; 174 AA. AC Q5F664; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90323.1}; GN ORFNames=NGO_1702 {ECO:0000313|EMBL:AAW90323.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90323.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90323.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F664; -. DR EnsemblBacteria; AAW90323; AAW90323; NGO_1702. DR PATRIC; 20336996; VBINeiGon24812_2038. DR HOGENOM; HOG000089187; -. DR OMA; FYEDPAP; -. DR OrthoDB; EOG6SV5D7; -. DR BioCyc; NGON242231:GI2G-1598-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR000415; Nitroreductase-like. DR SUPFAM; SSF55469; SSF55469; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 174 AA; 18953 MW; 834310D93F209DDD CRC64; MAVASNVSLD MSNPTVLRMG LPLYIASLRR GAIYKVWQFV EDALRAVVPA DSFEPTAQKL KLFKAGAATI LFYEDQNVVK GLQEQFPAYA ANFPVWADQA NAMVQYAVWT TLAAVGAGAN LQHYNPLPDV AIAKAWNIPE NWLLRAQMVI GGIEGAAGEK VFEPVAERLK VFGA // ID Q5F723_NEIG1 Unreviewed; 210 AA. AC Q5F723; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 73. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAW90014.1}; GN ORFNames=NGO_1366 {ECO:0000313|EMBL:AAW90014.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90014.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90014.1; -; Genomic_DNA. DR RefSeq; WP_003693763.1; NC_002946.2. DR RefSeq; YP_208426.1; NC_002946.2. DR ProteinModelPortal; Q5F723; -. DR EnsemblBacteria; AAW90014; AAW90014; NGO_1366. DR GeneID; 3281546; -. DR KEGG; ngo:NGO1366; -. DR PATRIC; 20336117; VBINeiGon24812_1607. DR HOGENOM; HOG000260115; -. DR KO; K03577; -. DR OMA; MMEIIFH; -. DR OrthoDB; EOG6SNDRN; -. DR BioCyc; NGON242231:GI2G-1279-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000710, KW ECO:0000256|SAAS:SAAS00483316}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 24193 MW; 41E26446CBEF57F2 CRC64; MRKTKTEALK TKEHLMLAAL ETFYRKGIAR TSLNEIAQAA GVTRGALYWH FKNKEDLFDA LFQRICDDIE NCIAQDAADA EGGSWTVFRH TLLHFFERLQ SNDIHYKFHN ILFLKCEHTE QNAAVIAIAR KHQAIWREKI TAVLTEAVEN QDLADDLDKE TAVIFIKSTL DGLIWRWFSS GESFDLGKTA PRIIGIMMDN LENHPCLRRK // ID Q5F974_NEIG1 Unreviewed; 62 AA. AC Q5F974; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89263.1}; GN ORFNames=NGO_0525 {ECO:0000313|EMBL:AAW89263.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89263.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89263.1; -; Genomic_DNA. DR RefSeq; WP_003689039.1; NC_002946.2. DR RefSeq; YP_207675.1; NC_002946.2. DR EnsemblBacteria; AAW89263; AAW89263; NGO_0525. DR GeneID; 3282924; -. DR KEGG; ngo:NGO0525; -. DR PATRIC; 20334096; VBINeiGon24812_0620. DR HOGENOM; HOG000071307; -. DR OMA; ALYVPFC; -. DR OrthoDB; EOG6JDWHB; -. DR BioCyc; NGON242231:GI2G-503-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 62 AA; 6805 MW; 4490F1B7E9DEC40D CRC64; MADGRKGFFD AIIKINIFFF PVKTPTLGAA NPIAGGSTRF RFGAEQMAVL YVPFCVLKHI GR // ID Q5F6D4_NEIG1 Unreviewed; 138 AA. AC Q5F6D4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90253.1}; GN ORFNames=NGO_1625 {ECO:0000313|EMBL:AAW90253.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90253.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90253.1; -; Genomic_DNA. DR RefSeq; WP_003693479.1; NC_002946.2. DR RefSeq; YP_208665.1; NC_002946.2. DR EnsemblBacteria; AAW90253; AAW90253; NGO_1625. DR GeneID; 3281405; -. DR KEGG; ngo:NGO1625; -. DR HOGENOM; HOG000289754; -. DR OMA; RANIPYD; -. DR OrthoDB; EOG6QRWDZ; -. DR BioCyc; NGON242231:GI2G-1522-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 138 AA; 15432 MW; 34C65E794A21A434 CRC64; MPQSWQCRQG ACLLIPSGPN SCQHLFTILV NPCILPNRGN KPQVLSVGIS SVRANIPYDN ACIIRQGEHP FVRHDSYVRY RDARIDAVEH IENRVHEGIF SVKPPCGEQL LKRIIAGAST SRYAGREVKL LIEKFAIA // ID Q5FAI0_NEIG1 Unreviewed; 127 AA. AC Q5FAI0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 09-DEC-2015, entry version 47. DE SubName: Full=Glucosamine-fructose-6-phosphate aminotransferase {ECO:0000313|EMBL:AAW88807.2}; GN ORFNames=NGO_0039 {ECO:0000313|EMBL:AAW88807.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88807.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88807.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88807; AAW88807; NGO_0039. DR PATRIC; 20332912; VBINeiGon24812_0041. DR HOGENOM; HOG000027868; -. DR OMA; YAYHEVS; -. DR OrthoDB; EOG6VHZCN; -. DR BioCyc; NGON242231:GI2G-35-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Aminotransferase {ECO:0000313|EMBL:AAW88807.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88807.2}. SQ SEQUENCE 127 AA; 14997 MW; DD8811D400BFA06C CRC64; MYCLRLRRLV LIFVNPLYQT EEGIAQTVVK GKTTRAEVEA RFGKRNPFGC YAYHEVSLPI YNFLPTNFIY MKSERRHWEW CADYDGEGVV RDYRFTHKVE KDERSVIRDT VGVIRKEAGK SLSQPEK // ID Q5F927_NEIG1 Unreviewed; 725 AA. AC Q5F927; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 97. DE SubName: Full=Metal ABC transporter ATPase {ECO:0000313|EMBL:AAW89310.1}; GN ORFNames=NGO_0579 {ECO:0000313|EMBL:AAW89310.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89310.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89310.1; -; Genomic_DNA. DR RefSeq; WP_010951087.1; NC_002946.2. DR RefSeq; YP_207722.1; NC_002946.2. DR ProteinModelPortal; Q5F927; -. DR EnsemblBacteria; AAW89310; AAW89310; NGO_0579. DR GeneID; 3282903; -. DR KEGG; ngo:NGO0579; -. DR PATRIC; 20334224; VBINeiGon24812_0684. DR HOGENOM; HOG000250397; -. DR KO; K17686; -. DR OMA; TLPKFSD; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NGON242231:GI2G-550-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000256|RuleBase:RU362081}; KW Membrane {ECO:0000256|RuleBase:RU362081}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|RuleBase:RU362081}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 89 111 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 123 141 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 153 175 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 187 205 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 339 361 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 367 392 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 676 693 Helical. {ECO:0000256|RuleBase:RU362081}. FT TRANSMEM 699 717 Helical. {ECO:0000256|RuleBase:RU362081}. FT DOMAIN 4 70 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 725 AA; 76988 MW; 966CEAB836DC0F74 CRC64; MQQKIRFQIE GMTCQACASR IEKVLNKKDF VESAGVNFAS EEAQVTFDGS KTSVADIAKI IEKTGYGAKE KTEDTLPQPE AEHHIGWRLW LLLTINIPFL IGMVGMMLKG LNWTRHDWMI PPVWQFVLAS IVQLWLAIPF YKSAWASIKG GLANMDVLVT IGTVSIYLYS VYMLFFSSHA AHGMAHVYFE AGVMVIGFVS LGKFLEHRTK KSSLNSLGLL LKLTPTQVNV QRNGEWKQLP IDQVQIGDLI RTNHGERIAA DGIIESGSGW ADESHLTGES NPEEKKAGGK VLAGALMTEG SVVYRAAQLG SQTLLGDMMN ALSEAQGSKA PIARVADKAA AVFVPTVVGI ALLTFIVAWL IKGDWTVALM HAVAVLVIAC PCALGLATPA AIMVGMGKAV KHGIWFKDAA AMEEAAHVDA VVLDKTGTLT EGRPQVAAVY YVPDSGFDED ALYRIAAAVE QNAAHPLARA IVSAAQARGL EIPAAQNAQT VVGAGITAEV EGVGLVKSGK AEFAELTLPK FSDGVWEIAS AVTVSVNGKP IGAFALSDAL KADTAEAIGR LKKHNIDVYI MSGDNQSTVE YVAKQLGIAH AFGNMSPCDK AAEVQKLKAA GKTVAMVGDG INDAPALAAA NVSFAMKGGA DVAEHTASAT LMQHSVNQLA DALLISQATL ENIKQNLFFA FFYNILGIPL AALGFLNPVI AGAAMAASSV SVLGNALRLK WVKID // ID Q5F8J1_NEIG1 Unreviewed; 131 AA. AC Q5F8J1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89496.2}; GN ORFNames=NGO_0782 {ECO:0000313|EMBL:AAW89496.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89496.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89496.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89496; AAW89496; NGO_0782. DR PATRIC; 20334710; VBINeiGon24812_0927. DR HOGENOM; HOG000071290; -. DR OMA; KEARTGC; -. DR OrthoDB; EOG6SFPGT; -. DR BioCyc; NGON242231:GI2G-736-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 131 AA; 13961 MW; D6B0C7AEBD763083 CRC64; MPSDKEARAG CLSLPANNGI IRTLPPPFYF TGINIRLFAA LGLLSLSGAA AQASIYHCNS NGKSVYTSDP SGSCADADLP KISSHQGGGY RLKIKKLSQE AKIHTGNKKK NKKHAGKKNR QAAKAPKENQ K // ID Q5F8F8_NEIG1 Unreviewed; 65 AA. AC Q5F8F8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89529.1}; GN ORFNames=NGO_0818 {ECO:0000313|EMBL:AAW89529.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89529.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89529.1; -; Genomic_DNA. DR RefSeq; WP_010358165.1; NC_002946.2. DR RefSeq; YP_207941.1; NC_002946.2. DR EnsemblBacteria; AAW89529; AAW89529; NGO_0818. DR GeneID; 3281953; -. DR KEGG; ngo:NGO0818; -. DR PATRIC; 20334790; VBINeiGon24812_0965. DR HOGENOM; HOG000027811; -. DR OMA; AVLFWIW; -. DR OrthoDB; EOG6FZ4HW; -. DR BioCyc; NGON242231:GI2G-771-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 62 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 65 AA; 7525 MW; 7422A30B3AFFFA26 CRC64; MPSEKIYYGV LIFLCIASML LSPFFYAGAL KPKKAALRKD GQWKLILLSN AVAAAVLFWI WWKWF // ID Q5F9M2_NEIG1 Unreviewed; 302 AA. AC Q5F9M2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Peroxidase {ECO:0000313|EMBL:AAW89115.1}; GN ORFNames=NGO_0371 {ECO:0000313|EMBL:AAW89115.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89115.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89115.1; -; Genomic_DNA. DR RefSeq; WP_010357322.1; NC_002946.2. DR RefSeq; YP_207527.1; NC_002946.2. DR ProteinModelPortal; Q5F9M2; -. DR EnsemblBacteria; AAW89115; AAW89115; NGO_0371. DR GeneID; 3282189; -. DR KEGG; ngo:NGO0371; -. DR PATRIC; 20333743; VBINeiGon24812_0449. DR HOGENOM; HOG000151980; -. DR KO; K07223; -. DR OMA; CAEPNLH; -. DR OrthoDB; EOG6N682X; -. DR BioCyc; NGON242231:GI2G-350-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Oxidoreductase {ECO:0000313|EMBL:AAW89115.1}; KW Peroxidase {ECO:0000313|EMBL:AAW89115.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 302 AA; 32829 MW; 848E575E06FA2023 CRC64; MNTPQSAIIP DHAQAGIFIE ADFAANRLND IKAACRASLD ALSALKARFP DDILGLTIAF GSKAWATFGH TDEGSEIKPF PEMGNGLAPS TQHDMSIHIQ SFRQNAAYAL AQSVLGAFGD SICVASEEHG LRLYQDRGLD GFVDGTENPQ GDETIREVAI IPEGLPDAGG SYVLLQKYLH DLKKWDAVPV AEQEASVGRS KETDDEFSRD VRLPDSHLGR VNLKENGVGL KIVRRSLPFG KISGEHGLMF TAYCRTLHNI EAQLLSMFGD TDGKTDLLLR HLSAAVSGGY YYAPSVERLQ NL // ID Q5F8S4_NEIG1 Unreviewed; 50 AA. AC Q5F8S4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89413.1}; GN ORFNames=NGO_0686 {ECO:0000313|EMBL:AAW89413.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89413.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89413.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89413; AAW89413; NGO_0686. DR BioCyc; NGON242231:GI2G-653-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 50 AA; 5900 MW; E76838836EFB68F5 CRC64; MRKKIKKWIY ATNGIIMSIW IIFFQILALC MTVAEQPFSM KTILFILFSA // ID Q5F535_NEIG1 Unreviewed; 139 AA. AC Q5F535; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90702.1}; GN ORFNames=NGO_2101 {ECO:0000313|EMBL:AAW90702.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90702.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90702.1; -; Genomic_DNA. DR RefSeq; WP_003687072.1; NC_002946.2. DR RefSeq; YP_209114.1; NC_002946.2. DR EnsemblBacteria; AAW90702; AAW90702; NGO_2101. DR GeneID; 3282816; -. DR KEGG; ngo:NGO2101; -. DR PATRIC; 20338039; VBINeiGon24812_2542. DR HOGENOM; HOG000130289; -. DR OMA; CTIAELC; -. DR OrthoDB; EOG6DZF1M; -. DR BioCyc; NGON242231:GI2G-1996-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 139 AA; 15553 MW; 6C03D44AF6985506 CRC64; MAQLPLYRTA EIGNFTVGTP KVLESFSKHI PYGVVFEDDG NTGYFYAASQ EGILDALHIY NVEDVSDKHI PNHVLILWDG ACTIAALCIN DYIHAVYDFV EQAGYCRNGF PEAGGEWVKV ENRVLDDELL DKILSRKPT // ID Q5F8P3_NEIG1 Unreviewed; 40 AA. AC Q5F8P3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89444.1}; GN ORFNames=NGO_0724 {ECO:0000313|EMBL:AAW89444.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89444.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89444.1; -; Genomic_DNA. DR RefSeq; WP_003691222.1; NC_002946.2. DR RefSeq; YP_207856.1; NC_002946.2. DR EnsemblBacteria; AAW89444; AAW89444; NGO_0724. DR GeneID; 3282009; -. DR KEGG; ngo:NGO0724; -. DR BioCyc; NGON242231:GI2G-684-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 40 AA; 4359 MW; 0E9676C9448938D8 CRC64; MPALPPVMKP ERFFGESRLK GDAALTFSPI FSGFFIADAV // ID Q5F9U9_NEIG1 Unreviewed; 246 AA. AC Q5F9U9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89038.1}; GN ORFNames=NGO_0290 {ECO:0000313|EMBL:AAW89038.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89038.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89038.1; -; Genomic_DNA. DR DNASU; 3281652; -. DR EnsemblBacteria; AAW89038; AAW89038; NGO_0290. DR PATRIC; 20333559; VBINeiGon24812_0360. DR HOGENOM; HOG000244091; -. DR OMA; MPPETAQ; -. DR OrthoDB; EOG63FW29; -. DR BioCyc; NGON242231:GI2G-270-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR008526; YedI. DR Pfam; PF05661; DUF808; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 100 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 164 186 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 246 AA; 26955 MW; 6B52A1473D062EC0 CRC64; MAFASLFTLP DYIAAVLDDV ALMTKAAAKK TAGVAGDDLA PNANRVTGVS AERELPIVWP VAKGSFANKP VLVSAALLLS AFLPQLITPL LTAGGIYLCF EGVEKLLHKF LHRHDAHDDG GETAVNEQAK IKGAIRTDFI LSAEIIIIAL CVVEQYSLMT RSLVMAAIGI GMTVLVYGIV AVIVKLDDLG MLLMRRPQPR PFARFPARAT LERWLDRVFR QPRCRAAFRF DCLRPALSLM NRFGRH // ID Q5F6E6_NEIG1 Unreviewed; 384 AA. AC Q5F6E6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Integrase {ECO:0000313|EMBL:AAW90241.1}; GN ORFNames=NGO_1613 {ECO:0000313|EMBL:AAW90241.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90241.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90241.1; -; Genomic_DNA. DR RefSeq; WP_003693486.1; NC_002946.2. DR RefSeq; YP_208653.1; NC_002946.2. DR ProteinModelPortal; Q5F6E6; -. DR EnsemblBacteria; AAW90241; AAW90241; NGO_1613. DR GeneID; 3281247; -. DR KEGG; ngo:NGO1613; -. DR PATRIC; 20336766; VBINeiGon24812_1928. DR HOGENOM; HOG000043213; -. DR OMA; VSGHRSW; -. DR OrthoDB; EOG68WR30; -. DR BioCyc; NGON242231:GI2G-1510-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 195 362 Phage_integrase. FT {ECO:0000259|Pfam:PF00589}. SQ SEQUENCE 384 AA; 44037 MW; F9B53D334A81A720 CRC64; MATITKRRNP SGETVYRVQV RVGKKGYPAF NESRTFSKKA LAVEWGKKRE AEIEAGPELL FKRGKVKMMT LSEAMRKYLN ETLGAGRSKK MGLRFLMEFP IGGIGIDKLK RSDFAEHVMQ RRRGIPELDI APIAASTALQ ELQYIRSVLK HAFYVWGLEI GWQELDFAAN GLKRSNMVAK SAIRDRLPTT EELQTLTTYF LRQWQSRKSS IPMHLIMWLA IYTSRRQDEI CRLLFDDWHK NDCTRPVRDL KNPNGSTGNN KEFDILPMAL PVIDELPEES VRKRMLANKG IADSLVPCNG KSVSAAWTRA CKVLGIKDLR FHDLRHEAAT RMAEDGFTIP QMQRVTLHDG WNSLQRYVSV RKRSTRLDFK EAMMQAQSDI KSGK // ID Q5F918_NEIG1 Unreviewed; 160 AA. AC Q5F918; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89319.1}; GN ORFNames=NGO_0588 {ECO:0000313|EMBL:AAW89319.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89319.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89319.1; -; Genomic_DNA. DR RefSeq; WP_003691328.1; NC_002946.2. DR RefSeq; YP_207731.1; NC_002946.2. DR EnsemblBacteria; AAW89319; AAW89319; NGO_0588. DR GeneID; 3282245; -. DR KEGG; ngo:NGO0588; -. DR PATRIC; 20334248; VBINeiGon24812_0696. DR HOGENOM; HOG000218991; -. DR OMA; NPQDAND; -. DR OrthoDB; EOG6JX7K0; -. DR BioCyc; NGON242231:GI2G-559-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025240; DUF4189. DR Pfam; PF13827; DUF4189; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 160 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256072. FT DOMAIN 24 142 DUF4189. {ECO:0000259|Pfam:PF13827}. SQ SEQUENCE 160 AA; 17123 MW; 30FBF7E7519C279C CRC64; MMKKILAVSA LCLMTAAAQA ADTYGYLAVW QNPQDANDVL QVKTTKEDSA KSEAFAELEA FCKGQDTLAG IAEDEPTGCR SVVSLNNTCV SLAYPKALGA MRVENAVVIT SPRFTSVHQV ALNQCIKKYG AQGQCGLETV YCTSSSYYGG AVRSLIQHLK // ID Q5F9X0_NEIG1 Unreviewed; 424 AA. AC Q5F9X0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Folylpolyglutamate synthase {ECO:0000313|EMBL:AAW89017.1}; GN ORFNames=NGO_0266 {ECO:0000313|EMBL:AAW89017.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89017.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89017.1; -; Genomic_DNA. DR RefSeq; WP_003687619.1; NC_002946.2. DR RefSeq; YP_207429.1; NC_002946.2. DR ProteinModelPortal; Q5F9X0; -. DR EnsemblBacteria; AAW89017; AAW89017; NGO_0266. DR GeneID; 3281551; -. DR KEGG; ngo:NGO0266; -. DR PATRIC; 20333501; VBINeiGon24812_0331. DR HOGENOM; HOG000019982; -. DR KO; K11754; -. DR OMA; FHALENI; -. DR OrthoDB; EOG6ZPSW2; -. DR BioCyc; NGON242231:GI2G-249-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. 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:UP000000535}; KW Ligase {ECO:0000256|PIRNR:PIRNR001563}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001563}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 45 267 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. SQ SEQUENCE 424 AA; 46418 MW; A92D8CE350A555F9 CRC64; MKTLQDWLSH LETAHSGGLI DMGLERVSEV KKRMNLTPQC PVVVVAGTNG KGSVCAYLTQ IYKQAGFKTG TLTSPHLLHY NERIAINAEP VSDDTIIASF ERIEAARGEI SLTYFEFNAL AAVDIFIREQ VDVMILEVGL GGRLDAVNAF DGDCAVVTSV DLDHQAFLGD TVEQVGFEKA GVFRSGKPAI CGQNPAPASL VAHAEAIGAK LLMVQRDFEF HAMENIQWNY RFRPQHSDGP ARNRNALPFP ALRGAYQLSN AACALTVLEC LDDRLPVDIG AIKRGLLLVE NPGRFQVLPG RPLTVLDVGH NPHAARALRR NLINLAYAQK RTAVFSMLSD KDIDGVSETV KDQFDEWYIA PLDVPRGMTA DALKAKLEQH HIENIQTFAA VRDAYRAAAS KAGEDDRIVV FGSFHTVADV MSVL // ID Q5F5P4_NEIG1 Unreviewed; 407 AA. AC Q5F5P4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 57. DE SubName: Full=Peptidoglycan-binding protein LysM {ECO:0000313|EMBL:AAW90493.2}; GN ORFNames=NGO_1873 {ECO:0000313|EMBL:AAW90493.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90493.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90493.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5P4; -. DR EnsemblBacteria; AAW90493; AAW90493; NGO_1873. DR PATRIC; 20337440; VBINeiGon24812_2251. DR HOGENOM; HOG000270067; -. DR OMA; PELWGMN; -. DR OrthoDB; EOG6F55N6; -. DR BioCyc; NGON242231:GI2G-1777-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 407 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364407. FT DOMAIN 34 83 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 407 AA; 45448 MW; 863A2087852495DB CRC64; MQRRIITLLC AAGMAFSTQT LAANLEVRPD APQRYTVKQG DTLWGISGKY LYSPWQWCRL WGANRDQIHN PDLIYPGQVL VLRYVGGEPR LGLEQTDGIP VVKISPDKEV SGYGIPAIDV NFYRVFMQHP QIVSRKETAA APRLLSGPEG RLLYTKGARV YTKGLKEPGR YLTYRINKNI TDPDTGKFLG QEVAFSGIVR SLDYTDSALE QRSKQAEERL KDNEYYTRTH PLITPVRTRS IQPLVVETAI SEIQQGDYLM KMPEDTDRFN MVPHEPSRPV QAKIVSVFEG VGVGGQFKTI TIDKGGDDGL DKGAVLSLYK RKKTMQVNLS NNLTEEPKSR DTVELISTPA EEVGLAMVYH TAPKLAYAII LENISDISEG DTAANPGRDL DNMPDQGRAR VDSDPFQ // ID Q5FAC4_NEIG1 Unreviewed; 650 AA. AC Q5FAC4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 62. DE SubName: Full=Cytochrome C biogenesis protein {ECO:0000313|EMBL:AAW88863.2}; GN ORFNames=NGO_0102 {ECO:0000313|EMBL:AAW88863.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88863.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88863.2; -; Genomic_DNA. DR EnsemblBacteria; AAW88863; AAW88863; NGO_0102. DR PATRIC; 20333103; VBINeiGon24812_0135. DR HOGENOM; HOG000254993; -. DR OMA; YSAWWFL; -. DR OrthoDB; EOG67T5FM; -. DR BioCyc; NGON242231:GI2G-92-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 46 72 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 145 163 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 583 602 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 633 ResB. {ECO:0000259|Pfam:PF05140}. SQ SEQUENCE 650 AA; 73828 MW; 0F4E949A9AE5BE3C CRC64; MRFAVALLSL LGIASVIGTV LQQNQPQTDY LVKFGPFWTR IFDFLGLYDV YASAWFVVIM MFLVVSTSLC LIRNVPPFWR EMKSFREKVK EKSLAAMRHS SLLDVKIAPE VAKRYLEVRG FQGKTVSRED GSVLIAAKKG TMNKWGYIFA HVALIVICLG GLIDSNLLLK LGMLAGRIVP DNQAVYAKDF KPESILGASN LSFRGNVNIS EGQSADVVFL NADNGMLVQD LPFEVKLKKF HIDFYNTGMP RDFASDIEVT DKATGEKLER TIRVNHPLTL HGITIYQASF ADGGSDLTFK AWNLRDASRE PVVLKATSIH QFPLEIGKHK YRLEFDQFTS MNVEDMSEGA EREKSLKSTL NDVRAVTQEG KKYTNIGPSI VYRIRDAAGQ AVEYKNYMLP ILQDKDYFWL TGTRSGLQQQ YRWLRIPLDK QLKADTFMAL REFLKDGEGR KRLVADATKD APAEIREQFM LAAENTLNIF AQKGYLGLDE FITSNIPKGQ QDKMQGYFYE MLYGVMNAAL DETIRRYGLP EWQQDEARNR FLLHSMDAYT GLTEYPAPML LQLDGFSEVR SSGLQMTRSP GALLVYLGSV LLVLGTVFMF YVREKRAWVL FSDGKIRFAM SSARSERDLQ KEFPKHVESL QRLGKDLNHD // ID Q5F5Q1_NEIG1 Unreviewed; 425 AA. AC Q5F5Q1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 81. DE SubName: Full=Nitrogen assimilation regulatory protein NtrX {ECO:0000313|EMBL:AAW90486.1}; GN ORFNames=NGO_1866 {ECO:0000313|EMBL:AAW90486.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90486.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3CO5} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 133-272, AND DISULFIDE RP BONDS. RA Osipiuk J., Hendricks R., Bigelow L., Clancy S., Joachimiak A.; RT "X-ray crystal structure of Sigma-54 interaction domain of putative RT transcriptional response regulator from Neisseria gonorrhoeae."; RL Submitted (MAR-2008) to the PDB data bank. 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; AE004969; AAW90486.1; -; Genomic_DNA. DR RefSeq; WP_003690124.1; NC_002946.2. DR RefSeq; YP_208898.1; NC_002946.2. DR PDB; 3CO5; X-ray; 2.40 A; A/B=133-272. DR PDBsum; 3CO5; -. DR ProteinModelPortal; Q5F5Q1; -. DR SMR; Q5F5Q1; 137-272. DR EnsemblBacteria; AAW90486; AAW90486; NGO_1866. DR GeneID; 3282368; -. DR KEGG; ngo:NGO1866; -. DR PATRIC; 20337426; VBINeiGon24812_2244. DR HOGENOM; HOG000058489; -. DR OMA; KHGAAKI; -. DR OrthoDB; EOG69GZGV; -. DR BioCyc; NGON242231:GI2G-1770-MONOMER; -. DR EvolutionaryTrace; Q5F5Q1; -. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3CO5}; KW ATP-binding {ECO:0000256|SAAS:SAAS00515313}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00515313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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}. FT DISULFID 242 253 {ECO:0000213|PDB:3CO5}. SQ SEQUENCE 425 AA; 46519 MW; 685E4309667A6305 CRC64; MRSSDILIVD DEVGIRDLLS EILQDEGYSV ALAENAEEAR KLRHQARPAM VLLDIWMPDC DGITLLKEWA KNGQLNMPVV VMSGHASIDT AVEATKIGAI DFLEKPISLQ KLLSAVENAL KHGAAQIETG PVFDKLGNSA AIQEMNREVE AAAKRTSPVF LTGEAGSPFE TVARYFHKNG TPWVSPARVE YLIDMPMELL QKAEGGVLYV GDIAQYSRNI QTGITFIIGK AERCRVRVIA SCSYAAGSDG ISCEEKLAGL FSESVVRIPP LSMQHEDIPF LIQGIACNVA ESQKITPTAF SDDALAVLSR YDWPGNFEQL QNVVTTLLLE ADGQEIGIGA ASSALGRGVP ADGTGHMACG FDFNLPLREL REEVERRYFE YHIAQEGQNM SKVAQKVGLE RTHLYRKLKQ LGIGVSRRAG EKTEE // ID Q5F7T7_NEIG1 Unreviewed; 106 AA. AC Q5F7T7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89750.1}; GN ORFNames=NGO_1083 {ECO:0000313|EMBL:AAW89750.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89750.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89750.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89750; AAW89750; NGO_1083. DR PATRIC; 20335412; VBINeiGon24812_1272. DR HOGENOM; HOG000071261; -. DR OMA; SKPLAMD; -. DR OrthoDB; EOG6HB9V6; -. DR BioCyc; NGON242231:GI2G-995-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 106 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255521. SQ SEQUENCE 106 AA; 11816 MW; 2974285287344B6E CRC64; MKTVPTILTG ILLATALPAS AHGMHKSKPL AMDELPPICQ QYFKRAETCY NKAGNKADFA RNNTKFLFQA LPAADLGQRK QMCQIAMDSF AEKNPQSELR IKPHQQ // ID Q5F9W5_NEIG1 Unreviewed; 189 AA. AC Q5F9W5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AAW89022.1}; GN ORFNames=NGO_0271 {ECO:0000313|EMBL:AAW89022.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89022.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89022.1; -; Genomic_DNA. DR RefSeq; WP_003687630.1; NC_002946.2. DR RefSeq; YP_207434.1; NC_002946.2. DR ProteinModelPortal; Q5F9W5; -. DR EnsemblBacteria; AAW89022; AAW89022; NGO_0271. DR GeneID; 3281589; -. DR KEGG; ngo:NGO0271; -. DR PATRIC; 20333511; VBINeiGon24812_0336. DR HOGENOM; HOG000249648; -. DR OMA; DIFGARI; -. DR OrthoDB; EOG6GBM9B; -. DR BioCyc; NGON242231:GI2G-254-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro. DR InterPro; IPR007685; RelA_SpoT. DR Pfam; PF04607; RelA_SpoT; 1. DR SMART; SM00954; RelA_SpoT; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000313|EMBL:AAW89022.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89022.1}. FT DOMAIN 76 187 RelA_SpoT. {ECO:0000259|SMART:SM00954}. SQ SEQUENCE 189 AA; 22460 MW; A45B4C662298C918 CRC64; MESNLQKTER LIREINRLHA QYSQDYFETG KVRKINLSHT LKNVPTEHIL SYRLNLHEAV NDYLAFADTR GIDFFYRVKT AESIHDKINR YLARGTQYPT NNILNDIFGA RLIWPSETVA GILEKLDGWK TEYGLKNWYL RDAGGYIGIH IYFKNSSNFY YPWELQVWDE KDAKANIENH MAYKRNFVR // ID Q5F5J0_NEIG1 Unreviewed; 322 AA. AC Q5F5J0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=RfaC {ECO:0000313|EMBL:AAW90547.1}; GN ORFNames=NGO_1934 {ECO:0000313|EMBL:AAW90547.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90547.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90547.1; -; Genomic_DNA. DR RefSeq; WP_003688094.1; NC_002946.2. DR RefSeq; YP_208959.1; NC_002946.2. DR ProteinModelPortal; Q5F5J0; -. DR CAZy; GT9; Glycosyltransferase Family 9. DR EnsemblBacteria; AAW90547; AAW90547; NGO_1934. DR GeneID; 3282685; -. DR KEGG; ngo:NGO1934; -. DR PATRIC; 20337608; VBINeiGon24812_2331. DR HOGENOM; HOG000257134; -. DR KO; K02841; -. DR OMA; LFYNRRH; -. DR OrthoDB; EOG6WQD45; -. DR BioCyc; NGON242231:GI2G-1837-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 322 AA; 36072 MW; 9B52A434751962B4 CRC64; MKILLVRLSS MGDLIHTLPA IEDLARQCSD VELHWLCEAG FAGIARLHPF VKKVHVMKWR QWRKHLFQAE TWREMGRLKQ ALLQEAFDFV LDSQGLIKSA CFAKMAKSPI YGLDKHSARE GVAALAYDKK YVVPKGRNAV WRNRDLFAQV FGYAMPETQV FGLSVPEASR LKNLAQPYYA ALHATSRDSK LWPMENWREL LQKLNQKQQC NVYLPWGNEA EKVRAEQIAD GLPFTIVCAK MNLLQAAYLL KHAVGIVGVD TGLLHLANAL EKPVVGIYTD TDPIKTGVQV SAIAKNVGNI GQIPTADLVY QTLMDCVSAD KG // ID Q5F659_NEIG1 Unreviewed; 432 AA. AC Q5F659; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 75. DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AAW90328.1}; GN ORFNames=NGO_1707 {ECO:0000313|EMBL:AAW90328.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90328.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the DNA photolyase family. CC {ECO:0000256|RuleBase:RU004182}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90328.1; -; Genomic_DNA. DR RefSeq; WP_003691893.1; NC_002946.2. DR RefSeq; YP_208740.1; NC_002946.2. DR ProteinModelPortal; Q5F659; -. DR EnsemblBacteria; AAW90328; AAW90328; NGO_1707. DR GeneID; 3281164; -. DR KEGG; ngo:NGO1707; -. DR PATRIC; 20337006; VBINeiGon24812_2043. DR HOGENOM; HOG000219123; -. DR KO; K01669; -. DR OMA; WGERYFR; -. DR OrthoDB; EOG6XWV2B; -. DR BioCyc; NGON242231:GI2G-1603-MONOMER; -. DR BRENDA; 4.1.99.3; 3590. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd. DR InterPro; IPR018394; DNA_photolyase_1_CS_C. DR InterPro; IPR006050; DNA_photolyase_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00875; DNA_photolyase; 1. DR Pfam; PF03441; FAD_binding_7; 1. DR SUPFAM; SSF48173; SSF48173; 1. DR SUPFAM; SSF52425; SSF52425; 1. DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1. DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lyase {ECO:0000313|EMBL:AAW90328.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 138 Photolyase/cryptochrome alpha/beta. FT {ECO:0000259|PROSITE:PS51645}. SQ SEQUENCE 432 AA; 48223 MW; 8DDE94456EED9CFE CRC64; MPSETALPLY ADTRAAHTLV WFRQNLRIRD NAALCAAVAE GSPVIGIWID DAETDNPRRA AFYRQSAAEL AQGLARRGIP LYTAASPAGL VRLAVRLNIR AVIADESHTF ADKLADNALW HELDKHGIAL TFVNDRSVFG KTDLTPDNGT AHTDFNRYRE VWLDRFSKQP PAGSDLFAAY RQPFPENLPA PPPAALSDGI FLPQNGGETA AWRQWRRFLE QAASYSVLKD FPSRKNTSLM GAYLSVGCIS PRLLARESLE RRLNAWADNI IRRDFFLQLA LQHADDDPSD GNPEHTLRLT LWQQGRTGIP IIDAAMRCLH KTGSLHPALR RLSADFFCHV LNLPRREGEI WFARQLTDFD AAINQGNWRL AASRHTCPDI AAASYRTDPD GTFIKRHIPE LAHLSADTVH TPWRFACSVD THGYPARPVA GV // ID Q5F504_NEIG1 Unreviewed; 61 AA. AC Q5F504; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90733.1}; GN ORFNames=NGO_2136 {ECO:0000313|EMBL:AAW90733.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90733.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90733.1; -; Genomic_DNA. DR RefSeq; WP_010951414.1; NC_002946.2. DR RefSeq; YP_209145.1; NC_002946.2. DR EnsemblBacteria; AAW90733; AAW90733; NGO_2136. DR GeneID; 3282785; -. DR KEGG; ngo:NGO2136; -. DR PATRIC; 20338121; VBINeiGon24812_2583. DR HOGENOM; HOG000027861; -. DR OMA; LECFRHN; -. DR OrthoDB; EOG6K405X; -. DR BioCyc; NGON242231:GI2G-2027-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 61 AA; 7213 MW; 7BB9FF5937D3CA6F CRC64; MEKTKCRLNR RLPELYAETA PPLECFRHNL YFSIICRLGA NRCLCPFQTA LSEMVARFLL Y // ID Q5F8U1_NEIG1 Unreviewed; 289 AA. AC Q5F8U1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89396.1}; GN ORFNames=NGO_0669 {ECO:0000313|EMBL:AAW89396.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89396.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89396.1; -; Genomic_DNA. DR RefSeq; WP_003691269.1; NC_002946.2. DR RefSeq; YP_207808.1; NC_002946.2. DR EnsemblBacteria; AAW89396; AAW89396; NGO_0669. DR GeneID; 3282059; -. DR KEGG; ngo:NGO0669; -. DR PATRIC; 20334434; VBINeiGon24812_0789. DR HOGENOM; HOG000261834; -. DR KO; K09977; -. DR OMA; QGFHAFE; -. DR OrthoDB; EOG60652J; -. DR BioCyc; NGON242231:GI2G-636-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR015003; DUF1853. DR Pfam; PF08907; DUF1853; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 289 AA; 32819 MW; C948F930335EF329 CRC64; MTDIRISMNY ALDALWWKLT SQPVRDLASL LTAPPLWQSG CELSVRELLG ERGFRYLLAL DADPAPLTDY LAQRAPFDHR LGIYAEELLA FWFTNAPHTK LHAYNLTVFS DGQTLGAADF VVSLNQQPYH IELACKYYGG DQVQNLRGLN PKDTLTDKAA KLVQQFQLVH TSQGKATLAA QDLPENPLPA SIVRGIGFFP QGFHAFEPPL NPYGWRGIYI QDWAEYGFER QEARYHLLDR MVYLAPARVA ETETLNATEI RRIDQGLIAV LECRPDGFWH EIERIMKAV // ID Q5F7M4_NEIG1 Unreviewed; 409 AA. AC Q5F7M4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 51. DE SubName: Full=Replication initiation factor family protein {ECO:0000313|EMBL:AAW89813.2}; GN ORFNames=NGO_1146 {ECO:0000313|EMBL:AAW89813.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89813.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89813.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89813; AAW89813; NGO_1146. DR PATRIC; 20335552; VBINeiGon24812_1341. DR HOGENOM; HOG000218820; -. DR OMA; FTIHENS; -. DR OrthoDB; EOG6MH585; -. DR BioCyc; NGON242231:GI2G-1059-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Initiation factor {ECO:0000313|EMBL:AAW89813.2}; KW Protein biosynthesis {ECO:0000313|EMBL:AAW89813.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 409 AA; 46649 MW; CB7EAE92EE61599D CRC64; MADALADGGA AATAVGCPPR LIGGEQNKTP NPKGAEKTEN QEFQFEYFSH FVSDGKGRFI EIPLRRGRDD GAFIDQITFT IHENSMTKVT GKGLVSDTEF VVRYSELLEE ILGFGITKKL PFKGKFFYQS CYQFGPDNVE YGKVHYGGQC ETMLVELNGT GCMAALPGWE NRLYEFLSKC VRPKITRIDV AHDFFNGEYT PDQAMLDHDN GHYDVHNMRP KSECRGTAWR NEDGSGKTFY IGKRGNSKFT RVYEKGRQLG DVDSPWVRFE GDIEIPLDVL LYSGSYLGGA YPICKEIFKT EAKRMEVKVK NVNLIFDVKL FHARNQVGKM VNFLRDIGWD DSRIVDELVK GVEGYPKGLQ PEQYDCKNQT QKFQYIHEEQ KAINALNIET LFDDLIEERE CAFPQDREW // ID Q5F5L2_NEIG1 Unreviewed; 94 AA. AC Q5F5L2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=GIY-YIG nuclease {ECO:0000313|EMBL:AAW90525.1}; GN ORFNames=NGO_1911 {ECO:0000313|EMBL:AAW90525.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90525.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90525.1; -; Genomic_DNA. DR RefSeq; WP_003692093.1; NC_002946.2. DR RefSeq; YP_208937.1; NC_002946.2. DR ProteinModelPortal; Q5F5L2; -. DR EnsemblBacteria; AAW90525; AAW90525; NGO_1911. DR GeneID; 3282262; -. DR KEGG; ngo:NGO1911; -. DR PATRIC; 20337548; VBINeiGon24812_2302. DR HOGENOM; HOG000285486; -. DR OMA; LIEEHNP; -. DR OrthoDB; EOG62K215; -. DR BioCyc; NGON242231:GI2G-1814-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 77 GIY-YIG. {ECO:0000259|PROSITE:PS50164}. SQ SEQUENCE 94 AA; 11366 MW; 119CFB9FF1EB13D0 CRC64; MQPAVYILAS QRNGTLYIGV TSDLVQRIYQ HREHLIEGFT SRYNVTMPVW YELHPTMESA ITREKQLKKW NRAWKLQLIE ENNVSWRDLW FDII // ID Q5F7V2_NEIG1 Unreviewed; 64 AA. AC Q5F7V2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89735.1}; GN ORFNames=NGO_1065 {ECO:0000313|EMBL:AAW89735.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89735.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89735.1; -; Genomic_DNA. DR RefSeq; WP_003688166.1; NC_002946.2. DR RefSeq; YP_208147.1; NC_002946.2. DR EnsemblBacteria; AAW89735; AAW89735; NGO_1065. DR GeneID; 3281120; -. DR KEGG; ngo:NGO1065; -. DR PATRIC; 20335364; VBINeiGon24812_1248. DR HOGENOM; HOG000239011; -. DR OrthoDB; EOG6M9F3Z; -. DR BioCyc; NGON242231:GI2G-980-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007423; DUF466. DR Pfam; PF04328; DUF466; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 7441 MW; FAE66A7DF7E86600 CRC64; MKHKLASWWK TIKLTANLMA GVPDYENYVA QQRKHNPNAP VMNKLQFQDY CRKRRCGANG GRCC // ID Q5F8M5_NEIG1 Unreviewed; 61 AA. AC Q5F8M5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89462.1}; GN ORFNames=NGO_0745 {ECO:0000313|EMBL:AAW89462.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89462.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89462.1; -; Genomic_DNA. DR RefSeq; WP_003706231.1; NC_002946.2. DR RefSeq; YP_207874.1; NC_002946.2. DR EnsemblBacteria; AAW89462; AAW89462; NGO_0745. DR GeneID; 3282458; -. DR KEGG; ngo:NGO0745; -. DR PATRIC; 20334630; VBINeiGon24812_0887. DR HOGENOM; HOG000263488; -. DR OMA; NQNREEN; -. DR OrthoDB; EOG6K9QNW; -. DR BioCyc; NGON242231:GI2G-702-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR021853; DUF3460. DR Pfam; PF11943; DUF3460; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 61 AA; 7394 MW; 3B1F49F348962FB4 CRC64; MYHYQSEATQ FLNRLIEEKP ELAQERLKNQ GLLWDVELNP EEQKNFESAK VAKKPYTYYQ D // ID Q5F7G5_NEIG1 Unreviewed; 556 AA. AC Q5F7G5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Long-chain fatty acid--CoA ligase {ECO:0000313|EMBL:AAW89872.1}; DE EC=6.2.1.3 {ECO:0000313|EMBL:AAW89872.1}; GN ORFNames=NGO_1213 {ECO:0000313|EMBL:AAW89872.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89872.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89872.1; -; Genomic_DNA. DR RefSeq; WP_003689655.1; NC_002946.2. DR RefSeq; YP_208284.1; NC_002946.2. DR ProteinModelPortal; Q5F7G5; -. DR EnsemblBacteria; AAW89872; AAW89872; NGO_1213. DR GeneID; 3281827; -. DR KEGG; ngo:NGO1213; -. DR PATRIC; 20335735; VBINeiGon24812_1426. DR HOGENOM; HOG000229983; -. DR KO; K01897; -. DR OMA; FIGDRMD; -. DR OrthoDB; EOG6MH5BV; -. DR BioCyc; NGON242231:GI2G-1124-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW89872.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 61429 MW; AF86C25A9804D4EC CRC64; MEKIWLESYE KGVSAEIDIT QYNSVSDVFR QSVEKFARLP AFQNMGKTLT YAETGKLATD FASYLQNVLK LPRGERVAIM MPNVLQYPIA LFGILQAGLV AVNTNPLYTP RELEHQLKDS GATAIIVLEN FANTLELVLP RTQIKHVIVA SVGEMFGLLK GSLINFIIRK IKKMVPEYRI RETVSFQTAL KEGAKHVFQP VALNREDTAL LQYTGGTTGV ARGAVLSHGN ICANMLQAKE WIKNQLREGK ETVIAALPLY HIFALTVNLM IFANAGSKIV LIANPRDMKG FIGELKKQRV NVFIGVNTLF NAMVNRPDFA EVDFSGLRLT LGGGMATQKA VAEKWKKITG TPIVEAYGLT EASPGVCCNP LNIESYSGSI GLPVPSTEVE LRDANGKEVP VGQPGELWVK GPQVMQGYWN RPEETAKAID ACGFLETGDI AVMDEKGRLK LVDRKKDLVV VSGFNVYPNE IEEFIAHHEK VMEVACIGVP NEKTGEALKV FVVKKDPSLT KEELTAFCRT GLTAYKVPKD IEFRDELPKS NVGKILRREL RQSAGK // ID Q5FA93_NEIG1 Unreviewed; 506 AA. AC Q5FA93; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88894.1}; GN ORFNames=NGO_0136 {ECO:0000313|EMBL:AAW88894.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88894.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88894.1; -; Genomic_DNA. DR RefSeq; WP_010950999.1; NC_002946.2. DR RefSeq; YP_207306.1; NC_002946.2. DR EnsemblBacteria; AAW88894; AAW88894; NGO_0136. DR GeneID; 3281295; -. DR KEGG; ngo:NGO0136; -. DR PATRIC; 20333183; VBINeiGon24812_0174. DR HOGENOM; HOG000276345; -. DR OMA; LVPISSW; -. DR OrthoDB; EOG6CGC8T; -. DR BioCyc; NGON242231:GI2G-124-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 96 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 208 225 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; 53467 MW; 2A12AA8A36E8D477 CRC64; MQLIDYSHSF FSVVPPFLAL ALAVITRRVL LSLGIGILVG VAFLVGGNPV DGLTHLKDMV VGLAWADGDW SLGKPKILVF LILLGIFTSL LTYSGSNQAF ADWAKRHIKN RCGAKMLTAC LVFVTFIDDY FHSLAVGAIA RPVTDKFKVS RAKLAYILDS TASPMCVLMP VSSWGASIIA TLAGLLVTYK ITEYTPMGTF VAMSLMNYYA LFALIMVFVV AWFSFDIGSM ARFEQAALNE AHDETAASDA TKGRVYALII PVLALIASTV SAMIYTGAQA SETFSILGAF ENTDVNTSLV FGGTCGVLAV VLCTFGTIKT ADYPKAVWQG AKSMFGAIAI LILAWLISTV VGEMHTGDYL STLVAGNIHP GFLPVILFLL ASVMAFATGT SWGTFGIMLP IAAAMAVKVE PALIIPCMSA VMAGAVCGDH CSPISDTTIL SSTGARCNHI DHVTSQLPYA LTVAAAAASG YLALGLTKSA LLGFGTTGIV LAVLIFLLKD KKRADV // ID Q5F7H6_NEIG1 Unreviewed; 31 AA. AC Q5F7H6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89861.2}; GN ORFNames=NGO_1201 {ECO:0000313|EMBL:AAW89861.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89861.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89861.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89861; AAW89861; NGO_1201. DR HOGENOM; HOG000027914; -. DR OrthoDB; EOG61P6Z7; -. DR BioCyc; NGON242231:GI2G-1113-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 31 AA; 3880 MW; BFBB7BBB29ADEE21 CRC64; MIMELLWQNI STSRRELTKL FLYKNFWGCT R // ID Q5F9K7_NEIG1 Unreviewed; 385 AA. AC Q5F9K7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AAW89130.1}; GN ORFNames=NGO_0386 {ECO:0000313|EMBL:AAW89130.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89130.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89130.1; -; Genomic_DNA. DR RefSeq; WP_003698156.1; NC_002946.2. DR RefSeq; YP_207542.1; NC_002946.2. DR ProteinModelPortal; Q5F9K7; -. DR EnsemblBacteria; AAW89130; AAW89130; NGO_0386. DR GeneID; 3281083; -. DR KEGG; ngo:NGO0386; -. DR PATRIC; 20333779; VBINeiGon24812_0467. DR HOGENOM; HOG000246415; -. DR KO; K01758; -. DR OMA; PPIYQVS; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; NGON242231:GI2G-365-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. 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:UP000000535}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT MOD_RES 197 197 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 385 AA; 42255 MW; 9BEA99CD3E1A6AB5 CRC64; MKFPTRTIHS GYDCDEHNRA LMPPIYQNSM FALHEIGENV PYRYSRLSNP TRQILEDTVA DLEHGAAGFA FSSGMAGIDA VWRTFLRPGD TIVAVADIYG GAYDLLVDVY QKWGVNVVFA DLGNPDNLDE LLKAHNVKLV WLEMPSNPLL RLVDIKALAA KAKAADALVG IDNTFATPYL QQPLDMGCDF AFHSATKYLC GHSDVLMGIV VAKTKELAQP LHDMMVHTGA IAGPTDCWLV LRGIKTLALR MEAHCKNALE IARRLEAHPA IEKVFHPGLP SHEHYALAQA QMPKGIGGVV TVYLKNDTRE AANSVIKNMK LVKMTSSLGG VESLVNHCYS QSHSGVPHNV KMEMGIRVGL LRFSIGIEDV DDIWNDISAA LDTTL // ID Q5F5Q5_NEIG1 Unreviewed; 112 AA. AC Q5F5Q5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90482.1}; GN ORFNames=NGO_1861 {ECO:0000313|EMBL:AAW90482.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90482.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90482.1; -; Genomic_DNA. DR RefSeq; WP_003690303.1; NC_002946.2. DR RefSeq; YP_208894.1; NC_002946.2. DR EnsemblBacteria; AAW90482; AAW90482; NGO_1861. DR GeneID; 3282338; -. DR KEGG; ngo:NGO1861; -. DR PATRIC; 20337410; VBINeiGon24812_2236. DR OrthoDB; EOG6FV87D; -. DR BioCyc; NGON242231:GI2G-1766-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 112 AA; 12059 MW; 080104DEC08E5CE0 CRC64; MPSEPSDGIF DALAVYGRGA GAGKYPYRHC RYTVTLKPAI PAQAGIRICR DSLKSGGGGM VLQINDVDTN SGEFAIYTAQ DASVKLDLLK MELKHCKEML EQKTKKSSCS AS // ID Q5F733_NEIG1 Unreviewed; 445 AA. AC Q5F733; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. DE RecName: Full=Transporter {ECO:0000256|RuleBase:RU003732}; GN ORFNames=NGO_1355 {ECO:0000313|EMBL:AAW90004.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90004.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90004.1; -; Genomic_DNA. DR RefSeq; WP_003695694.1; NC_002946.2. DR RefSeq; YP_208416.1; NC_002946.2. DR ProteinModelPortal; Q5F733; -. DR EnsemblBacteria; AAW90004; AAW90004; NGO_1355. DR GeneID; 3282052; -. DR KEGG; ngo:NGO1355; -. DR PATRIC; 20336093; VBINeiGon24812_1595. DR HOGENOM; HOG000033129; -. DR KO; K03308; -. DR OMA; MTLESMP; -. DR OrthoDB; EOG6PGK51; -. DR BioCyc; NGON242231:GI2G-1269-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 48333 MW; F79493BF906FB707 CRC64; MSNHTSWSSK IGFVLAAAGS AIGLGAIWKF PYTAGTNGGA VFFLLFLIFT VLVALPVQLA EFYIGRTGGK NAVDSFRVLR PGTQWLWVGR MGVAACFILL SFYSVVGGWV LNYVVHSFTG AIHAGADFEA LFGTTISNPA GSLSYQALFM LITVWVVKGG ISDGIEKANR YLMPGLFILF IALAVRSLTL PDAMEGVSFL LKPNWSYFKA DTMITALGQA FFALSIGVSA MITYASYLGK DQDMFRSGHT IMWMNLLVSL LAGLVIFPAV FAFGFEPNQG PGLIFIVLPA VFMKMPFGTV LFAVFMLLVV FATLTSAFSM LETVIASTIR QDERKRKKHT WLIGTAIFIV GIPSALSFGA WGEFKVFGKT IFDLWDYVIS AVIMPIGALS VSIFTAWIQD KQSVLKDAGA GSTVPRAVLL LWLNTLRYLA PIAIIIVFVN SLGIL // ID Q5F9T8_NEIG1 Unreviewed; 81 AA. AC Q5F9T8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89049.1}; GN ORFNames=NGO_0302 {ECO:0000313|EMBL:AAW89049.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89049.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89049.1; -; Genomic_DNA. DR RefSeq; WP_003687680.1; NC_002946.2. DR RefSeq; YP_207461.1; NC_002946.2. DR REBASE; 10869; M.NgoAXIIIP. DR EnsemblBacteria; AAW89049; AAW89049; NGO_0302. DR GeneID; 3281680; -. DR KEGG; ngo:NGO0302; -. DR HOGENOM; HOG000071239; -. DR OMA; WLLASEK; -. DR OrthoDB; EOG6SBTBR; -. DR BioCyc; NGON242231:GI2G-282-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 81 AA; 9690 MW; 00603C31BCF4688C CRC64; MRLSDYILNN KININNLSDK QVQEIIDYFS SEIDDWLLAS EKELKDYDVY LYKLVLDGQQ YVQGIRKSVL YDFLMENQKD S // ID Q5F9L2_NEIG1 Unreviewed; 143 AA. AC Q5F9L2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 52. DE SubName: Full=Cyclase {ECO:0000313|EMBL:AAW89125.2}; GN ORFNames=NGO_0381 {ECO:0000313|EMBL:AAW89125.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89125.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89125.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F9L2; -. DR EnsemblBacteria; AAW89125; AAW89125; NGO_0381. DR PATRIC; 20333767; VBINeiGon24812_0461. DR HOGENOM; HOG000261730; -. DR OMA; LREDACK; -. DR OrthoDB; EOG6RFZZ5; -. DR BioCyc; NGON242231:GI2G-360-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 134 Polyketide_cyc. FT {ECO:0000259|Pfam:PF03364}. SQ SEQUENCE 143 AA; 16721 MW; 0C931798DFB94DF4 CRC64; MKKVEKNILV LHGADKMFEL VDKVEDYPHF LPWYSKTEVI GRSGNELKAR LFMDYMRVRQ SFATHNRNIP GREIRMELLE GPFKTLRGTW KFIDLGDDMC KIEFNLEYDF SNAVLSALIS PVFNHLSATL VEAFVKEADR RYA // ID Q5F777_NEIG1 Unreviewed; 718 AA. AC Q5F777; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:AAW89960.1}; GN ORFNames=NGO_1308 {ECO:0000313|EMBL:AAW89960.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89960.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89960.1; -; Genomic_DNA. DR RefSeq; WP_003705879.1; NC_002946.2. DR RefSeq; YP_208372.1; NC_002946.2. DR ProteinModelPortal; Q5F777; -. DR DNASU; 3281878; -. DR EnsemblBacteria; AAW89960; AAW89960; NGO_1308. DR GeneID; 3281878; -. DR KEGG; ngo:NGO1308; -. DR PATRIC; 20335977; VBINeiGon24812_1539. DR HOGENOM; HOG000018299; -. DR KO; K01139; -. DR OMA; GIYKKMR; -. DR OrthoDB; EOG6SV551; -. DR BioCyc; NGON242231:GI2G-1223-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase 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; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89960.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 642 718 ACT. {ECO:0000259|PROSITE:PS51671}. SQ SEQUENCE 718 AA; 80158 MW; 8A74BEEE88FF7BCB CRC64; MPAPQPSAPY DPLTAEARTL LFHTASYLKP EQQAELEKAV AYAFRAHDGQ TRKSGDPYIT HPIAVATQLA LWHMDIQGLC AGVMHDVLED TGVTKGEMAA VFGNTVAEMV DGLSKLEKLK FEDHAEHQAE SFRKLILAMT KDVRVIVVKL ADRLHNMRTL GSMRPDKRRR IARETLEIYA QIANRIGLNN AYRELQDLSF QNLHPNRYET LKKAMDKSRK NRQDVVGKVL RAFGQRLVGA NIEAKIKGRE KNLYGIHQKM MAKKLRFAEV MDIYGFRVIV NSIPACYAAL GTLHTLYQPK PGRFKDYIAI PKSNGYQSLH TILVGPYGLP IEVQIRTREM DAVAEGGIVG HWSYKSDSKT VDQAVLHTNQ WLKNILDLQA SSANAIEFLE HVKVDLFPNE IYILTPKGKI LTLPKGATPV DFAYAVHTDI GHKTVAARVN NVMMPLRTKL KTGDSVEIIT SEHAKPNPAW LNFAVSGRAR SAIRQYIKNL NRHDAVVLGE SLLQKALSSL LPKDVLLSDG IKEKYLADLN DKQTSFEEVL YNVGMGHTLP VYVAMHIAEL AGEHFGSEVR LSSIKVDGQE SGHIHFAECC HPVPGDSIRL LLVKGKGMII HRDTCPTLLK SDPEQQLDAD WENMNGQNYR VGLQVQSEDS HGLLALMAQA ISDSGADIES VETPSKSQSG TEGFVEFKFL LKVKNLDQLN QIIQNLHSIP YIRKVIRS // ID Q5F9A4_NEIG1 Unreviewed; 473 AA. AC Q5F9A4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Phage terminase, large subunit {ECO:0000313|EMBL:AAW89233.1}; GN ORFNames=NGO_0495 {ECO:0000313|EMBL:AAW89233.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89233.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89233.1; -; Genomic_DNA. DR RefSeq; WP_003697216.1; NC_002946.2. DR RefSeq; YP_207645.1; NC_002946.2. DR EnsemblBacteria; AAW89233; AAW89233; NGO_0495. DR GeneID; 3282954; -. DR KEGG; ngo:NGO0495; -. DR PATRIC; 20334032; VBINeiGon24812_0588. DR HOGENOM; HOG000262140; -. DR OMA; EFIHASY; -. DR OrthoDB; EOG61ZTCX; -. DR BioCyc; NGON242231:GI2G-473-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006517; Arc_phage_psiM2_terminase_lsu. DR InterPro; IPR004921; Terminase_lsu. DR Pfam; PF03237; Terminase_6; 1. DR TIGRFAMs; TIGR01630; psiM2_ORF9; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 79 451 Terminase_6. {ECO:0000259|Pfam:PF03237}. SQ SEQUENCE 473 AA; 52434 MW; 39F1A2C4E1D2BAFF CRC64; MALGQFDDVE TSVIRSLSSA SLYMFTRRMF YQRRGYVWQR ANHHAPICNA LERVFNGETK RLIINIPPRY SKTEIAVVNF IAWAMGRVPD CEFIHASYSA ALAVNNSVQI RNLVQHEEYR AIFPDLALAG ESGHHWKTTA GGVMYATGAG GTITGFGAGR HREGFGGCII IDDPHKADEA RSEVRRQNVI DWFQNTVESR KNSPDTPIIL IMQRLHEKDL AGWLLDGGNG EEWEHLCLPA IQEDGTALWP EKHDIETLRR MEQAAPYVFA GQYLQKPAPP DGGTFKPDNL QFVKALPAGN IRWVRAWDLA STANGGDYTA GGRLGVTEDG RYIIANVVRG RYGADERDRI LRNTAQKDGV KTKISIPQDP GQAGKSQTLY LTRQLAGFSV SAGPESGDKV TRAGPFAAQV NIGNVMVLDD GTWDTDALIA EMRMFPNGRH DDQIDCLGRA FGELLDTRTG MIDFLRSQVE AVK // ID Q5F9R7_NEIG1 Unreviewed; 164 AA. AC Q5F9R7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000313|EMBL:AAW89070.1}; GN ORFNames=NGO_0323 {ECO:0000313|EMBL:AAW89070.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89070.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89070.1; -; Genomic_DNA. DR RefSeq; WP_003687713.1; NC_002946.2. DR RefSeq; YP_207482.1; NC_002946.2. DR ProteinModelPortal; Q5F9R7; -. DR EnsemblBacteria; AAW89070; AAW89070; NGO_0323. DR GeneID; 3281734; -. DR KEGG; ngo:NGO0323; -. DR PATRIC; 20333635; VBINeiGon24812_0395. DR HOGENOM; HOG000217741; -. DR KO; K00950; -. DR OMA; DWFLNAA; -. DR OrthoDB; EOG6XHC8G; -. DR BioCyc; NGON242231:GI2G-305-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:InterPro. 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:UP000000535}; KW Kinase {ECO:0000313|EMBL:AAW89070.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89070.1}. FT DOMAIN 91 102 HPPK. {ECO:0000259|PROSITE:PS00794}. SQ SEQUENCE 164 AA; 18217 MW; E4EEA74B51972D4D CRC64; MNNRHFAVIA LGSNLDNPAQ QIRGALDALS SHPDIRLEQA SSLYMTAPVG YDNQPDFINA VCTVSTTLDG IALLAELNRI EADFGRERSF RNAPRTLDLD IIDFDGISSD DPRLTLPHPR AHERSFVIRP LAEILPDFIL GKYGKVVELS KRLGNQGIRL LPDR // ID Q5F4Y2_NEIG1 Unreviewed; 264 AA. AC Q5F4Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Inositol monophosphatase {ECO:0000313|EMBL:AAW90755.1}; GN ORFNames=NGO_2161 {ECO:0000313|EMBL:AAW90755.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90755.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90755.1; -; Genomic_DNA. DR RefSeq; WP_003687170.1; NC_002946.2. DR RefSeq; YP_209167.1; NC_002946.2. DR ProteinModelPortal; Q5F4Y2; -. DR EnsemblBacteria; AAW90755; AAW90755; NGO_2161. DR GeneID; 3282763; -. DR KEGG; ngo:NGO2161; -. DR PATRIC; 20338176; VBINeiGon24812_2610. DR HOGENOM; HOG000282238; -. DR KO; K01092; -. DR OMA; YLHGGQK; -. DR OrthoDB; EOG6QK4W4; -. DR BioCyc; NGON242231:GI2G-2049-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 264 AA; 29436 MW; 31CCD99820FB972E CRC64; MLHRLQKVVR HIAQTEIMPR FLNTPSRRKE DGSMLSEADI AAQTAFAAAL PLLIDCPMLG EEMSRQEQSA LWEQYSGEKG LWIVDPIDGT NNFVNGLPHF AVSVAFVRNG RAELGVIYNP VSGECFYAER GQGAFLNGTR LPLRLVDKKL NEAIAGVEIK YLRSGKLSSR MSTLAPFGTI RSMGSSTLDW CYLACGRYDV YVHGGQKLWD YAAGALIFEE AGGRLTTLEG DGFWSGEHVF KRSVVAALEP KLFERWVGWI RENQ // ID Q5FA70_NEIG1 Unreviewed; 155 AA. AC Q5FA70; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88917.1}; GN ORFNames=NGO_0161 {ECO:0000313|EMBL:AAW88917.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88917.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88917.1; -; Genomic_DNA. DR RefSeq; WP_010356746.1; NC_002946.2. DR RefSeq; YP_207329.1; NC_002946.2. DR EnsemblBacteria; AAW88917; AAW88917; NGO_0161. DR GeneID; 3281372; -. DR KEGG; ngo:NGO0161; -. DR PATRIC; 20333245; VBINeiGon24812_0205. DR HOGENOM; HOG000218876; -. DR OMA; MQINNIS; -. DR OrthoDB; EOG6QCD90; -. DR BioCyc; NGON242231:GI2G-147-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 155 AA; 18505 MW; C7AFCFE162F83339 CRC64; MQINNISDEQ VMIVKMSCYL KKDEIFKNIE RYGYQSSDIK KINPPFPLNI LPVPKPYYFY LYDTHLNQIY DLAWSCNDFL MFEIFILDRE SIKYIDKDKL FKSGETLYSN FKSIKNQCKN YFFCGFDFDA PYFKSGVSQV ADYNFVPDAF SLFFI // ID Q5F6Q1_NEIG1 Unreviewed; 53 AA. AC Q5F6Q1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90136.1}; GN ORFNames=NGO_1498 {ECO:0000313|EMBL:AAW90136.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90136.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90136.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90136; AAW90136; NGO_1498. DR PATRIC; 20336462; VBINeiGon24812_1778. DR HOGENOM; HOG000071341; -. DR OrthoDB; EOG647V87; -. DR BioCyc; NGON242231:GI2G-1402-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 5609 MW; D2E00DD407EA3FC2 CRC64; MPQLGECPLP GPPPRGRERI AADFAVAGGL KSNLDLPLIS GRMKNKKQPA QAD // ID Q5F760_NEIG1 Unreviewed; 45 AA. AC Q5F760; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89977.1}; GN ORFNames=NGO_1327 {ECO:0000313|EMBL:AAW89977.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89977.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89977.1; -; Genomic_DNA. DR RefSeq; WP_010951241.1; NC_002946.2. DR RefSeq; YP_208389.1; NC_002946.2. DR EnsemblBacteria; AAW89977; AAW89977; NGO_1327. DR GeneID; 3281931; -. DR KEGG; ngo:NGO1327; -. DR OrthoDB; EOG6N0HVW; -. DR BioCyc; NGON242231:GI2G-1240-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 13 30 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 45 AA; 5366 MW; F97964099304A159 CRC64; MFLIDYKTNG LNQYPYISFF IILLFIHPIG QTDFKDEKPI LFTPI // ID Q5F7N8_NEIG1 Unreviewed; 64 AA. AC Q5F7N8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89799.1}; GN ORFNames=NGO_1132 {ECO:0000313|EMBL:AAW89799.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89799.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89799.1; -; Genomic_DNA. DR RefSeq; WP_003693991.1; NC_002946.2. DR RefSeq; YP_208211.1; NC_002946.2. DR EnsemblBacteria; AAW89799; AAW89799; NGO_1132. DR GeneID; 3282232; -. DR KEGG; ngo:NGO1132; -. DR PATRIC; 20335522; VBINeiGon24812_1327. DR HOGENOM; HOG000071321; -. DR OMA; SEYLDPQ; -. DR OrthoDB; EOG68SW3F; -. DR BioCyc; NGON242231:GI2G-1044-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 64 AA; 7876 MW; BDE7E9B7D64ED19C CRC64; MDSEYLDPQQ CADILSVKKR TFLERYAPRP DFPARISVSK KRFWWKKEEV EGWLDRQKEK RPMM // ID Q5F9H8_NEIG1 Unreviewed; 107 AA. AC Q5F9H8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Periplasmic protein {ECO:0000313|EMBL:AAW89159.1}; GN ORFNames=NGO_0416 {ECO:0000313|EMBL:AAW89159.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89159.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89159.1; -; Genomic_DNA. DR RefSeq; WP_003687855.1; NC_002946.2. DR RefSeq; YP_207571.1; NC_002946.2. DR EnsemblBacteria; AAW89159; AAW89159; NGO_0416. DR GeneID; 3283000; -. DR KEGG; ngo:NGO0416; -. DR PATRIC; 20333843; VBINeiGon24812_0499. DR HOGENOM; HOG000218872; -. DR OrthoDB; EOG6KT2S0; -. DR BioCyc; NGON242231:GI2G-394-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256248. FT COILED 15 42 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 107 AA; 11812 MW; 876F1DBB72CA04FC CRC64; MKKCILGILT ACAAMPAFAD RISDLEARLA QLEHRVAVLE SGGNTVKIDL FGSNSTMYVC SVTPFQKTFE ASDRNEGVAR QKVRQACNRE TSAMFCGDEA IRCRKFD // ID Q5F949_NEIG1 Unreviewed; 316 AA. AC Q5F949; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89288.1}; GN ORFNames=NGO_0554 {ECO:0000313|EMBL:AAW89288.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89288.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89288.1; -; Genomic_DNA. DR RefSeq; WP_003706105.1; NC_002946.2. DR RefSeq; YP_207700.1; NC_002946.2. DR EnsemblBacteria; AAW89288; AAW89288; NGO_0554. DR GeneID; 3282103; -. DR KEGG; ngo:NGO0554; -. DR PATRIC; 20334160; VBINeiGon24812_0652. DR HOGENOM; HOG000071305; -. DR OMA; FGEWAPR; -. DR OrthoDB; EOG6GTZJ6; -. DR BioCyc; NGON242231:GI2G-528-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 316 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255557. SQ SEQUENCE 316 AA; 33400 MW; 3B6CFB5601348010 CRC64; MKASQLTLAV LLAAAFGSAY AVEVKGGDSS KGQLIQAAES DFLPFGSGAA DIKVSTGNGL SKSINLEAGP AQRIRNKYGN APINGGNQNT NVNGAANSRY LQPGDINPIA GWFSKTRLAQ VWYEKRANNT EVFSVRQMAD PLLPIAPKFG GMTFAKVPTA ATNVFFGEWA PRKGNSNQIT NSTDLNMNDG NRTVWFVGEN PTKNTRNLTA VTYNVVGINK HTPGKNDFYT GEITATFGTG DKGFMSGELE HTDDGELSFN GVEITNADGS FNSIPGRNNE GIKGQFYGNG AAAMAGYATR GTDNKGDDVA FGGAKK // ID Q5F586_NEIG1 Unreviewed; 104 AA. AC Q5F586; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Alanine aminotransferase {ECO:0000313|EMBL:AAW90651.1}; GN ORFNames=NGO_2043 {ECO:0000313|EMBL:AAW90651.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90651.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90651.1; -; Genomic_DNA. DR RefSeq; WP_010951389.1; NC_002946.2. DR RefSeq; YP_209063.1; NC_002946.2. DR ProteinModelPortal; Q5F586; -. DR EnsemblBacteria; AAW90651; AAW90651; NGO_2043. DR GeneID; 3282704; -. DR KEGG; ngo:NGO2043; -. DR PATRIC; 20337881; VBINeiGon24812_2463. DR HOGENOM; HOG000071361; -. DR KO; K00018; -. DR OMA; NCGRGGP; -. DR OrthoDB; EOG6VXFC3; -. DR BioCyc; NGON242231:GI2G-1945-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 4: Predicted; KW Aminotransferase {ECO:0000313|EMBL:AAW90651.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90651.1}. FT DOMAIN 3 73 2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}. SQ SEQUENCE 104 AA; 11093 MW; 03E51AA36134511B CRC64; MSGENELRQM KPGAVLINCG RGGPVDENAL LAALKYGQIG GAGVDVLTEE PPRGGNPLLN ARLPNLIVTP HTAWASREAL DRLFEILLAN IHAFVKGEAQ NRVV // ID Q5F990_NEIG1 Unreviewed; 93 AA. AC Q5F990; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89247.1}; GN ORFNames=NGO_0509 {ECO:0000313|EMBL:AAW89247.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89247.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89247.1; -; Genomic_DNA. DR RefSeq; WP_010951066.1; NC_002946.2. DR RefSeq; YP_207659.1; NC_002946.2. DR ProteinModelPortal; Q5F990; -. DR EnsemblBacteria; AAW89247; AAW89247; NGO_0509. DR GeneID; 3282940; -. DR KEGG; ngo:NGO0509; -. DR PATRIC; 20334060; VBINeiGon24812_0602. DR HOGENOM; HOG000258408; -. DR OMA; DNDIVET; -. DR OrthoDB; EOG67DPPK; -. DR BioCyc; NGON242231:GI2G-487-MONOMER; -. DR Proteomes; UP000000535; 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 SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 34 91 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 93 AA; 10186 MW; A5A96B8E830018AF CRC64; MESRTLILRH LDALCDTPAQ AANMRLRAGL MMHIADTVRE NGWTQKQAAE HCGLTRPRIN DLLNGKIDKF SLDALVNINA GLGQCISLSF APA // ID Q5FA00_NEIG1 Unreviewed; 391 AA. AC Q5FA00; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 69. DE SubName: Full=Coproporphyrinogen III oxidase {ECO:0000313|EMBL:AAW88987.1}; GN ORFNames=NGO_0234 {ECO:0000313|EMBL:AAW88987.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88987.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88987.1; -; Genomic_DNA. DR RefSeq; WP_003706670.1; NC_002946.2. DR RefSeq; YP_207399.1; NC_002946.2. DR ProteinModelPortal; Q5FA00; -. DR EnsemblBacteria; AAW88987; AAW88987; NGO_0234. DR GeneID; 3281485; -. DR KEGG; ngo:NGO0234; -. DR PATRIC; 20333417; VBINeiGon24812_0290. DR HOGENOM; HOG000015379; -. DR KO; K02495; -. DR OMA; PFCVRKC; -. DR OrthoDB; EOG683S9D; -. DR BioCyc; NGON242231:GI2G-218-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 233 Elp3. {ECO:0000259|SMART:SM00729}. SQ SEQUENCE 391 AA; 43412 MW; F1460B83BD2F31CF CRC64; MHTISFPNRT RLTALPPLSL YIHIPWCIKK CPYCDFNSHS LKNGLPEAAY IDALLTDLQL ELPNIWGRPV ETIFFGGGTP SLFQAESIDR LLSGVRSLLR LQPEAEITLE ANPGTVEIEK FQGFKDAGIT RLSIGVQSFN DDMLSRLGRV HNGKEALTAI ATALKLFDKV NIDLMYALPN QTVQTALDDV QTAIATDATH ISAYHLTMEP NTPFGHTPPK GLPQDEAALD IEDAVHGTLE GAGFIHYETS AFAKPTMQCR HNLNYWQFGD YLGIGAGAHG KISYPDRIER TVRRRHPNDY LALMQSQPGE AVERKTVAAE DLPFEFMMNA LRLTDGVPAA MLQERTGVPA AKIMVQIETA RQKGLLETDP TVFRPTEKGR LFLNDLLQCF L // ID Q5F6W6_NEIG1 Unreviewed; 90 AA. AC Q5F6W6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90071.1}; GN ORFNames=NGO_1428 {ECO:0000313|EMBL:AAW90071.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90071.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90071.1; -; Genomic_DNA. DR RefSeq; WP_003689282.1; NC_002946.2. DR RefSeq; YP_208483.1; NC_002946.2. DR EnsemblBacteria; AAW90071; AAW90071; NGO_1428. DR GeneID; 3281745; -. DR KEGG; ngo:NGO1428; -. DR PATRIC; 20336275; VBINeiGon24812_1686. DR HOGENOM; HOG000218804; -. DR OrthoDB; EOG6J1DH6; -. DR BioCyc; NGON242231:GI2G-1336-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 90 AA; 10365 MW; 76343B5719B75CF1 CRC64; MKKTSKYLIY TAAFTSFCFA FQENRSEAKQ PDITLSASLC EQFNMLNAKD MDTEQVSLSK ECDIIESSHD WEKEYGNLNE QEMLAGVVYE // ID Q5FAE0_NEIG1 Unreviewed; 388 AA. AC Q5FAE0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 57. DE SubName: Full=Glycosyl transferase family 1 {ECO:0000313|EMBL:AAW88847.1}; GN ORFNames=NGO_0086 {ECO:0000313|EMBL:AAW88847.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88847.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88847.1; -; Genomic_DNA. DR RefSeq; WP_003704930.1; NC_002946.2. DR RefSeq; YP_207259.1; NC_002946.2. DR ProteinModelPortal; Q5FAE0; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAW88847; AAW88847; NGO_0086. DR GeneID; 3282285; -. DR KEGG; ngo:NGO0086; -. DR PATRIC; 20333059; VBINeiGon24812_0113. DR HOGENOM; HOG000218778; -. DR OMA; YDVETVC; -. DR OrthoDB; EOG68M4CB; -. DR BioCyc; NGON242231:GI2G-76-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88847.1}. SQ SEQUENCE 388 AA; 44141 MW; 0137F30960C424B4 CRC64; MNITIAAPYC SLPSEPHFNR FWYLAELLSQ SHDVLLITSN FKHYDKSFRR PEDAKAASQG RLKVMLLEES GYSKNVSLGR VTSHHRFVKH FEKWLENCRP GEQDVVYSAY PLIATNLLLG KHKARLGYKL IVDVQDVWPE SFSSVVPFLK KIPHNLLPFA SRANRAYRYA DALVAVSQTY LDRAKEANPN VPGEVVYIGA DFAAIAPPPR FRSKTVRFFY LGTLSYNYDV ETVCKGVRKL LDDGENVELH IMGGGPDLDR LKQYACDGIK FYGYIPYAEM MSVAKGCDIA VNAIHSYAMQ SITNKLSDYM ALQKPILNSQ VHDEVAEVLT LLPHENYRSG DVDGFVQAAK DILKRKNDPV QSDEIVRRFR HDISYRKIVN LIERLANE // ID Q5F8B3_NEIG1 Unreviewed; 312 AA. AC Q5F8B3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 72. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_0873 {ECO:0000313|EMBL:AAW89574.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89574.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89574.1; -; Genomic_DNA. DR RefSeq; WP_003693270.1; NC_002946.2. DR RefSeq; YP_207986.1; NC_002946.2. DR ProteinModelPortal; Q5F8B3; -. DR REBASE; 3462; M.NgoAIV. DR DNASU; 3281993; -. DR EnsemblBacteria; AAW89574; AAW89574; NGO_0873. DR GeneID; 3281993; -. DR KEGG; ngo:NGO0873; -. DR PATRIC; 20334919; VBINeiGon24812_1029. DR HOGENOM; HOG000225505; -. DR KO; K00558; -. DR OMA; ENYRNHI; -. DR OrthoDB; EOG6JDW86; -. DR BioCyc; NGON242231:GI2G-816-MONOMER; -. DR Proteomes; UP000000535; 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; 2. 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW89574.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW89574.1}. FT DOMAIN 4 212 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. FT DOMAIN 257 306 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 312 AA; 34688 MW; 7A2A376380561C30 CRC64; MQFTSLEICA GAGGQALGLE RAGFSHVALI EIEPSACQTL RLNRPDWNVI EGDVRLFQGE GYDGIDLLAG GVPCPPFSKA GKQLGKDDER DLFPEAIRLA KETDPKAIML ENVRGLLDPK FENYRNHITE QFAKLGYLGQ WKLLYAADYG VSQLRPRVLF VALKNEYTNF FKWPEPNSEQ PKTVGELLFD LMSENNWQGA HNWRLKAAQI APTLVGGSKK HGGADLGPTR SKRAWAELGV DGSGLWDSAP PEDFSGMPRL TVRMTARIQG FPDDWQFFGK KTPMYRQIGN AFPPPVAEAV GRQIIKALKK EN // ID Q5F6D9_NEIG1 Unreviewed; 167 AA. AC Q5F6D9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Putative phage associated protein {ECO:0000313|EMBL:AAW90248.1}; GN ORFNames=NGO_1620 {ECO:0000313|EMBL:AAW90248.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90248.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90248.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90248; AAW90248; NGO_1620. DR PATRIC; 20336780; VBINeiGon24812_1935. DR HOGENOM; HOG000071218; -. DR OrthoDB; EOG6TBHF7; -. DR BioCyc; NGON242231:GI2G-1517-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 167 AA; 18759 MW; 54883522EF5F02A6 CRC64; MLMPDGRPYL ISRRYTASLH SKSQLATDLK SWRGRDFTPE ERDNFDLRNI LGKPCLLSIA HQESRDGKTT YANIPAISNK MKSYTPKHPD NAVFAFDLSD PDWANYGLLN EKLREQIAKS PEYAEAVNGR QPPAPPQKQA QAAEGRPEHP QGNAAPAEDI EDDIPFN // ID Q5FAI6_NEIG1 Unreviewed; 225 AA. AC Q5FAI6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 76. DE SubName: Full=Glycoprotease {ECO:0000313|EMBL:AAW88801.1}; GN ORFNames=NGO_0032 {ECO:0000313|EMBL:AAW88801.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88801.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88801.1; -; Genomic_DNA. DR RefSeq; WP_003687250.1; NC_002946.2. DR RefSeq; YP_207213.1; NC_002946.2. DR ProteinModelPortal; Q5FAI6; -. DR EnsemblBacteria; AAW88801; AAW88801; NGO_0032. DR GeneID; 3281867; -. DR KEGG; ngo:NGO0032; -. DR PATRIC; 20332894; VBINeiGon24812_0032. DR HOGENOM; HOG000052125; -. DR KO; K14742; -. DR OMA; LFHQEAG; -. DR OrthoDB; EOG6D8B8B; -. DR BioCyc; NGON242231:GI2G-29-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW88801.1}; KW Protease {ECO:0000313|EMBL:AAW88801.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 41 134 Peptidase_M22. FT {ECO:0000259|Pfam:PF00814}. SQ SEQUENCE 225 AA; 23876 MW; 4B503D0FDA4D21E2 CRC64; MQADFNRPVL AVDTGTSYLS LALRADGEIR LFHQEVGIRQ SELILPEIRT LFRNAGITAA DLGAIVYAKG PGAFTGLRIG IGVAQGLATP FDTPLIGIPT LDAAASLPPP QSCILAAADA RMGEVFYAWF DTLNRRRLSD YQVGRAADIA LPEGYVFSDG IGSAFALENR PPFSGKPDMP TAADFLALAL GGGYPATGAA HAELLYVRNK IALTAKEQAE RKART // ID Q5F8I5_NEIG1 Unreviewed; 315 AA. AC Q5F8I5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 58. DE SubName: Full=Stomatin 2 {ECO:0000313|EMBL:AAW89502.1}; GN ORFNames=NGO_0788 {ECO:0000313|EMBL:AAW89502.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89502.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89502.1; -; Genomic_DNA. DR RefSeq; WP_003688626.1; NC_002946.2. DR RefSeq; YP_207914.1; NC_002946.2. DR ProteinModelPortal; Q5F8I5; -. DR EnsemblBacteria; AAW89502; AAW89502; NGO_0788. DR GeneID; 3281955; -. DR KEGG; ngo:NGO0788; -. DR PATRIC; 20334724; VBINeiGon24812_0934. DR HOGENOM; HOG000217038; -. DR OMA; REANEWG; -. DR OrthoDB; EOG6J48MH; -. DR BioCyc; NGON242231:GI2G-742-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 17 175 PHB. {ECO:0000259|SMART:SM00244}. SQ SEQUENCE 315 AA; 34477 MW; A235E500E95D2D51 CRC64; MEFFIILLAA VAVFGFKSFV VIPQQEVHVV ERLGRFHRAL TAGLNILIPF IDRVAYRHSL KEIPLDVPSQ VCITRDNTQL TVDGIIYFQV TDPKLASYGS SNYIMAITQL AQTTLRSVIG RMELDKTFEE RDEINSTVVS ALDEAAGAWG VKVLRYEIKD LVPPQEILRA MQAQITAERE KRARIAESEG RKIEQINLAS GQREAEIQQS EGEAQAAVNA SNAEKIARIN RAKGEAESLR LVAEANAEAI RQIAAALQTQ GGADAVNLKI AEQYVAAFNN LAKESNTLIM PANVADIGSL ISAGMKIIDS SKTAK // ID Q5F8N3_NEIG1 Unreviewed; 98 AA. AC Q5F8N3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89454.1}; GN ORFNames=NGO_0736 {ECO:0000313|EMBL:AAW89454.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89454.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89454.1; -; Genomic_DNA. DR RefSeq; WP_003688700.1; NC_002946.2. DR RefSeq; YP_207866.1; NC_002946.2. DR EnsemblBacteria; AAW89454; AAW89454; NGO_0736. DR GeneID; 3282882; -. DR KEGG; ngo:NGO0736; -. DR HOGENOM; HOG000071293; -. DR OrthoDB; EOG6SR94H; -. DR BioCyc; NGON242231:GI2G-694-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 11844 MW; CB1A0B16CB3380A8 CRC64; MNKNIIYIFS LLITIVIFFI FEKNVISKIS FDYNKKEFLI SDITNFNWDH VKLYIINSDF QKIVFYDKGK IVFEELIELD RKGKVLPQYL FDSYLKNV // ID Q5F796_NEIG1 Unreviewed; 446 AA. AC Q5F796; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=GTP-binding protein {ECO:0000313|EMBL:AAW89941.1}; GN ORFNames=NGO_1287 {ECO:0000313|EMBL:AAW89941.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89941.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89941.1; -; Genomic_DNA. DR RefSeq; WP_003691594.1; NC_002946.2. DR RefSeq; YP_208353.1; NC_002946.2. DR ProteinModelPortal; Q5F796; -. DR EnsemblBacteria; AAW89941; AAW89941; NGO_1287. DR GeneID; 3282080; -. DR KEGG; ngo:NGO1287; -. DR PATRIC; 20335917; VBINeiGon24812_1513. DR HOGENOM; HOG000219059; -. DR OMA; RAHPQWS; -. DR OrthoDB; EOG6NWBPV; -. DR BioCyc; NGON242231:GI2G-1199-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 49980 MW; 9A459ECC04E86716 CRC64; MNKQPLSLAV VGHTNTGKTS LLRTLLRDSG FGEVRNAPST TRHVEEAAIS DGADMLVFLY DTPGLEDAGG VLEWLENHTD NRSDGIERLQ QFLGSHGAHH DFNQEAKVLR QVLQSDMAMY VIDAREPVLD KYRDELTILS WCAKPVMPVF NFTGGQLPES WTTMLARRNL HVFAGFDTVA FDFEGELRLW ENLATMLPER STLDRLTAMR RREWQRLDGG ARREIADFLL DAAAFRQEVD ENEDTATVLQ TMQAEIRQLE RQMQQRLFAL YRFYHSEIDG GDWMPQAFRQ DPFDSELLKQ YGIRTGTGAA TGALIGLGLD IATLGGSLGL GTAIGGFLGG ILPNTRTISD KLAGRQTLHT DPETLTLLAA RALDLLHVLQ TRGHAAQSDI ELHSRKAPWD AAKLPPELNK ARSHWKWSSL NTHRPETSRA ERREYAEKIG IRLAGK // ID Q5F5E4_NEIG1 Unreviewed; 202 AA. AC Q5F5E4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Hemolysin {ECO:0000313|EMBL:AAW90593.1}; GN ORFNames=NGO_1985 {ECO:0000313|EMBL:AAW90593.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90593.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90593.1; -; Genomic_DNA. DR RefSeq; WP_003686871.1; NC_002946.2. DR RefSeq; YP_209005.1; NC_002946.2. DR EnsemblBacteria; AAW90593; AAW90593; NGO_1985. DR GeneID; 3282639; -. DR KEGG; ngo:NGO1985; -. DR PATRIC; 20337737; VBINeiGon24812_2395. DR HOGENOM; HOG000254779; -. DR OMA; MLQGCIG; -. DR OrthoDB; EOG6C5RQ0; -. DR BioCyc; NGON242231:GI2G-1883-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007055; BON_dom. DR Pfam; PF04972; BON; 1. DR PROSITE; PS50914; BON; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 53 123 BON. {ECO:0000259|PROSITE:PS50914}. SQ SEQUENCE 202 AA; 21728 MW; 28B3BDCE5B63DA6C CRC64; MKPKPHTVRT LIAAVLSLAL GGCFSAVVGG AAVGAKSVID RRTTGAQTDD NVMALRIETT ARSYLRQNNQ TKGYTPQISV VGYNRHLLLL GQVATEGEKQ FVGQIARSEQ AAEGVYNYIT VASLPRTAGD IAGDTWNTSK VRATLLGISP ATQARVKIIT YGNVTYVMGI LTPEEQAQIT QKVSTTVGVQ KVITLYQNYV QR // ID Q5F6Q7_NEIG1 Unreviewed; 375 AA. AC Q5F6Q7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 57. DE SubName: Full=Phospholipase A1 {ECO:0000313|EMBL:AAW90130.2}; GN ORFNames=NGO_1492 {ECO:0000313|EMBL:AAW90130.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90130.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90130.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6Q7; -. DR PRIDE; Q5F6Q7; -. DR EnsemblBacteria; AAW90130; AAW90130; NGO_1492. DR PATRIC; 20336438; VBINeiGon24812_1766. DR HOGENOM; HOG000288150; -. DR OMA; SRFWELE; -. DR OrthoDB; EOG6HQSN6; -. DR BioCyc; NGON242231:GI2G-1396-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 375 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364413. SQ SEQUENCE 375 AA; 42103 MW; 078F9C687F4EC6CC CRC64; MNTRNMRYIL LTGLLPTASA FGETALQCAA LTDNVTRLAC YDRIFAAQLP SSAGQEGQES KAVLNLTETV RSSLDKGEAV IVVEKGGDAL PADSAGETAD IYTPLSLMYD LDKNDLRGLL GVREHNPMYL MPFWYNNSPN YAPSSPTRGT TVQEKFGQQK RAETKLQVSF KSKIAENLFK TRADLWFGYT QRSDWQIYNQ GRKSAPFRNT DYKPEIFLTQ PVKADLPFGG RLRMLGAGFV HQSNGQSRPE SRSWNRIYAM AGMEWGKLTV IPRVWVRAFD QSGDKNDNPD IADYMGYGDV KLQYRLNDRQ NVYSVLRYNP KTGYGAIEAA YTFPIKGKLK GVVRGFHGYG ESLIDYNHKQ NGIGIGLMFN DWDGI // ID Q5F9P4_NEIG1 Unreviewed; 259 AA. AC Q5F9P4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=DNAase {ECO:0000313|EMBL:AAW89093.1}; GN ORFNames=NGO_0349 {ECO:0000313|EMBL:AAW89093.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89093.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89093.1; -; Genomic_DNA. DR RefSeq; WP_003694907.1; NC_002946.2. DR RefSeq; YP_207505.1; NC_002946.2. DR ProteinModelPortal; Q5F9P4; -. DR EnsemblBacteria; AAW89093; AAW89093; NGO_0349. DR GeneID; 3281194; -. DR KEGG; ngo:NGO0349; -. DR PATRIC; 20333695; VBINeiGon24812_0425. DR HOGENOM; HOG000201520; -. DR KO; K03424; -. DR OMA; LHVREAY; -. DR OrthoDB; EOG66QM1C; -. DR BioCyc; NGON242231:GI2G-328-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 259 AA; 28761 MW; 4CC5AABCEA21BA8D CRC64; MHIIDSHCHL NFEGLKERLP EVLSNMEANG VGQALAISVS RESFSEVFAV AEAHEHIYCT IGVHPDSKEA EEFSIAEMVE AAAHPKVVGI GETGLDYYWC KGDLSWQHKR FADHIEAANQ TGLPVIVHTR DAAADTLAIL KECKTNSGVI HCFSEDVGFA RAAMDLGLYI SFSGIVTFKN APLVQEAAKY VPDDRILVET DAPFLAPVPK RGRQNEPAFV RHTAEHIAKL RNQTLEQVAA YTTENFYRLF KKVPDMRVV // ID Q5F9W9_NEIG1 Unreviewed; 146 AA. AC Q5F9W9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Transcriptional regulator FolI {ECO:0000313|EMBL:AAW89018.1}; GN ORFNames=NGO_0267 {ECO:0000313|EMBL:AAW89018.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89018.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89018.1; -; Genomic_DNA. DR RefSeq; WP_003687622.1; NC_002946.2. DR RefSeq; YP_207430.1; NC_002946.2. DR EnsemblBacteria; AAW89018; AAW89018; NGO_0267. DR GeneID; 3281570; -. DR KEGG; ngo:NGO0267; -. DR PATRIC; 20333503; VBINeiGon24812_0332. DR HOGENOM; HOG000218844; -. DR KO; K19168; -. DR OMA; CIMPDMT; -. DR OrthoDB; EOG679TD5; -. DR BioCyc; NGON242231:GI2G-250-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 146 AA; 16474 MW; 17797D71A5637FB3 CRC64; MRAFQTALRP SRILNILTVS LHSASIAVCL TWFYGRMMWF GLAALAASYA YSLRITNLKH RHAITAITID RDGRAEIVSG KDKTAATLAG SSMVTPYALF LQWDTGGKTV RQCIMPDMTD KESYRRLKVW VLWRQPKKTA ETDTSD // ID Q5F565_NEIG1 Unreviewed; 550 AA. AC Q5F565; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 59. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90672.1}; GN ORFNames=NGO_2071 {ECO:0000313|EMBL:AAW90672.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90672.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90672.1; -; Genomic_DNA. DR RefSeq; WP_010951396.1; NC_002946.2. DR RefSeq; YP_209084.1; NC_002946.2. DR ProteinModelPortal; Q5F565; -. DR EnsemblBacteria; AAW90672; AAW90672; NGO_2071. DR GeneID; 3282846; -. DR KEGG; ngo:NGO2071; -. DR PATRIC; 20337973; VBINeiGon24812_2509. DR HOGENOM; HOG000218722; -. DR OMA; PRAGPYI; -. DR OrthoDB; EOG6XQ3GD; -. DR BioCyc; NGON242231:GI2G-1966-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 27 44 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 68 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 118 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 130 147 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 210 455 Sulfatase. {ECO:0000259|Pfam:PF00884}. SQ SEQUENCE 550 AA; 62248 MW; A8FD433677439F10 CRC64; MVAYAFLFLF VTAAVLLIVR SHYRWTYFFA SALFVFLAGG MLMLTAQWQR ALNFASVWFV VLILFHRLKI HYYKQPLLIS DFLLIADWRN WETLFHYKEA VIGMAGLLAL AGYAVFGWSG ADSLGMPWRW AGAVLFAAAF VSVRHFSKHP GAVKTWLDSL PDDGRDVFLN LPMSCRAVFF QVPVFEGDGE AFARQMPSET RPYGMSDEKP DIVVTLMEST LDPHCFDFAA AKIPDLKMFG RQEDTVFSSP LRVHTFGGAT WKSEFAFLAG VPSTDFGALA SGVFYSVVPH LQTGFVRNLR EHGYFCVALS PFTKGNYNAK AAYDHFGFNL MFQPQDLGYP APMGKNLWHI SSEEMMQYAR MILEKRHPDL ENVRQPMFVY VLTMKEHGPY RTDTDNVFDL DAPDLNAKTV SALNDYIGRI ADLDKAVESF DRYLHERGKP FVFGYFGDHQ VPFEGVSVRK KWDYAQPDYV TQFAVRSNIA GGFVQRQDFL DLAFAGGVLM EAAGLEAKDG FMRANMAMRG LCGGGLEDCP NRELVGNYRN YLYDVLKIAR // ID Q5F8U5_NEIG1 Unreviewed; 447 AA. AC Q5F8U5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 71. DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AAW89392.1}; GN ORFNames=NGO_0665 {ECO:0000313|EMBL:AAW89392.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89392.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89392.1; -; Genomic_DNA. DR RefSeq; WP_003691271.1; NC_002946.2. DR RefSeq; YP_207804.1; NC_002946.2. DR ProteinModelPortal; Q5F8U5; -. DR EnsemblBacteria; AAW89392; AAW89392; NGO_0665. DR GeneID; 3282053; -. DR KEGG; ngo:NGO0665; -. DR PATRIC; 20334426; VBINeiGon24812_0785. DR HOGENOM; HOG000271513; -. DR KO; K08324; -. DR OMA; EFTNAQT; -. DR OrthoDB; EOG6BS8QW; -. DR BioCyc; NGON242231:GI2G-632-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003344}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 443 Aldedh. {ECO:0000259|Pfam:PF00171}. SQ SEQUENCE 447 AA; 49377 MW; ECDDFF91A2132557 CRC64; MFHSVNVFTG ETLYRRPDQD YAEFERRLAD LKMHGRAFAQ LGVTERAARL QKFAGRLEAE KERFAEMVCE EVGRCLHECR AEIVKSIELI RYYARLAPEL LAHKTIATQA SLSQVRFEPL GVVFAVMPWN YPVWQVLRFA VPAMCAGNAC AVKPAPSVAR VSRALFDLAS DGIPLAGAWL DEADTLKAVE DTDAMAFTGS THTGRILAAH AGANLKKTVL ELGGSNAFIV MPDADLERAA AEACYSRFRD AGQSCNAAKR IIVTEAAADR FIQLFLAECA KLKMGDPKHP DTTLAPLHRE DLRDRVHGQV EDAVSNGAVC LTGGKVPQGS GWFYPATVLD RVNPACRVWR EEVFGPVALI LRAENEEHAI CLANDSPFGL GACIYTADTE RAWRFAEKIQ AGSVFINRHT SSDLRLPFGG VKDSGYGREL SEFGLYEFVN VKTYWQK // ID Q5FAE2_NEIG1 Unreviewed; 401 AA. AC Q5FAE2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 61. DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAW88845.2}; GN ORFNames=NGO_0084 {ECO:0000313|EMBL:AAW88845.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88845.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88845.2; -; Genomic_DNA. DR ProteinModelPortal; Q5FAE2; -. DR EnsemblBacteria; AAW88845; AAW88845; NGO_0084. DR PATRIC; 20333055; VBINeiGon24812_0111. DR HOGENOM; HOG000230163; -. DR OMA; IGHIGAW; -. DR OrthoDB; EOG6MPWRD; -. DR BioCyc; NGON242231:GI2G-74-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. 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 Aminotransferase {ECO:0000313|EMBL:AAW88845.2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-1, KW ECO:0000256|RuleBase:RU004508, ECO:0000256|SAAS:SAAS00486653}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88845.2}. FT MOD_RES 195 195 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR000390-1}. SQ SEQUENCE 401 AA; 44341 MW; 129D5D0A7F05340E CRC64; MPSEPDGPNT MLNTALSPWP SFTREEADAV SKVLLSNKVN YWTGSECREF EKEFAAFAGT RYAVALSNGT LALDAALKAI GIGAGDDVIV TSRTFLASAS CIVNAGANPV FADVDLNSQN ISAETVKAVL TPNTKAVIVV HLAGMPAEMD GIMALAKEHD LWVIEDCAQA HGATYKGKSV GSIGHVGAWS FCQDKIITTG GEGGMVTTND KTLWEKMWAY KDHGKSYDAV YHREHAPGFR WLHESFGTNW RMMEMQAVIG RIQLKHLPEW TARRQENAAK LAESLRKFKS IRLIEVAGYI GHAQYKFYAF VKPEHLKDDW TRDRIVSELN ARNVPCYQGG CSEVYLEKAF DNTPWRPKER LKNAVELGGT ALTFLVHPTL TDDEIAFCKK HIEAVLTEAA R // ID Q5F8Y6_NEIG1 Unreviewed; 1234 AA. AC Q5F8Y6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 91. 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 ORFNames=NGO_0623 {ECO:0000313|EMBL:AAW89351.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89351.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89351.1; -; Genomic_DNA. DR RefSeq; WP_010951092.1; NC_002946.2. DR RefSeq; YP_207763.1; NC_002946.2. DR ProteinModelPortal; Q5F8Y6; -. DR EnsemblBacteria; AAW89351; AAW89351; NGO_0623. DR GeneID; 3282896; -. DR KEGG; ngo:NGO0623; -. DR PATRIC; 20334330; VBINeiGon24812_0737. DR HOGENOM; HOG000216592; -. DR KO; K03723; -. DR OMA; GTHKLIQ; -. DR OrthoDB; EOG6FNHKW; -. DR BioCyc; NGON242231:GI2G-591-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}. FT DOMAIN 701 862 Helicase ATP-binding. {ECO:0000256|HAMAP- FT Rule:MF_00969, FT ECO:0000259|PROSITE:PS51192}. FT DOMAIN 883 1035 Helicase C-terminal. {ECO:0000256|HAMAP- FT Rule:MF_00969, FT ECO:0000259|PROSITE:PS51194}. FT NP_BIND 714 721 ATP. {ECO:0000256|HAMAP-Rule:MF_00969}. FT MOTIF 815 818 DEAH box. {ECO:0000256|HAMAP- FT Rule:MF_00969}. SQ SEQUENCE 1234 AA; 136469 MW; A888F605449748D6 CRC64; MTCPIPKPRE KSRWFNLSQG SLPLALARYL PHKRLKAVLT QDAEQALRLQ TAWRFFRPHD TAVFLPDWET LPYERFSPHQ DLVSERLSAL WQIKSGAADV LFVPVATAMQ KLPPVPFLAG RTFWLKTGQT LDIGRLKTDL VDAGYNHVSH VVAAGEFAVR GGIVDLFPMG SETPYRIDLF DDEIDSIKTF DTDTQRTISP VSEIRLLPAH EFPTDSEAQK IFRSRFREEV DGNPNDAAVY KAVSNGHFGA GVEYYLPLFF ENELETLFDY IGEDALFVSL GDVHAEANRF WNDVKSRYAM AQGDETYPPL LPQHLYLSAD VFAGRLKNYG QVLPDVSGKA HSLPDLAVNR QSDDPLQALK DFQTAFDGRI LLCAESLGRR ETMLGFLQQN GLKAKPVSDW QGFLSAHEPL MITVAPLAYG FKLGGLQSSS QQQTVPASEG EGKAVTDQTE FSASATNPLP SPLPQEREQS AAAVSDGLKA AAVSTESSLY LVASDLHGQT RQQSAPSPVG EGWGEGKAVA AQSAIAVITE SDLYQYVARS RVHNRRKKHA AVSDGLLRDL AEINIGDPVV HEEHGIGRYT GLVTMDLGGE TNEMMLLEYA GEAQLYVPVS QLHLISRYSG QAHESVALHK LGSGAWNKAK RKAAEKARDT AAELLNLYAQ RAAQSGHKFE INESDYQAFA DGFGYEETED QAAAIAAVIK DLTQAKPMDR LVCGDVGFGK TEVALRAAFV AVMGGKQVAV LAPTTLLVEQ HAQNFADRFA DFPVKVASLS RFNNSKATKA TLEGMADGTV DIVIGTHKLV QDDIKFKNLG LLIIDEEHRF GVRQKEQLKR LRANVDILTM TATPIPRTLS MALEGLRDFS LITTAPSRRL AVKTFVKPFS EGSVREAVLR ELKRGGQVFF LHNEVDTIEN MRERLETLLP EARIGVAHGQ LRERELEQVM RDFLQQRFNV LLCSTIIETG IDIPNANTII INRADKFGLA QLHQLRGRVG RSHHQAYAYL LTPEYITKDA EKRLDAIAAA DELGAGFTLA MQDLEIRGAG EILGEGQSGE MMQVGFTLYT EMLKQAVRDL KKGRQPDLDA PLGITTEIKL HSPALLPEDY CPDIHERLVL YKRLAVCETV QKINAIHEEL VDRFGLTEQP VKTLIESHHL RLAAKELGID AIDATSEAVT VTFGKHHCID PTGIILLIQT DKKYRLAGAD KLRFAAEMEN IEVRINTVKT VLKTLQGKRL PKGN // ID Q5F8Y4_NEIG1 Unreviewed; 82 AA. AC Q5F8Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89353.1}; GN ORFNames=NGO_0625 {ECO:0000313|EMBL:AAW89353.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89353.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89353.1; -; Genomic_DNA. DR RefSeq; WP_003688901.1; NC_002946.2. DR RefSeq; YP_207765.1; NC_002946.2. DR EnsemblBacteria; AAW89353; AAW89353; NGO_0625. DR GeneID; 3282894; -. DR KEGG; ngo:NGO0625; -. DR PATRIC; 20334334; VBINeiGon24812_0739. DR HOGENOM; HOG000027820; -. DR OMA; FPTYPIC; -. DR OrthoDB; EOG64BQ9F; -. DR BioCyc; NGON242231:GI2G-593-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 82 AA; 8519 MW; 55B7C3796562FE67 CRC64; MRIAGKYGGR QISGGAKGNA RHSAKPPIAA DTAFRASPLC RFPTYPICSE CVYGKEKNTA AGNLFGGFVC LYGDGGPHTP GK // ID Q5F706_NEIG1 Unreviewed; 125 AA. AC Q5F706; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90031.1}; GN ORFNames=NGO_1383 {ECO:0000313|EMBL:AAW90031.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90031.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90031.1; -; Genomic_DNA. DR RefSeq; WP_003705822.1; NC_002946.2. DR RefSeq; YP_208443.1; NC_002946.2. DR EnsemblBacteria; AAW90031; AAW90031; NGO_1383. DR GeneID; 3281773; -. DR KEGG; ngo:NGO1383; -. DR PATRIC; 20336155; VBINeiGon24812_1626. DR HOGENOM; HOG000219105; -. DR OrthoDB; EOG6GXTST; -. DR BioCyc; NGON242231:GI2G-1296-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028959; Imm41. DR Pfam; PF15592; Imm41; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 125 AA; 15447 MW; BD84A0D2B8AC9874 CRC64; MCEFKDFRRN IPCFEEYDEN SFIGKWYDDG VWDDEEYWKL ENDLIEVRRK YPYPMDIPRD IVIGIGTIID FLMVPNWELF EIKASPWLPD SVGIHERYER FTTMLRYIFT EKDIVNVRFD YYNKK // ID Q5F7R6_NEIG1 Unreviewed; 101 AA. AC Q5F7R6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89771.1}; GN ORFNames=NGO_1104 {ECO:0000313|EMBL:AAW89771.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89771.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89771.1; -; Genomic_DNA. DR RefSeq; WP_003687981.1; NC_002946.2. DR RefSeq; YP_208183.1; NC_002946.2. DR EnsemblBacteria; AAW89771; AAW89771; NGO_1104. DR GeneID; 3282516; -. DR KEGG; ngo:NGO1104; -. DR PATRIC; 20335458; VBINeiGon24812_1295. DR OMA; FRSRAWR; -. DR OrthoDB; EOG6M6JR3; -. DR BioCyc; NGON242231:GI2G-1016-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR010774; DUF1364. DR Pfam; PF07102; DUF1364; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 101 AA; 10578 MW; A7C3E4FC12631C38 CRC64; MSSAIRKAAK GGQCTPNIAG VCNDNPETVV LCRFPGETHG AGLKSGGLGA GFGCGCRRGA IDGRGAGLSR EDKEFYMRRS QLRTIRRLEA LGVVGVKGRL K // ID Q5FAE9_NEIG1 Unreviewed; 207 AA. AC Q5FAE9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Esterase {ECO:0000313|EMBL:AAW88838.1}; GN ORFNames=NGO_0077 {ECO:0000313|EMBL:AAW88838.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88838.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88838.1; -; Genomic_DNA. DR ProteinModelPortal; Q5FAE9; -. DR ESTHER; neime-NMB1828; A85-IroE-IroD-Fes-Yiel. DR DNASU; 3282275; -. DR EnsemblBacteria; AAW88838; AAW88838; NGO_0077. DR PATRIC; 20333035; VBINeiGon24812_0101. DR HOGENOM; HOG000220693; -. DR OMA; EYLREAW; -. DR OrthoDB; EOG6423DP; -. DR BioCyc; NGON242231:GI2G-67-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 207 AA; 23653 MW; 7682F2CC84220D46 CRC64; MQSLMNNPVT RSNAPCLIVG IGYTTGSVRD LAQRAADYTP PLGDNATADE RRQFGQADRF ADFIDSELTA FLESRYTLNR NETAVFGHSF GALFGLYSLL SHRCFRRHWL VSPSIWWHNR RILDFMPSEN RLDGIDACLN IGALERSSGC KRREERDMAG QAEQMAAELD RRGTAVFFRE YPNADHGNVP FYSLTDCVEY LREAWQR // ID Q5F6T2_NEIG1 Unreviewed; 137 AA. AC Q5F6T2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90105.1}; GN ORFNames=NGO_1465 {ECO:0000313|EMBL:AAW90105.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90105.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90105.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90105; AAW90105; NGO_1465. DR PATRIC; 20336363; VBINeiGon24812_1730. DR OrthoDB; EOG63Z78C; -. DR BioCyc; NGON242231:GI2G-1370-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 137 AA; 15454 MW; FF52BCF2565F9393 CRC64; MPSEGFSDGI FALFTVILKS RHSHAGRNLD ENPSCQKYPN RQEYPCHHSR YTVILKPVIP AQTEIRICPR GNLCAAIPAK AGIRTVRFRL FPINSCCFSF LDSHFRGNDE GVGIRFLSSG HFRQIALALD ISYFNPL // ID Q5F9I8_NEIG1 Unreviewed; 283 AA. AC Q5F9I8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Damage-inducible protein D {ECO:0000313|EMBL:AAW89149.1}; GN Name=dinD {ECO:0000313|EMBL:AAW89149.1}; GN ORFNames=NGO_0405 {ECO:0000313|EMBL:AAW89149.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89149.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89149.1; -; Genomic_DNA. DR RefSeq; WP_003687842.1; NC_002946.2. DR RefSeq; YP_207561.1; NC_002946.2. DR EnsemblBacteria; AAW89149; AAW89149; NGO_0405. DR GeneID; 3283004; -. DR KEGG; ngo:NGO0405; -. DR PATRIC; 20333819; VBINeiGon24812_0487. DR HOGENOM; HOG000003507; -. DR KO; K14623; -. DR OMA; RIRSKGD; -. DR OrthoDB; EOG69WFNW; -. DR BioCyc; NGON242231:GI2G-384-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003497; BRO_N_domain. DR Pfam; PF02498; Bro-N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 13 100 Bro-N. {ECO:0000259|Pfam:PF02498}. SQ SEQUENCE 283 AA; 32263 MW; 6F97828A3C60680D CRC64; MTTENNAFEN AKHIDETGNE YWSARTLQQI LEYSEWRNFQ RAIDKAITAC ETSGNDKNHH FVETNKMIAL GKGGQREVAD YRLSRYACYL IVQNGDPSKS VIAAGQTYFA VQARRQELQD EAAFRSLGED KQRLLLRRQL REHNTDLAAA AKDAGVEKPV EYAVFQNHGY RGLYGGLDKQ GIHSRKGLKK SQRILDHMNA SEPAANLFRA TQTEEKLRRK NIQGKTQANR VHFEVGQKVR QTIEELGGIM PENQPVPEKS IKQLENEEQK RLAATEQHQN GKK // ID Q5F976_NEIG1 Unreviewed; 159 AA. AC Q5F976; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89261.1}; GN ORFNames=NGO_0523 {ECO:0000313|EMBL:AAW89261.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89261.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89261.1; -; Genomic_DNA. DR RefSeq; WP_002241413.1; NC_002946.2. DR RefSeq; YP_207673.1; NC_002946.2. DR EnsemblBacteria; AAW89261; AAW89261; NGO_0523. DR GeneID; 3282927; -. DR KEGG; ngo:NGO0523; -. DR PATRIC; 20334092; VBINeiGon24812_0618. DR HOGENOM; HOG000220713; -. DR OMA; MTVIGVF; -. DR OrthoDB; EOG686NHT; -. DR BioCyc; NGON242231:GI2G-501-MONOMER; -. DR Proteomes; UP000000535; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 26 53 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 159 AA; 17978 MW; C092B5320E2A00DF CRC64; MTDNLIQIAT PILTVIGVFV AAYGIMRNTE NAKKRATIDM IMAERNNAAL QEAITIVNGL AKTDGCILAT YTSDTPDKKK DREAILTVLN QREFVCAGVL GGALHEKMYK DFEYSMLLRD WDNLSSFIFE IRRIRSAPTA FQEFEAVARK WKKKPLKTK // ID Q5F7W0_NEIG1 Unreviewed; 337 AA. AC Q5F7W0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 62. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW89727.2}; GN ORFNames=NGO_1056 {ECO:0000313|EMBL:AAW89727.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89727.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89727.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7W0; -. DR MEROPS; M23.011; -. DR EnsemblBacteria; AAW89727; AAW89727; NGO_1056. DR PATRIC; 20335346; VBINeiGon24812_1239. DR HOGENOM; HOG000159026; -. DR OMA; GQRAICA; -. DR OrthoDB; EOG61ZTBJ; -. DR BioCyc; NGON242231:GI2G-972-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.10.350.10; -; 1. DR InterPro; IPR011055; Dup_hybrid_motif. DR InterPro; IPR018392; LysM_dom. DR InterPro; IPR016047; Peptidase_M23. DR Pfam; PF01476; LysM; 1. DR Pfam; PF01551; Peptidase_M23; 1. DR SMART; SM00257; LysM; 1. DR SUPFAM; SSF51261; SSF51261; 1. DR SUPFAM; SSF54106; SSF54106; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 337 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5005364488. FT DOMAIN 104 147 LysM. {ECO:0000259|SMART:SM00257}. SQ SEQUENCE 337 AA; 34490 MW; B648701A0F9229DB CRC64; MLKQTTLLAA CTAVAALLGG CATQQPAPVI AGNSGMQTVS SAPVYNPYGA TPYNAAPAAN DAPYVPPVQT APVYSPPAYV PPSAPAVSGT YVPSYAPVDI NAATHTIVRG DTVYNISKRY HISQDDFRAW NGMTDNTLSI GQIVKVKPAG YAAPKTAAVE SRPAVPAAAQ TPVKPAAQPP VQSAPQPAAP AAENKAVPAP APAPQSPAAS PSGTRSVGGI VWQRPTQGKV VADFGGGNKG VDIAGNAGQP VLAAADGKVV YAGSGLRGYG NLVIIQHNSS FLTAYGHNQK LLVGEGQQVK RGQQVALMGN TDASRTQLHF EVRQNGKPVN PNSYIAF // ID Q5F630_NEIG1 Unreviewed; 99 AA. AC Q5F630; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90357.2}; GN ORFNames=NGO_1736 {ECO:0000313|EMBL:AAW90357.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90357.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90357.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90357; AAW90357; NGO_1736. DR PATRIC; 20337070; VBINeiGon24812_2075. DR HOGENOM; HOG000262580; -. DR OMA; LPFVNQR; -. DR OrthoDB; EOG6V7BRP; -. DR BioCyc; NGON242231:GI2G-1632-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR016768; UCP019883. DR Pfam; PF10993; DUF2818; 1. DR PIRSF; PIRSF019883; UCP019883; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 27 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39 57 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 88 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 99 AA; 11327 MW; F636ABF80BD402C9 CRC64; MTASMYILLV LALIFANAPF LTTRLFGVAA LKRKHFGHHL IELAAGFALT ASLAYILESR AGAVHNQGWE FYATVVCLYL IFAFPCFVRR YFWHTRNRE // ID Q5F8G0_NEIG1 Unreviewed; 458 AA. AC Q5F8G0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. 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 {ECO:0000256|HAMAP-Rule:MF_02020}; GN ORFNames=NGO_0815 {ECO:0000313|EMBL:AAW89527.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89527.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89527.1; -; Genomic_DNA. DR RefSeq; WP_003688594.1; NC_002946.2. DR RefSeq; YP_207939.1; NC_002946.2. DR ProteinModelPortal; Q5F8G0; -. DR DNASU; 3281819; -. DR EnsemblBacteria; AAW89527; AAW89527; NGO_0815. DR GeneID; 3281819; -. DR KEGG; ngo:NGO0815; -. DR PATRIC; 20334784; VBINeiGon24812_0962. DR HOGENOM; HOG000256032; -. DR KO; K02558; -. DR OMA; CDANVYP; -. DR OrthoDB; EOG64BQ73; -. DR BioCyc; NGON242231:GI2G-769-MONOMER; -. DR UniPathway; UPA00544; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; 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:UP000000535}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02020, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AAW89527.1}; 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:UP000000535}. 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; 49446 MW; C90E671A963848CD CRC64; MKHIHIIGIG GTFMGGIAAI AKEAGFKVSG CDAKMYPPMS TQLEALGIGV HEGFDAAQLE EFQADIYVIG NVARRGMDVV EAILNRGLPY ISGPQWLAEN VLHHHWVLGV AGTHGKTTTA SMLAWVLEYA GLAPGFLIGG VPENFGVSAR LPQTPRQDPN SKSPFFVIEA DEYDTAFFDK RSKFVHYRPR TAVLNNLEFD HADIFADLGA IQTQFHHLVR TVPSEGLIVC NGQQQSLQDT LDKGCWTPVE KFGTGHGWQI GEVNADGSFD VLLDGKKAGH VAWDLMGGHN RMNALAVIAA ARHAGVDVQT ACEALGAFKN VKRRMEIKGT ANGITVYDDF AHHPTAIETT IQGLRQRVGG ARILAVLEPR SNTMKLGTMK SALPASLKEA DQVFCYAGGA DWDVAEALAP LGCRLRVGKD FDTFVAEIVK NARTGDHILV MSNGGFGGIH TKLLDALR // ID Q5F850_NEIG1 Unreviewed; 162 AA. AC Q5F850; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89637.1}; GN ORFNames=NGO_0942 {ECO:0000313|EMBL:AAW89637.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89637.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89637.1; -; Genomic_DNA. DR RefSeq; WP_003688359.1; NC_002946.2. DR RefSeq; YP_208049.1; NC_002946.2. DR EnsemblBacteria; AAW89637; AAW89637; NGO_0942. DR GeneID; 3281522; -. DR KEGG; ngo:NGO0942; -. DR PATRIC; 20335069; VBINeiGon24812_1104. DR HOGENOM; HOG000023032; -. DR KO; K09793; -. DR OMA; FEYLSGR; -. DR OrthoDB; EOG64NB1M; -. DR BioCyc; NGON242231:GI2G-879-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 67 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 155 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 162 AA; 16453 MW; 9C75A018D10174A6 CRC64; MTALLVILAL ALIAVGTAGI VYPALPGLAL MFAGTWLLAY AGGYQIYGAG ILWTVGLISL GGILADYMAG MLGVKYTGAG KLAVRGALAG SIIGIFFSLP GLILGPFIGA AAGELIDRRN MLQAGKAGLG TLLGLVVGTA FKIGCAVSIL FILLVKYIAY LF // ID Q5F5C7_NEIG1 Unreviewed; 274 AA. AC Q5F5C7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Cell division protein {ECO:0000313|EMBL:AAW90610.1}; GN ORFNames=NGO_2002 {ECO:0000313|EMBL:AAW90610.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90610.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90610.1; -; Genomic_DNA. DR RefSeq; WP_003686904.1; NC_002946.2. DR RefSeq; YP_209022.1; NC_002946.2. DR EnsemblBacteria; AAW90610; AAW90610; NGO_2002. DR GeneID; 3282622; -. DR KEGG; ngo:NGO2002; -. DR PATRIC; 20337781; VBINeiGon24812_2414. DR HOGENOM; HOG000218718; -. DR OrthoDB; EOG6HTNWJ; -. DR BioCyc; NGON242231:GI2G-1903-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. PE 4: Predicted; KW Cell cycle {ECO:0000313|EMBL:AAW90610.1}; KW Cell division {ECO:0000313|EMBL:AAW90610.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 68 119 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 274 AA; 29393 MW; FFFC2201F43B5A30 CRC64; MKWLFTLLAV LNIAVFGGTV GYKLAVKAAG GVPENRAVEN TPPATPAAGN AAASVEDTAA LLKPGDILSE EQAEQLRLKK EAEQKKLREK KQREEKARRE KLAAEKAQAE RENGAADALC AAQASLTMDE DDYHRIKGLL GKWSHVASRS VEKRTAKAKP ADKTYRVVLP VSADAENQAA ELSAKGFNPI PFDGALSLGV GNSRENAQAL QNRLADAGFG GAHIVEHFAE ADRQDDSLSV SRMTVLFTGV NAADADEIRK ITSLYGKLNL KSCK // ID Q5F532_NEIG1 Unreviewed; 231 AA. AC Q5F532; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90705.1}; GN ORFNames=NGO_2104 {ECO:0000313|EMBL:AAW90705.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90705.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90705.1; -; Genomic_DNA. DR RefSeq; WP_003697882.1; NC_002946.2. DR RefSeq; YP_209117.1; NC_002946.2. DR ProteinModelPortal; Q5F532; -. DR EnsemblBacteria; AAW90705; AAW90705; NGO_2104. DR GeneID; 3282813; -. DR KEGG; ngo:NGO2104; -. DR PATRIC; 20338047; VBINeiGon24812_2546. DR HOGENOM; HOG000271058; -. DR OMA; NDAVNGM; -. DR OrthoDB; EOG6KHG1J; -. DR BioCyc; NGON242231:GI2G-1999-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 81 216 Fido. {ECO:0000259|PROSITE:PS51459}. SQ SEQUENCE 231 AA; 25927 MW; 089828C9220700FE CRC64; MFPDKYKLSL EENIFLAKKV LVAQIHNLSR FENCQTTLLQ TEQIINDKNV ASASLEDIQT ILNLKRAYQY VISHISNGEP VNISLLKRIN NIVAKDDSLV PVDFRTGSVG VTLLDGSRHA PNPVKEIEVA RVLQNIGLQS GSTTETAVRF MLYCMRQQVF WDGNKRTATL FANGLMMAGG CGILEISEMQ MPRFNEKLSA FYRTGDDTDI SKFVYQNCIS GIDYFGADED I // ID Q5F6U8_NEIG1 Unreviewed; 40 AA. AC Q5F6U8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90089.1}; GN ORFNames=NGO_1447 {ECO:0000313|EMBL:AAW90089.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90089.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90089.1; -; Genomic_DNA. DR RefSeq; WP_003703677.1; NC_002946.2. DR RefSeq; YP_208501.1; NC_002946.2. DR EnsemblBacteria; AAW90089; AAW90089; NGO_1447. DR GeneID; 3281696; -. DR KEGG; ngo:NGO1447; -. DR OrthoDB; EOG6DJZ9Z; -. DR BioCyc; NGON242231:GI2G-1354-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 40 AA; 4493 MW; 9B997D054E39F32B CRC64; MLGAAFAVLP RRRARYNPPR HPPDLETCLC DPPISFPTCI // ID Q5F8V8_NEIG1 Unreviewed; 110 AA. AC Q5F8V8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 81. DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077}; GN ORFNames=NGO_0652 {ECO:0000313|EMBL:AAW89379.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89379.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89379.1; -; Genomic_DNA. DR RefSeq; WP_002247584.1; NC_002946.2. DR RefSeq; YP_207791.1; NC_002946.2. DR ProteinModelPortal; Q5F8V8; -. DR SMR; Q5F8V8; 3-110. DR EnsemblBacteria; AAW89379; AAW89379; NGO_0652. DR GeneID; 3282200; -. DR KEGG; ngo:NGO0652; -. DR PATRIC; 20334392; VBINeiGon24812_0768. DR HOGENOM; HOG000292977; -. DR KO; K03671; -. DR OMA; QYGIMSI; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NGON242231:GI2G-619-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 7ADBB212199FDE45 CRC64; MSSELIVHTG DAAFEQDVLK SDLPVLLDFW APWCGPCKMI APILDDIAAE FEGRLKVVKI NIDDNEATPS RFGVRGIPTL MVFKNGEVVA TKVGALAKGQ LTAFVEASIA // ID Q5F7H4_NEIG1 Unreviewed; 196 AA. AC Q5F7H4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE SubName: Full=Anthranilate synthase component II {ECO:0000313|EMBL:AAW89863.1}; DE EC=4.1.3.27 {ECO:0000313|EMBL:AAW89863.1}; GN ORFNames=NGO_1204 {ECO:0000313|EMBL:AAW89863.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89863.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89863.1; -; Genomic_DNA. DR RefSeq; WP_003689643.1; NC_002946.2. DR RefSeq; YP_208275.1; NC_002946.2. DR ProteinModelPortal; Q5F7H4; -. DR MEROPS; C26.955; -. DR EnsemblBacteria; AAW89863; AAW89863; NGO_1204. DR GeneID; 3281971; -. DR KEGG; ngo:NGO1204; -. DR PATRIC; 20335709; VBINeiGon24812_1413. DR HOGENOM; HOG000025029; -. DR KO; K01658; -. DR OMA; PCSPDEA; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NGON242231:GI2G-1115-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. 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:UP000000535}; KW Lyase {ECO:0000313|EMBL:AAW89863.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 194 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. SQ SEQUENCE 196 AA; 21862 MW; 3CE1754E236EECF0 CRC64; MLLFIDNYDS FTYNIVQYFA ELGQEVAVRR NDDITLEEIE ALNPQYLVIG PGPCSPKEAG ISVEAMRHFA GRLPIMGVCL GHQTIGEAFG GDVVRAKTLM HGKVSPVSHS GKGMFKGLPN PVTCTRYHSL VIERGTLPDC LEITAWTEDG EIMGVRHKEY AVEGVQFHPE ALLTERGHDM LNNFLVEFQN FKPQKI // ID Q5F965_NEIG1 Unreviewed; 478 AA. AC Q5F965; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Alginate O-acetyltransferase {ECO:0000313|EMBL:AAW89272.1}; GN ORFNames=NGO_0534 {ECO:0000313|EMBL:AAW89272.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89272.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89272.1; -; Genomic_DNA. DR RefSeq; WP_003706086.1; NC_002946.2. DR RefSeq; YP_207684.1; NC_002946.2. DR EnsemblBacteria; AAW89272; AAW89272; NGO_0534. DR GeneID; 3282915; -. DR KEGG; ngo:NGO0534; -. DR PATRIC; 20334114; VBINeiGon24812_0629. DR HOGENOM; HOG000003940; -. DR OMA; WDWRFVA; -. DR OrthoDB; EOG6QCD9F; -. DR BioCyc; NGON242231:GI2G-512-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89272.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 5 22 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 63 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 94 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 114 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 216 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 416 436 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 476 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 478 AA; 53529 MW; 679AC39DBDCEF639 CRC64; MPLLSVEFAL FFIVFLPIYW GFAKYPSVQN LLLLAAGMGW LYHISPVFAA IIVLYSSCVY LLGELLRSDR ESTRRFWLGC GIAASITVLG FFKYFDFFRP LIAQYAGKGG AIDILMPLGL SYYTFQSVAY LVYCFRAPHA ARFGWHELLL HLSFFPTVTS GPIIRAAAFK STDGEQAGAL AQIRTRRPRS PVRPALAVSL ILLGIAKKWW LAGILAENWV SPVFENPTQF DGWGVLAGVY GYTFQLFLDF SGYSDLVIGM AMLLGFRLPK NFSAPLRAAN IRAFWDKWHI SLSTWIRDYI YIPLGGSKKG FLRTQLNLMA AMVLSGIWHG YGWNFLIWGA LHGTALALLN TGDRYFGRDA LCRLKYLAPL SWFVTFHFVC LSFVVFNTAN PDDAGAVFSA LFANAGGWNA PQRADMLLLA SFASLMLLYP YLQRAFDGAV KGLEKIPMWL WFIQISIILL LIIVLAPSGI PGFIYANF // ID Q5F7L6_NEIG1 Unreviewed; 152 AA. AC Q5F7L6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89821.1}; GN ORFNames=NGO_1155 {ECO:0000313|EMBL:AAW89821.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89821.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89821.1; -; Genomic_DNA. DR RefSeq; WP_003689755.1; NC_002946.2. DR RefSeq; YP_208233.1; NC_002946.2. DR ProteinModelPortal; Q5F7L6; -. DR EnsemblBacteria; AAW89821; AAW89821; NGO_1155. DR GeneID; 3282168; -. DR KEGG; ngo:NGO1155; -. DR PATRIC; 20335579; VBINeiGon24812_1354. DR OrthoDB; EOG65QWDB; -. DR BioCyc; NGON242231:GI2G-1067-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0019867; C:outer membrane; IEA:InterPro. DR Gene3D; 2.40.128.130; -; 1. DR InterPro; IPR005546; Autotransporte_beta. DR InterPro; IPR006315; OM_autotransptr_brl. DR Pfam; PF03797; Autotransporter; 1. DR SUPFAM; SSF103515; SSF103515; 1. DR TIGRFAMs; TIGR01414; autotrans_barl; 1. DR PROSITE; PS51208; AUTOTRANSPORTER; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 152 Autotransporter (TC 1.B.12). FT {ECO:0000259|PROSITE:PS51208}. SQ SEQUENCE 152 AA; 17543 MW; 7090C8A7CD27B59D CRC64; MPICFPPKPV GGWKNKTAAK TYRWQPEVQL SYWFTRGYGF PLSNGLSAET DNFRSLMGRF GFRAGVDGLD GGRLNIYGKL MYKREFIGTI RHRFNGSAVE EFKHRGGWLE YGLGVVRRNA GNGRQLYFEA QRSSMHTMRQ NWQVNMGVRS MF // ID Q5F7K8_NEIG1 Unreviewed; 52 AA. AC Q5F7K8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89829.1}; GN ORFNames=NGO_1163 {ECO:0000313|EMBL:AAW89829.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89829.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89829.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89829; AAW89829; NGO_1163. DR OMA; HGNDEKL; -. DR BioCyc; NGON242231:GI2G-1076-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 52 AA; 6090 MW; 254B4B23243193C4 CRC64; MGFRRHRPPP SFPRRRESRT SGNGNIQKPS ENLKVLDSRF HGNDEKLRTA EE // ID Q5F722_NEIG1 Unreviewed; 70 AA. AC Q5F722; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90015.2}; GN ORFNames=NGO_1367 {ECO:0000313|EMBL:AAW90015.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90015.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90015.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90015; AAW90015; NGO_1367. DR PATRIC; 20336119; VBINeiGon24812_1608. DR HOGENOM; HOG000219081; -. DR OMA; WHEDDFK; -. DR OrthoDB; EOG6R2H31; -. DR BioCyc; NGON242231:GI2G-1280-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 70 AA; 8367 MW; 0F32CCDB53D46B1A CRC64; MKNEIQKIMD KYDPWHEDDF KSYEDIAKDV SLMTDKTFIE HYLLEVYSEE NGHFDQDNVH AMIGEIKNAI // ID Q5FA17_NEIG1 Unreviewed; 331 AA. AC Q5FA17; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Iron ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW88970.1}; GN ORFNames=NGO_0217 {ECO:0000313|EMBL:AAW88970.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88970.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88970.1; -; Genomic_DNA. DR RefSeq; WP_003687545.1; NC_002946.2. DR RefSeq; YP_207382.1; NC_002946.2. DR ProteinModelPortal; Q5FA17; -. DR SMR; Q5FA17; 23-331. DR EnsemblBacteria; AAW88970; AAW88970; NGO_0217. DR GeneID; 3281438; -. DR KEGG; ngo:NGO0217; -. DR PATRIC; 20333373; VBINeiGon24812_0269. DR HOGENOM; HOG000238625; -. DR KO; K02012; -. DR OMA; FTAYKGN; -. DR OrthoDB; EOG625JVF; -. DR BioCyc; NGON242231:GI2G-200-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Iron {ECO:0000256|PIRSR:PIRSR002825-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR002825-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 331 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256087. FT METAL 31 31 Iron. {ECO:0000256|PIRSR:PIRSR002825-1}. FT METAL 79 79 Iron. {ECO:0000256|PIRSR:PIRSR002825-1}. FT METAL 217 217 Iron. {ECO:0000256|PIRSR:PIRSR002825-1}. FT METAL 218 218 Iron. {ECO:0000256|PIRSR:PIRSR002825-1}. SQ SEQUENCE 331 AA; 35840 MW; 843DC30F1B3E8EA4 CRC64; MKTSIRYALL AAALTAATPA LADITVYNGQ HKEAAQAVAD AFTRATGIKV KLNSAKGDQL AGQIKEEGSR SPADVFYSEQ IPALATLSAA NLLEPLPAST INETRGKGVP VAAKKDWVAL SGRSRVVVYD TRKLSEKDLE KSVLNYATPK WKNRIGYVPT SGAFLEQIVA IVKLKGEAAA LKWLKGLKEY GKPYAKNSVA LQAVENGEID AALINNYYWH AFAREKGVQN VHTRLNFVRH RDPGALVTYS GAAVLKSSQN KDEAKKFVAF LAGKEGQRAL TAVRAEYPLN PHVVSTFNLE PIAKLEAPQV SATTVSEKEH ATRLLEQAGM K // ID Q5F620_NEIG1 Unreviewed; 433 AA. AC Q5F620; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 70. DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:AAW90367.1}; DE EC=1.6.5.11 {ECO:0000313|EMBL:AAW90367.1}; GN ORFNames=NGO_1746 {ECO:0000313|EMBL:AAW90367.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90367.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90367.1; -; Genomic_DNA. DR RefSeq; WP_003689949.1; NC_002946.2. DR RefSeq; YP_208779.1; NC_002946.2. DR ProteinModelPortal; Q5F620; -. DR DNASU; 3281091; -. DR EnsemblBacteria; AAW90367; AAW90367; NGO_1746. DR GeneID; 3281091; -. DR KEGG; ngo:NGO1746; -. DR PATRIC; 20337094; VBINeiGon24812_2087. DR HOGENOM; HOG000251534; -. DR KO; K00335; -. DR OMA; LRWTEFY; -. DR OrthoDB; EOG6W9XGK; -. DR BioCyc; NGON242231:GI2G-1642-MONOMER; -. DR Proteomes; UP000000535; 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:InterPro. 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:UP000000535}; 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:AAW90367.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 333 378 NADH_4Fe-4S. {ECO:0000259|SMART:SM00928}. SQ SEQUENCE 433 AA; 47417 MW; E51C0463F676D81F 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 LYRIVRRIVE GKGRMEDLDL LDSVGNQMAG RTICALADAA VFPVRSFTKH FRDEFAHYIE HGGPMKEHKW GGW // ID Q5F8U3_NEIG1 Unreviewed; 64 AA. AC Q5F8U3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89394.2}; GN ORFNames=NGO_0667 {ECO:0000313|EMBL:AAW89394.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89394.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89394.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89394; AAW89394; NGO_0667. DR PATRIC; 20334430; VBINeiGon24812_0787. DR HOGENOM; HOG000071298; -. DR OMA; GSITIFQ; -. DR OrthoDB; EOG6KT306; -. DR BioCyc; NGON242231:GI2G-634-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 42 63 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 64 AA; 7570 MW; 1616549FF4BE75AD CRC64; MNKMPSEPFS KRSDGISSIK NIKNRRFNRF NTKGRITRLI GFYTRLPAIF FFFAKIYGSI TIFQ // ID Q5FAD1_NEIG1 Unreviewed; 181 AA. AC Q5FAD1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Pilin assembly protein {ECO:0000313|EMBL:AAW88856.1}; GN ORFNames=NGO_0095 {ECO:0000313|EMBL:AAW88856.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88856.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88856.1; -; Genomic_DNA. DR RefSeq; WP_003692554.1; NC_002946.2. DR RefSeq; YP_207268.1; NC_002946.2. DR ProteinModelPortal; Q5FAD1; -. DR SMR; Q5FAD1; 69-181. DR EnsemblBacteria; AAW88856; AAW88856; NGO_0095. DR GeneID; 3282291; -. DR KEGG; ngo:NGO0095; -. DR PATRIC; 20333087; VBINeiGon24812_0127. DR HOGENOM; HOG000281372; -. DR KO; K02665; -. DR OMA; CQANDES; -. DR OrthoDB; EOG6GBMC8; -. DR BioCyc; NGON242231:GI2G-85-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR007446; Pilus_assembly_PilP. DR Pfam; PF04351; PilP; 1. DR PIRSF; PIRSF016481; Pilus_assembly_PilP; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256260. SQ SEQUENCE 181 AA; 20095 MW; 689A9B9535F7994C CRC64; MKHYALLISF LALSACSQNS EDLNEWMAQT RREAKAEIIP FQAPTLPVAP VYSPPQLTGP NAFDFRRMET AKKGENAPDT KRIKETLEKF SLENMRYVGI LKSGQKVSGF IEAEGYVYTV GVGNYLGQNY GRIESITDDS IILNELIEDS TGNWVSRKAE LLLNSSDKNT EQAAAPAAEQ N // ID Q5F508_NEIG1 Unreviewed; 69 AA. AC Q5F508; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90729.2}; GN ORFNames=NGO_2132 {ECO:0000313|EMBL:AAW90729.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90729.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90729.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90729; AAW90729; NGO_2132. DR PATRIC; 20338113; VBINeiGon24812_2579. DR HOGENOM; HOG000027860; -. DR OMA; CPCRFDI; -. DR OrthoDB; EOG667811; -. DR BioCyc; NGON242231:GI2G-2023-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 69 AA; 7848 MW; B76118D419DCB2E8 CRC64; MFQTAFCPMG RKRNPFVGKT CFGVSKPCCP CRFDIRTLKM PSEPAIRASD GVLSDIRAIR RSVRFSRFC // ID Q5F5N5_NEIG1 Unreviewed; 490 AA. AC Q5F5N5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 79. DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504}; DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504}; GN ORFNames=NGO_1881 {ECO:0000313|EMBL:AAW90502.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90502.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90502.1; -; Genomic_DNA. DR RefSeq; WP_003690149.1; NC_002946.2. DR RefSeq; YP_208914.1; NC_002946.2. DR ProteinModelPortal; Q5F5N5; -. DR EnsemblBacteria; AAW90502; AAW90502; NGO_1881. DR GeneID; 3282312; -. DR KEGG; ngo:NGO1881; -. DR PATRIC; 20337466; VBINeiGon24812_2264. DR HOGENOM; HOG000021558; -. DR KO; K00873; -. DR OMA; EKMPSVN; -. DR OrthoDB; EOG6GBMB0; -. DR BioCyc; NGON242231:GI2G-1786-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000535; 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 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:UP000000535}; KW Glycolysis {ECO:0000256|RuleBase:RU000504}; KW Kinase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:AAW90502.1}; KW Magnesium {ECO:0000256|RuleBase:RU000504}; KW Pyruvate {ECO:0000313|EMBL:AAW90502.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU000504, KW ECO:0000313|EMBL:AAW90502.1}. FT DOMAIN 13 355 PK. {ECO:0000259|Pfam:PF00224}. FT DOMAIN 375 487 PK_C. {ECO:0000259|Pfam:PF02887}. SQ SEQUENCE 490 AA; 52508 MW; 716351B849E6A0AE CRC64; MNQTSRDLTR ISHNTKIVAT LGPGSNNVEL LEDMIRVGGL NVVRFNFSHG TPEFHQENAR IVREAAKRAG QEIAIIADLQ GPKIRVGKIA GGGIELNKGE TLVLDAALEG EGTREAVGLD YRDLPDDVAA GDVLWLDDGL LTLTVESVEG SRIITRVENS HILKSNKGIN KRGGGLSAGA LTEKDFRDLK TAIAIGCDYL AISFVKSAED LHIARAKVEE EMKGSTAVRP GLVSKIERVE AIENLDEIIL AGDGIMVARG DLAVEVGHAA VPALQKRMIR RARELRRFSI TATQMMESMI TNPVPTRAEV SDVANAVLDG TDAVMCSAET AVGAYPFETV SQMAIICAAA EKEQDSLNGV AEQTEYPEAV STNLAIAGGA VSVARAVHAK AIVALTESGS TAFEISRHNI TLPIFALTPS VSAQRRMAMY RGVRPLILAT STDHDTALNE VETMLVEHNI LHSGDQYIIT SGSQMRESGS TNTLEVLRVK // ID Q5F9E8_NEIG1 Unreviewed; 169 AA. AC Q5F9E8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89189.1}; GN ORFNames=NGO_0449 {ECO:0000313|EMBL:AAW89189.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89189.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89189.1; -; Genomic_DNA. DR RefSeq; WP_003687909.1; NC_002946.2. DR RefSeq; YP_207601.1; NC_002946.2. DR EnsemblBacteria; AAW89189; AAW89189; NGO_0449. DR GeneID; 3282994; -. DR KEGG; ngo:NGO0449; -. DR PATRIC; 20333928; VBINeiGon24812_0538. DR HOGENOM; HOG000044222; -. DR OMA; WIAMIAE; -. DR OrthoDB; EOG6Z6FZS; -. DR BioCyc; NGON242231:GI2G-427-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 19408 MW; 0CFE53DA67AA9837 CRC64; MTMILSILSL FFIIRLLFLA VSIKHEKALI AKGAKQYGKT NSTVLAAVHT LYYLACFVWV WLSDTAFNGI SLIGTLTVMA SFVILSLIIK QLGEIWTVKI YILPNHQINR SWLFKTFRHP NYFLNIIPEL IGIALLCQAW YVLLIGLPIY LLVLFKRIRQ EEQAMATLF // ID Q5F9R4_NEIG1 Unreviewed; 312 AA. AC Q5F9R4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=D-alanyl-D-alanine endopeptidase {ECO:0000313|EMBL:AAW89073.1}; GN ORFNames=NGO_0327 {ECO:0000313|EMBL:AAW89073.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89073.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89073.1; -; Genomic_DNA. DR RefSeq; WP_003687718.1; NC_002946.2. DR RefSeq; YP_207485.1; NC_002946.2. DR ProteinModelPortal; Q5F9R4; -. DR MEROPS; S11.007; -. DR EnsemblBacteria; AAW89073; AAW89073; NGO_0327. DR GeneID; 3283042; -. DR KEGG; ngo:NGO0327; -. DR PATRIC; 20333645; VBINeiGon24812_0400. DR HOGENOM; HOG000199620; -. DR KO; K07262; -. DR OMA; ESKMSIH; -. DR OrthoDB; EOG6RJV2H; -. DR BioCyc; NGON242231:GI2G-308-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256635. FT DOMAIN 70 291 Peptidase_S11. FT {ECO:0000259|Pfam:PF00768}. SQ SEQUENCE 312 AA; 34152 MW; 8E68987C608D1732 CRC64; MSIRTLKRLP SSLLLGLCLS LPSAHLFADN DILGQFLEQN MLTSSDPIEI FAESTIYPAD TQAITGGLIL SSQSALVVNN KTGQILYQKN ADRIMPIASI SKLMSAMVVL DANLDMNETV TITPDEIDRL KGTGSRLAIG TALTRKELLH LSLMSSENRA THALGRTYPG GMGAFVAAMN RKAQSLGMYG SRFYEPTGLN FQNVSTAKDL SLMVNAAAQY PQIRTNSTSN YASVQTKNGQ QNYKNSNALV REGMWNIELQ KTGYIREAGR SMVVKANIQN QPVTIVLLNS PTSATRVNDA RKIESWMLQQ RS // ID Q5F909_NEIG1 Unreviewed; 383 AA. AC Q5F909; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=ATPase {ECO:0000313|EMBL:AAW89328.1}; GN ORFNames=NGO_0598 {ECO:0000313|EMBL:AAW89328.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89328.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89328.1; -; Genomic_DNA. DR RefSeq; WP_003688944.1; NC_002946.2. DR RefSeq; YP_207740.1; NC_002946.2. DR ProteinModelPortal; Q5F909; -. DR EnsemblBacteria; AAW89328; AAW89328; NGO_0598. DR GeneID; 3282552; -. DR KEGG; ngo:NGO0598; -. DR PATRIC; 20334272; VBINeiGon24812_0708. DR HOGENOM; HOG000259599; -. DR KO; K06916; -. DR OMA; MRTHFHR; -. DR OrthoDB; EOG63NMFD; -. DR BioCyc; NGON242231:GI2G-568-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 383 AA; 43769 MW; DE5A13462110E848 CRC64; MNNRDQLFKA PPFENHSPLT WYQAASQLPN FIRDDAQAAA IEHLDRLWTE LMMFKRKRNR FLGRSLRSPQ VPKGLYFYGG VGRGKSFLMD AFFGCLPYRR KRRVHFHAFM AEIHRRLKAL KSESNPLKSV AAEITKETRV LCFDEFHVSD IADAMILGRL LENLLNEGVV LVATSNYAPS ELYPQGQNRS GFLPTIALIE SSLTVLNVDG GEDYRLRTLR PAEIFFTPAN EENEAKLAKL FKEMTGITDL NPGISTIHGR EIPHKAESGR TIWFDFRALC FSPRSQSDYL YLAEHYEMVF ISGLEQLSPQ EKAEARRLTW LIDVLYDFRV KLCATGAVDV NHIYTEGDFA EEFTRTASRM VEMQSEVYLE QPHLTLSPKA SGG // ID Q5F888_NEIG1 Unreviewed; 177 AA. AC Q5F888; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89599.1}; GN ORFNames=NGO_0901 {ECO:0000313|EMBL:AAW89599.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89599.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89599.1; -; Genomic_DNA. DR RefSeq; WP_010358242.1; NC_002946.2. DR RefSeq; YP_208011.1; NC_002946.2. DR ProteinModelPortal; Q5F888; -. DR MEROPS; C40.006; -. DR EnsemblBacteria; AAW89599; AAW89599; NGO_0901. DR GeneID; 3281599; -. DR KEGG; ngo:NGO0901; -. DR PATRIC; 20334983; VBINeiGon24812_1061. DR HOGENOM; HOG000229978; -. DR OMA; KMARFAF; -. DR OrthoDB; EOG6GTZPF; -. DR BioCyc; NGON242231:GI2G-841-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 65 171 NLPC_P60. {ECO:0000259|Pfam:PF00877}. SQ SEQUENCE 177 AA; 19266 MW; D11CAFF24919642C CRC64; MFSPDKTLFL CLGALLLASC GTTSGKHRQP KPKQTVRQIQ AVRISHIGRT QGSQELMLHS LGLIGTPYKW GGSSTATGFD CSGMIQFVYK NALNVKLPRT ARDMAAASRK IPDSRLKAGD LVFFNTGGAH RYSHVGLYIG NGEFIHAPGS GKTIKTEKLS TPFYAKNYLG AHTFFTE // ID Q5F9A9_NEIG1 Unreviewed; 77 AA. AC Q5F9A9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89228.1}; GN ORFNames=NGO_0490 {ECO:0000313|EMBL:AAW89228.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89228.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89228.1; -; Genomic_DNA. DR RefSeq; WP_010951061.1; NC_002946.2. DR RefSeq; YP_207640.1; NC_002946.2. DR EnsemblBacteria; AAW89228; AAW89228; NGO_0490. DR GeneID; 3282957; -. DR KEGG; ngo:NGO0490; -. DR OrthoDB; EOG6TBHPG; -. DR BioCyc; NGON242231:GI2G-468-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 77 AA; 8719 MW; 0CDFD1005A260AF4 CRC64; MKSKTEAEKS HLQKVADIGC IVCRNCGRFG VPAEVRHIRN GAGAGCGRIW NHLGVLMYRT AWRIVRKGKF RRPSRKV // ID Q5F893_NEIG1 Unreviewed; 60 AA. AC Q5F893; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Cytochrome C oxidase subunit II {ECO:0000313|EMBL:AAW89594.1}; GN ORFNames=NGO_0895 {ECO:0000313|EMBL:AAW89594.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89594.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89594.1; -; Genomic_DNA. DR RefSeq; WP_003688481.1; NC_002946.2. DR RefSeq; YP_208006.1; NC_002946.2. DR EnsemblBacteria; AAW89594; AAW89594; NGO_0895. DR GeneID; 3281792; -. DR KEGG; ngo:NGO0895; -. DR PATRIC; 20334963; VBINeiGon24812_1051. DR HOGENOM; HOG000027916; -. DR OMA; NASAFGM; -. DR OrthoDB; EOG6M9F24; -. DR BioCyc; NGON242231:GI2G-836-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 60 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256061. SQ SEQUENCE 60 AA; 6740 MW; 91C985A9CED72146 CRC64; MFWYVIGFCA FVVALLSLWV NAGAFGMQED DTPQSDYEKR LGLGAKLKNK NTPKAGEKRQ // ID Q5F954_NEIG1 Unreviewed; 120 AA. AC Q5F954; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 58. DE SubName: Full=Endoribonuclease L-PSP {ECO:0000313|EMBL:AAW89283.1}; GN ORFNames=NGO_0549 {ECO:0000313|EMBL:AAW89283.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89283.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89283.1; -; Genomic_DNA. DR RefSeq; WP_010357712.1; NC_002946.2. DR RefSeq; YP_207695.1; NC_002946.2. DR ProteinModelPortal; Q5F954; -. DR EnsemblBacteria; AAW89283; AAW89283; NGO_0549. DR GeneID; 3282121; -. DR KEGG; ngo:NGO0549; -. DR PATRIC; 20334150; VBINeiGon24812_0647. DR HOGENOM; HOG000267214; -. DR OMA; TIIYLAD; -. DR OrthoDB; EOG6QVRPF; -. DR BioCyc; NGON242231:GI2G-523-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 120 AA; 13124 MW; 8E0E3B1F431F913F CRC64; MDIRYFGTTP RYSEAVCAGG LIFLSGMVPE NGETAAEQTA DVLAQTDRWL AECGSDKAHV LDAVIYLRDM GDYAEMNGVW DAWVAAGRTP ARACVEARLA RPEWRVEIKI TAVKRDAATA // ID Q5F5X4_NEIG1 Unreviewed; 330 AA. AC Q5F5X4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 75. DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417}; DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417}; GN ORFNames=NGO_1795 {ECO:0000313|EMBL:AAW90413.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90413.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90413.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5X4; -. DR SMR; Q5F5X4; 1-328. DR REBASE; 2790; M.NgoAII. DR EnsemblBacteria; AAW90413; AAW90413; NGO_1795. DR PATRIC; 20337240; VBINeiGon24812_2155. DR HOGENOM; HOG000225505; -. DR OMA; MANAKDY; -. DR OrthoDB; EOG6F294J; -. DR BioCyc; NGON242231:GI2G-1693-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Methyltransferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90413.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Restriction system {ECO:0000256|RuleBase:RU004244}; KW Transferase {ECO:0000256|RuleBase:RU000417, KW ECO:0000313|EMBL:AAW90413.2}. FT DOMAIN 1 326 SAM-dependent_MTases. FT {ECO:0000259|Pfam:PF00145}. SQ SEQUENCE 330 AA; 37222 MW; 0A384A98B1EB03E1 CRC64; MKIISLFSGC GGLDLGFEKA GFEIPAANEY DKTIWATFKA NHPKTHLIEG DIRKIKEEDF PEEIDGIIGG PPCQSWSEAG ALRGIDDARG QLFFDYIRIL KSKQPKFFLA ENVSGMLANR HNGAVQNLLK MFDGCGYDVT LTMANAKDYG VAQERKRVFY IGFRKDLEIK FSFPKGSTVE DKDKITLKDV IWDLQDTAVP SAPQNKTNPD AVNNNEYFTG SFSPIFMSRN RVKAWDEQGF TVQASGRQCQ LHPQAPKMEK HGANDYRFAA GKETLYRRMT VREVARIQGF PDNFKFIYQN VNDAYKMIGN AVPVNLAYEI AAAIKKTLER // ID Q5F803_NEIG1 Unreviewed; 161 AA. AC Q5F803; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89684.1}; GN ORFNames=NGO_1001 {ECO:0000313|EMBL:AAW89684.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89684.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89684.1; -; Genomic_DNA. DR RefSeq; WP_003706356.1; NC_002946.2. DR RefSeq; YP_208096.1; NC_002946.2. DR EnsemblBacteria; AAW89684; AAW89684; NGO_1001. DR GeneID; 3282576; -. DR KEGG; ngo:NGO1001; -. DR PATRIC; 20335204; VBINeiGon24812_1170. DR HOGENOM; HOG000009751; -. DR KO; K07464; -. DR OrthoDB; EOG6PCPX0; -. DR BioCyc; NGON242231:GI2G-927-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4. DR InterPro; IPR022765; Dna2/Cas4_DUF83. DR Pfam; PF01930; Cas_Cas4; 1. DR TIGRFAMs; TIGR00372; cas4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 20 157 Cas_Cas4. {ECO:0000259|Pfam:PF01930}. SQ SEQUENCE 161 AA; 18187 MW; DE29377E2C075585 CRC64; MTALLTETQR ENQDTRLIPL SALQHYAFCP RQCALIHNEQ AWAENYLTAQ GKALHERVDS DEPETCKGVR FEWTVHVLAD KLGISGILDL VEVDTKTGRL KPVEYKRGKP KPDPGDEIQL CAQGLCLEEM TGQTVSEGAL WYMQTRHRVP VVFSDGLRPL Q // ID Q5F9A3_NEIG1 Unreviewed; 715 AA. AC Q5F9A3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Phage head morphogenesis, SPP1 gp7 family domain protein {ECO:0000313|EMBL:AAW89234.1}; GN ORFNames=NGO_0496 {ECO:0000313|EMBL:AAW89234.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89234.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89234.1; -; Genomic_DNA. DR RefSeq; WP_003691423.1; NC_002946.2. DR RefSeq; YP_207646.1; NC_002946.2. DR ProteinModelPortal; Q5F9A3; -. DR EnsemblBacteria; AAW89234; AAW89234; NGO_0496. DR GeneID; 3282953; -. DR KEGG; ngo:NGO0496; -. DR PATRIC; 20334034; VBINeiGon24812_0589. DR OMA; TREMIRG; -. DR OrthoDB; EOG6N944X; -. DR BioCyc; NGON242231:GI2G-474-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR006944; Phage/GTA_portal. DR InterPro; IPR006528; Phage_head_morphogenesis. DR Pfam; PF04233; Phage_Mu_F; 1. DR Pfam; PF04860; Phage_portal; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 596 704 Phage_Mu_F. {ECO:0000259|Pfam:PF04233}. SQ SEQUENCE 715 AA; 78894 MW; 8F943AF0D2E147ED CRC64; MSKKTPLSQG FIARVAAGVR YAFTGNADGW FDAGEPPAPA AQQAEGRRFD YEPFYNVGHS KPREREAVGF AQLRALADNY DVLRLVIEAR KDQMECLKWT IQKRDVESTE DDESQRKDRK VDEAVAFFRS PDKEHTWADW LRILLEDLFV IDAPCIYPRK TLGGGLYALE VMDGATIKRV LDNTGRMPLP PDTAYQQILH GMAAVDYTAD ELIYRSRNNR SYKVYGYSPV EQIIMTVNIA LKRQVHALEY YTAGSVPDAL VGVPETWSAD DIRRFQEYWD LLLSGETAQR RKMRFVPGEL SRNFRETKQP PLKDVYDEWL ARVVCFAFSV EPTPFVAQVN RSVAETSREQ SLSDGMGSLK NWVKALIDDV LARYMDMAAY EFVWKGEESL NPKEQAEIYA IYKNAGILTA DEIRAELGKE PLPGQGQPEP DKQDGRKPEE PPNQGAEKLG KSESPMSEDE SAALIEAYLL TRIDGLAEQI AALIEGAAVD WQAGDLAAEL SRAAGVVANG LDFGDWSGLS DVVEPIIRRV AEDGAVAALL RVMPEPAAGM VTNIRSRAVK WAHERAAEMV GMKRAGGGLV RNPAAEWQIT EGTREMIRAQ VAEAMRNGDS VQELAGRLKE SHAFGNARAR TIARTETAMA DGMGNLIGWE GTGLVAGKQW ITAKDDKVSD VCNANGGMGV IGLHEPFSHG ALTIPGHPNC RCAVVPVLAG DMPES // ID Q5F5S6_NEIG1 Unreviewed; 63 AA. AC Q5F5S6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90461.1}; GN ORFNames=NGO_1839 {ECO:0000313|EMBL:AAW90461.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90461.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90461.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90461; AAW90461; NGO_1839. DR PATRIC; 20337352; VBINeiGon24812_2211. DR OrthoDB; EOG6RJVFH; -. DR BioCyc; NGON242231:GI2G-1741-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 7287 MW; D2906FCBE1BF65EB CRC64; MPRLAVLFVL SAASSLCPDL NLIHYILNNK ELNLEERHDL ERAVKILQDT HVIPVCRRKM HTP // ID Q5F7T1_NEIG1 Unreviewed; 157 AA. AC Q5F7T1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Phage structural protein {ECO:0000313|EMBL:AAW89756.1}; GN ORFNames=NGO_1089 {ECO:0000313|EMBL:AAW89756.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89756.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89756.1; -; Genomic_DNA. DR RefSeq; WP_010951177.1; NC_002946.2. DR RefSeq; YP_208168.1; NC_002946.2. DR EnsemblBacteria; AAW89756; AAW89756; NGO_1089. DR GeneID; 3281578; -. DR KEGG; ngo:NGO1089; -. DR PATRIC; 20335430; VBINeiGon24812_1281. DR HOGENOM; HOG000225128; -. DR OMA; RIRCQSA; -. DR OrthoDB; EOG6V1M5V; -. DR BioCyc; NGON242231:GI2G-1001-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 157 AA; 16399 MW; B0F1F71B70D28AFC CRC64; MARIHVRNNG GNRFGGVPYG NLAAEHYCIV AKQDGAILGA DAYGPPKDGD VLALGVLEQG FRLDDAQIIV KTAMSSGITA DVGFAYADGA DDAHVPQDAA YFASGADFAS AGRIRCQSAK LVTLPKQALL TVTLKGAENK KAADIDILIY GEKFGQL // ID Q5F615_NEIG1 Unreviewed; 118 AA. AC Q5F615; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. 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 ORFNames=NGO_1751 {ECO:0000313|EMBL:AAW90372.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90372.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90372.1; -; Genomic_DNA. DR RefSeq; WP_010951338.1; NC_002946.2. DR RefSeq; YP_208784.1; NC_002946.2. DR EnsemblBacteria; AAW90372; AAW90372; NGO_1751. DR GeneID; 3281406; -. DR KEGG; ngo:NGO1751; -. DR PATRIC; 20337104; VBINeiGon24812_2092. DR HOGENOM; HOG000100119; -. DR KO; K00330; -. DR OMA; MKGALEW; -. DR OrthoDB; EOG6QVRQ6; -. DR BioCyc; NGON242231:GI2G-1647-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01394, KW ECO:0000256|RuleBase:RU003639}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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, KW ECO:0000313|EMBL:AAW90372.1}. 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; 13643 MW; 6277C8C4B56BBD09 CRC64; MLSAYFPVFV FILVGLAAGV LFILLGTILG PKRHYAEKDA PYKCGFESFE NARMKFDVRY YLVDILFILF DLEVAFMLPW AVVFKDLGAY GFWSMLVFIV VLTVGFVYEW KKGALEWE // ID Q5F9N2_NEIG1 Unreviewed; 405 AA. AC Q5F9N2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. DE SubName: Full=Heme biosynthesis protein HemY {ECO:0000313|EMBL:AAW89105.1}; GN ORFNames=NGO_0361 {ECO:0000313|EMBL:AAW89105.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89105.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89105.1; -; Genomic_DNA. DR RefSeq; WP_003698136.1; NC_002946.2. DR RefSeq; YP_207517.1; NC_002946.2. DR ProteinModelPortal; Q5F9N2; -. DR EnsemblBacteria; AAW89105; AAW89105; NGO_0361. DR GeneID; 3283029; -. DR KEGG; ngo:NGO0361; -. DR PATRIC; 20333717; VBINeiGon24812_0436. DR HOGENOM; HOG000263403; -. DR KO; K02498; -. DR OMA; MACETLL; -. DR OrthoDB; EOG6MPWRV; -. DR BioCyc; NGON242231:GI2G-340-MONOMER; -. DR Proteomes; UP000000535; 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; -; 3. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 405 AA; 45199 MW; CFE21A2B8C25919F CRC64; MKTVVWIVVL FAAAVGLALA SGIYTGDVYI VLGQTMLRIN LHAFVLGSLI AVVVWYFLFK FIIGVLNIPE NMRRSGSARK GRKAALALNK AGLAYFEGRF EKAELEASRV LGNKEAGDNR TLALMLGAHA AGQMENIELR DRYLAEIAKL PEKQQLSRYL LLAESALNRR DYEAAEANLH AAAKMNANLT RLVRLQLRYA FDRGDALQVL AKTEKLSKAG ALGKSEMERY QNWAYRRQMA DAADAAALKT CLKRIPDSLK NGELSVSVAE KYERLGLYAD AVKWVKQHYP HNRRPELLEA FVESVRFLGE REQQKAIDFA DSWLKEQPDN ALLLMYLGRL AYGRKLWGKA KGYLEASIAL KPSIPARLVL AKVFDETAQS QKAEAQRNLV LASVAGENRP SAETR // ID Q5F6Y4_NEIG1 Unreviewed; 198 AA. AC Q5F6Y4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 51. DE SubName: Full=Peptidase {ECO:0000313|EMBL:AAW90053.2}; GN ORFNames=NGO_1408 {ECO:0000313|EMBL:AAW90053.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90053.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90053.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90053; AAW90053; NGO_1408. DR PATRIC; 20336223; VBINeiGon24812_1660. DR HOGENOM; HOG000255677; -. DR OMA; RSPYPML; -. DR OrthoDB; EOG6JHRKB; -. DR BioCyc; NGON242231:GI2G-1318-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR009858; DUF1415. DR Pfam; PF07209; DUF1415; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 198 AA; 21910 MW; DDCF3C3275E27CD1 CRC64; MNIDTSENKD AVAEHTGQWL EKAVIGLNLC PFAKAPHVKN LVRIAISEAK HLDGFLEDLD EELQRLGNTP ATELETTLLV HPTLFPDFDV FNDMLDIADA AVVENGLEGI VQIAPFHPYF QFEGTDSDGI GNYTNRSPYP TLHLIREDSI AKAAQAFPDA SAIFERNIAL LEKMGHEGWA KLGITSCPYP HNKKNISK // ID Q5FA71_NEIG1 Unreviewed; 63 AA. AC Q5FA71; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88916.1}; GN ORFNames=NGO_0160 {ECO:0000313|EMBL:AAW88916.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88916.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88916.1; -; Genomic_DNA. DR RefSeq; WP_003704485.1; NC_002946.2. DR RefSeq; YP_207328.1; NC_002946.2. DR EnsemblBacteria; AAW88916; AAW88916; NGO_0160. DR GeneID; 3281354; -. DR KEGG; ngo:NGO0160; -. DR PATRIC; 20333243; VBINeiGon24812_0204. DR HOGENOM; HOG000027907; -. DR OrthoDB; EOG6KMBCQ; -. DR BioCyc; NGON242231:GI2G-146-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 63 AA; 6997 MW; 47601ACE2A84CE5D CRC64; MLPTRSVSSL LLGEYLEFEE NGTKITAEIG SAWHFLGAAC RISINGKYYA GNRIVWFAKK AES // ID Q5F582_NEIG1 Unreviewed; 171 AA. AC Q5F582; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 50. DE SubName: Full=Lipoprotein {ECO:0000313|EMBL:AAW90655.2}; GN ORFNames=NGO_2047 {ECO:0000313|EMBL:AAW90655.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90655.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90655.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90655; AAW90655; NGO_2047. DR PATRIC; 20337889; VBINeiGon24812_2467. DR HOGENOM; HOG000218695; -. DR OMA; CNGKPTL; -. DR OrthoDB; EOG68DD0V; -. DR BioCyc; NGON242231:GI2G-1949-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoprotein {ECO:0000313|EMBL:AAW90655.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 133 160 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 171 AA; 19136 MW; 2B7FB8B4C1BF1CA6 CRC64; MKQMLLAVGV AAVLAGCGKD AGGYEGYWRE KSDKKEGVIA VKKKGNYFLN KINVFTGKEE SLLLSEKDGA LSINTGIGEI PIKLSDDGKE LYVERRRYVK TDAAMKDKII AHQKKCGQTA QAYLDARNAL PSNQTYQQRQ AAIEQLKRRF EAEFDELEKE IKCNGKPTLL F // ID Q5F7S0_NEIG1 Unreviewed; 80 AA. AC Q5F7S0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89767.1}; GN ORFNames=NGO_1100 {ECO:0000313|EMBL:AAW89767.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89767.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89767.1; -; Genomic_DNA. DR RefSeq; WP_003706439.1; NC_002946.2. DR RefSeq; YP_208179.1; NC_002946.2. DR EnsemblBacteria; AAW89767; AAW89767; NGO_1100. DR GeneID; 3282527; -. DR KEGG; ngo:NGO1100; -. DR PATRIC; 20335454; VBINeiGon24812_1293. DR OrthoDB; EOG6CVVBH; -. DR BioCyc; NGON242231:GI2G-1012-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 9204 MW; B5B2C06EE5BB9458 CRC64; MPRLSDEDWR KVELDYRRGV LSIAEIGRKY NVSAQHVGRV AKERVWTRDL NDEVQAKARA MVLSADKNGN APDYADFNLK // ID Q5F809_NEIG1 Unreviewed; 183 AA. AC Q5F809; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 79. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89678.1}; GN ORFNames=NGO_0994 {ECO:0000313|EMBL:AAW89678.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89678.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3AY2} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-183 IN COMPLEX WITH ZINC, RP AND DISULFIDE BONDS. RA Hashimoto W., Ochiai A., Yamada T., Chakrabarty A.M., Murata K.; RT "Crystal structure of Neisserial Azurin."; RL Submitted (APR-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; AE004969; AAW89678.1; -; Genomic_DNA. DR RefSeq; WP_003688275.1; NC_002946.2. DR RefSeq; YP_208090.1; NC_002946.2. DR PDB; 3AY2; X-ray; 1.90 A; A/B=17-183. DR PDBsum; 2N0M; -. DR PDBsum; 3AY2; -. DR ProteinModelPortal; Q5F809; -. DR SMR; Q5F809; 58-181. DR EnsemblBacteria; AAW89678; AAW89678; NGO_0994. DR GeneID; 3281780; -. DR KEGG; ngo:NGO0994; -. DR PATRIC; 20335192; VBINeiGon24812_1164. DR HOGENOM; HOG000280572; -. DR OMA; KSCKTFT; -. DR OrthoDB; EOG6G20MV; -. DR BioCyc; NGON242231:GI2G-921-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3AY2}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Metal-binding {ECO:0000213|PDB:3AY2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000213|PDB:3AY2}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 183 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255530. FT DOMAIN 58 181 Copper-bind. {ECO:0000259|Pfam:PF00127}. FT METAL 101 101 Zinc; via carbonyl oxygen. FT {ECO:0000213|PDB:3AY2}. FT METAL 102 102 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:3AY2}. FT METAL 166 166 Zinc. {ECO:0000213|PDB:3AY2}. FT METAL 171 171 Zinc; via pros nitrogen. FT {ECO:0000213|PDB:3AY2}. FT DISULFID 59 82 {ECO:0000213|PDB:3AY2}. SQ SEQUENCE 183 AA; 18532 MW; 50EEAB89163277EC CRC64; MKAYLALISA AVIGLAACSQ EPAAPAAEAT PAGEAPASEA PAAEAAPADA AEAPAAGNCA ATVESNDNMQ FNTKDIQVSK ACKEFTITLK HTGTQPKASM GHNLVIAKAE DMDGVFKDGV GAADTDYVKP DDARVVAHTK LIGGGEESSL TLDPAKLADG DYKFACTFPG HGALMNGKVT LVD // ID Q5F9K9_NEIG1 Unreviewed; 94 AA. AC Q5F9K9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Ribosome assembly protein YhbY {ECO:0000313|EMBL:AAW89128.1}; GN ORFNames=NGO_0384 {ECO:0000313|EMBL:AAW89128.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89128.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89128.1; -; Genomic_DNA. DR RefSeq; WP_003690833.1; NC_002946.2. DR RefSeq; YP_207540.1; NC_002946.2. DR ProteinModelPortal; Q5F9K9; -. DR EnsemblBacteria; AAW89128; AAW89128; NGO_0384. DR GeneID; 3282564; -. DR KEGG; ngo:NGO0384; -. DR PATRIC; 20333773; VBINeiGon24812_0464. DR HOGENOM; HOG000016279; -. DR OMA; NKQLSNV; -. DR OrthoDB; EOG6SBT94; -. DR BioCyc; NGON242231:GI2G-363-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 94 CRM. {ECO:0000259|PROSITE:PS51295}. SQ SEQUENCE 94 AA; 10530 MW; 5A03B067EA6032FC CRC64; MADTKLNTKE ILELKARAHH LHPVVMVGQQ GLTDAVIKET DAALTAHELI KVRVFGDDRA ERIEICNTLC EAVDAQPVRH IGKLLVLWRK NIEA // ID Q5F5H8_NEIG1 Unreviewed; 112 AA. AC Q5F5H8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90559.1}; GN ORFNames=NGO_1947 {ECO:0000313|EMBL:AAW90559.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90559.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90559.1; -; Genomic_DNA. DR RefSeq; WP_003705166.1; NC_002946.2. DR RefSeq; YP_208971.1; NC_002946.2. DR EnsemblBacteria; AAW90559; AAW90559; NGO_1947. DR GeneID; 3282673; -. DR KEGG; ngo:NGO1947; -. DR PATRIC; 20337639; VBINeiGon24812_2346. DR HOGENOM; HOG000218683; -. DR OMA; KSAQGSC; -. DR BioCyc; NGON242231:GI2G-1849-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 112 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256024. SQ SEQUENCE 112 AA; 10479 MW; 8904A30F0A0B3756 CRC64; MNKNIAAALA GALSLSLAAG AVAAHKPASN ATGVQKSAQG SCGASKSAEG SCGASKSAEG SCGAAASKAG EGKCGEGKCG ATVKKAHKHT KASKAKAKSA EGKCGEGKCG SK // ID Q5F5X5_NEIG1 Unreviewed; 375 AA. AC Q5F5X5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 55. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90412.2}; GN ORFNames=NGO_1793 {ECO:0000313|EMBL:AAW90412.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90412.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90412.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90412; AAW90412; NGO_1793. DR PATRIC; 20337234; VBINeiGon24812_2152. DR HOGENOM; HOG000218658; -. DR OMA; QRTHRNI; -. DR OrthoDB; EOG6XWTZW; -. DR BioCyc; NGON242231:GI2G-1692-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 42400 MW; 710E7E90284FD4E1 CRC64; MNSSQRKRLS GRWLNSYERY RHRRLIHAVR LGGTVLFATA LARLLHLQHG EWIGMTVFVV LGMLQFQGAI YSKAVERMLG TVIGLGAGLG VLWLNQHYFH GNLLFYLTIG TASALAGWAA VGKNGYVPML AGLTMCMLIG DNGSEWLDSG LMRAMNVLIG AAIAIAAAKL LPLKSTLMWR FMLADNLADC SKMIAEISNG RRMTRERLEQ NMVKMRQINA RMVKSRSHLA ATSGESRISP SMMEAMQHAH RKIVNTTELL LTTAAKLQSP KLNGSEIRLL DRHFTLLQTD LQQTAALING RHARRIRIDT AINPELEALA EHLHYQWQGF LWLSTNMRQE ISALVILLQR TRRKWLDAHE RQHLRQSLLE TREHG // ID Q5F846_NEIG1 Unreviewed; 98 AA. AC Q5F846; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89641.1}; GN ORFNames=NGO_0950 {ECO:0000313|EMBL:AAW89641.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89641.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89641.1; -; Genomic_DNA. DR RefSeq; WP_003688350.1; NC_002946.2. DR RefSeq; YP_208053.1; NC_002946.2. DR EnsemblBacteria; AAW89641; AAW89641; NGO_0950. DR GeneID; 3282129; -. DR KEGG; ngo:NGO0950; -. DR PATRIC; 20335083; VBINeiGon24812_1111. DR OrthoDB; EOG680X49; -. DR BioCyc; NGON242231:GI2G-883-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 35 54 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 98 AA; 11430 MW; 91FC189182336567 CRC64; MLDLRAGACA ILNQALPRRL EGRGLTVRKQ WQSGLFLSDI VWVFFSMIYF RLFMQYFPID GFYRDFSAFA FRGGLCFVRD VACRDVRIVR SNMGEDDV // ID Q5F544_NEIG1 Unreviewed; 323 AA. AC Q5F544; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 58. DE SubName: Full=Iron ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW90693.1}; GN ORFNames=NGO_2092 {ECO:0000313|EMBL:AAW90693.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90693.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90693.1; -; Genomic_DNA. DR RefSeq; WP_010951405.1; NC_002946.2. DR RefSeq; YP_209105.1; NC_002946.2. DR ProteinModelPortal; Q5F544; -. DR PRIDE; Q5F544; -. DR EnsemblBacteria; AAW90693; AAW90693; NGO_2092. DR GeneID; 3282825; -. DR KEGG; ngo:NGO2092; -. DR PATRIC; 20338019; VBINeiGon24812_2532. DR HOGENOM; HOG000099140; -. DR KO; K02016; -. DR OMA; AWKKGQV; -. DR OrthoDB; EOG61VZ9F; -. DR BioCyc; NGON242231:GI2G-1987-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 61 323 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. SQ SEQUENCE 323 AA; 34407 MW; F5A3539CB8213182 CRC64; MLRLTALTLC TVLALGACSP QNSDPAPQAK EQAVSAAQSE SASVTVKTAR GDVQIPQNPE RIAVYDLGML DTLSKLGVKT GLSVDKNRLP YLEEYFKTTK PAGTLFDPDY ETLNAYKPQL IIIGSRAAKA FDKLNEIAPT IEMTADTANL KESAKERIDA LAQIFGKQAE ADKLKAEIDA SFEAAKTAAQ GKGKGKGLVV LVNGGKMSAF GPSSRLGGWL HKDIGVPAVD ESIKEGSHGQ PISFEYLKEK NPDWLFVLDR SAAIGEEGQA AKDVLNNPLV AETTAWKKGQ VVYLVPETYL AAGGAQELLN ASKQVADAFN AAK // ID Q5FA37_NEIG1 Unreviewed; 431 AA. AC Q5FA37; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 61. DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW88950.2}; GN ORFNames=NGO_0197 {ECO:0000313|EMBL:AAW88950.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88950.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88950.2; -; Genomic_DNA. DR RefSeq; WP_003687505.1; NC_002946.2. DR RefSeq; YP_207362.2; NC_002946.2. DR ProteinModelPortal; Q5FA37; -. DR EnsemblBacteria; AAW88950; AAW88950; NGO_0197. DR GeneID; 3281682; -. DR KEGG; ngo:NGO0197; -. DR PATRIC; 20333323; VBINeiGon24812_0244. DR HOGENOM; HOG000185563; -. DR KO; K09471; -. DR OMA; AKVPHIT; -. DR OrthoDB; EOG67DPGV; -. DR BioCyc; NGON242231:GI2G-180-MONOMER; -. DR Proteomes; UP000000535; 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; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 35 387 DAO. {ECO:0000259|Pfam:PF01266}. SQ SEQUENCE 431 AA; 48427 MW; 04E748CBC09DBE35 CRC64; MIRPDFQEYL PSYYFSSVNP HTVYPKLQCR LKAETCIIGG GLSGLCTALP LAEHGHEAVV LEAARIGFGA SGRSGGQVIS DYACGMGEIE KQVGLEQAQW FWQQSLQAVE LVDERVRKHA IDCDWQRGYA TVAVRPQHWE ELQQWHEHAQ RHYGASHYQL WDKAELKQQL DSDMYQGAQF DPLSGHLHPL NYTLGVASAA AEAGAQIFEQ SPMTRIEPYQ NGWLVYTPEG SVECKNVVYA VNTYVGLNPI FRPLERKAIA VSTFIIATEP LGARTKGLIR NNMAVCDNRH ILDYYRLSAD GRLLFGGKDN EFIDNPARMT ELVRQDMLKV FPQLADVRIE YSWGGECDIT ANLVPHFGRL TSNVFYTQGY SGHGMAITGI AGLAVAEAIL GDECRLKPFE QLCQPNIILQ PFLRKLGSFL GSKYYQWKDS R // ID Q5F6Q3_NEIG1 Unreviewed; 703 AA. AC Q5F6Q3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 53. DE SubName: Full=Transferrin-binding protein 2 {ECO:0000313|EMBL:AAW90134.1}; GN ORFNames=NGO_1496 {ECO:0000313|EMBL:AAW90134.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90134.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90134.1; -; Genomic_DNA. DR RefSeq; WP_010951284.1; NC_002946.2. DR RefSeq; YP_208546.1; NC_002946.2. DR ProteinModelPortal; Q5F6Q3; -. DR EnsemblBacteria; AAW90134; AAW90134; NGO_1496. DR GeneID; 3281568; -. DR KEGG; ngo:NGO1496; -. DR PATRIC; 20336456; VBINeiGon24812_1775. DR HOGENOM; HOG000220760; -. DR OMA; VNQAAMV; -. DR OrthoDB; EOG6XHC16; -. DR BioCyc; NGON242231:GI2G-1400-MONOMER; -. DR Proteomes; UP000000535; 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; 3. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 703 AA; 75245 MW; 503DB8D79DEC0F03 CRC64; MNNPLVNQAA MVLPVFLLSA CLGGGGSFDL DSVDTEAPRP APKYQDVPSK KPEARKDQGG YGFAMRFKRR NWYPPSNPKE NEIRLSEGDW EQTGNGNIKN PSKQKNIIDA LSGNGEAPLQ DSSQQGEGIS KVTDYHDFKY VWSGFFYKQI GNTIKKDDSS SKIIEARNGP DGYIFYKGTD PSRKLPVSGS VEYKGTWDFL TDVQANQKFT DLGSAFTKSG DRYSAFSGEL DYIVRKEEDK KDGHVGLGLT TEITVNFEKK TLSGKLIKNN MVINNGDEPT TQYYSLEAQV TGNRFNGKAM VTDKPENSKS KQHPFVSDSS SLSGGFFGPQ GEELGFRFLS NDNKVAVVGS AKTKDETASS GGTSGGASVS ASNGATGTSS GNSNLTTVLD AVELTPDGKE IKDLDNFSNA AQLVVDGIMI PLLSTESGNG QADKGKNGGT DFTYTTTYMP ESDKKDTKAQ TGAGGMQTAS DAAGVNGGQA GTKTYKVEAC CSNLNYLKYG LLTRENSNSV MQTVRNSSQA AARTAQGAQS MFLQGERTDE KEIPKEQKVV YLGTWYGHIA ANGTSWTGNA SDQQSGNRAK FDVNFKDKKI TGTLTAANRQ EATFTIDAMI DDNGFKGTAK TGNDGFAPDQ NSSTGTYKVH IANAEVQGGF YGPNAEELGG WFAYPGNGQT KNAQENAQAS SGNGNSAVSA TVVFGAKRQQ LVK // ID Q5F7M1_NEIG1 Unreviewed; 386 AA. AC Q5F7M1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=O-succinylhomoserine sulfhydrolase {ECO:0000313|EMBL:AAW89816.1}; GN ORFNames=NGO_1149 {ECO:0000313|EMBL:AAW89816.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89816.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89816.1; -; Genomic_DNA. DR RefSeq; WP_010951202.1; NC_002946.2. DR RefSeq; YP_208228.1; NC_002946.2. DR ProteinModelPortal; Q5F7M1; -. DR EnsemblBacteria; AAW89816; AAW89816; NGO_1149. DR GeneID; 3282146; -. DR KEGG; ngo:NGO1149; -. DR PATRIC; 20335558; VBINeiGon24812_1344. DR HOGENOM; HOG000246417; -. DR KO; K10764; -. DR OMA; MTSQFAR; -. DR OrthoDB; EOG67DPN3; -. DR BioCyc; NGON242231:GI2G-1062-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89816.1}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT MOD_RES 207 207 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR001434-2}. SQ SEQUENCE 386 AA; 41574 MW; F279B93494D98534 CRC64; MSKKLHPQTL AIRGGKEQTG YREHNQALFL TSSFMWDNAQ HAADLFSKKI KGFTYTRTAN PTIAAFEKRI AALEGAERAV ATSTGMSAIQ AAFFTFLQAG DHVVSSRSLF GTTVGFINNI VTKFGIGVSR VSPTDINEWK AAVKANTKLL FLETPSNPLG EVADLEALAE LAHGIGALLV VDNSLLSPVG SQPLKHGADI SVSSATKAID GHGRVMGGVL AGSEELMAQV AVYCNSCGLA MSPFNAWQLL SGVETLSLRM EKQFDNALRI AQWLQEQPQV QAVYYTGLPD HPQAELIRKQ QNGGGIVIGF EVADQAAAWK VVELFSRTAN LGDVRSTITN PWTTTHGRMQ PEEKLAAGIR PGLVRLSVGL EYVGDLIDDL KQALAR // ID Q5FA62_NEIG1 Unreviewed; 291 AA. AC Q5FA62; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 73. DE SubName: Full=Zinc ABC transporter permease {ECO:0000313|EMBL:AAW88925.2}; GN ORFNames=NGO_0169 {ECO:0000313|EMBL:AAW88925.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88925.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88925.2; -; Genomic_DNA. DR RefSeq; WP_003692612.1; NC_002946.2. DR RefSeq; YP_207337.2; NC_002946.2. DR ProteinModelPortal; Q5FA62; -. DR EnsemblBacteria; AAW88925; AAW88925; NGO_0169. DR GeneID; 3281401; -. DR KEGG; ngo:NGO0169; -. DR PATRIC; 20333259; VBINeiGon24812_0212. DR HOGENOM; HOG000181428; -. DR KO; K02075; -. DR OMA; GVFVVWR; -. DR OrthoDB; EOG6GR389; -. DR BioCyc; NGON242231:GI2G-155-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003943}. FT TRANSMEM 16 38 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 45 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 180 196 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 273 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 291 AA; 30988 MW; 442A3F4BB448AE5E CRC64; MNLYDLLLAP FAEFDFMHYA LASVFCLSLS AAPVGVFLVM RRMSLIGDAL SHAVLPGAAV GYMFAGLSLP AMGVGGFAAG MLMALLAGLV SRFTTLKEDA NFAAFYLSSL AIGVILISKN GSSVDLLHLL FGSVLAVDIP ALQLIAAVSG LTLITLAVIY RPLVLESIDP LFLKSVNGKG GLWHVIFLIL VVMNLVSGFQ ALGILMSVGL MMLPAITARL WARNMGTLIL LSVLIALFCG LIGLLISYHI EIPSGPAIIL CCSVLYLFSV ILGKEGGILP KWFKNHRHHT T // ID Q5F9G7_NEIG1 Unreviewed; 218 AA. AC Q5F9G7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:AAW89170.1}; GN ORFNames=NGO_0427 {ECO:0000313|EMBL:AAW89170.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89170.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89170.1; -; Genomic_DNA. DR RefSeq; WP_003687878.1; NC_002946.2. DR RefSeq; YP_207582.1; NC_002946.2. DR ProteinModelPortal; Q5F9G7; -. DR EnsemblBacteria; AAW89170; AAW89170; NGO_0427. DR GeneID; 3281937; -. DR KEGG; ngo:NGO0427; -. DR PATRIC; 20333869; VBINeiGon24812_0512. DR HOGENOM; HOG000218674; -. DR KO; K06992; -. DR OMA; EENPIAY; -. DR OrthoDB; EOG6PZXBB; -. DR BioCyc; NGON242231:GI2G-405-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256084. FT DOMAIN 53 176 Peptidase C39. FT {ECO:0000259|PROSITE:PS50990}. SQ SEQUENCE 218 AA; 24501 MW; 643D924C23AEF5C7 CRC64; MEQKRRFAAS LLLAAALPLC AHSFPFAEEN PIAYGKVKIQ SWKARRDFNI VKQDLDFSCG AASVATLLNN FYGQTLTEEE VLEKLGKEQM RASFEDMRRI MPDLGFEAKG YALSFEQLAQ LKIPVIVYLK YRKDDHFSVL RGIGGNTVLL ADPSPGHVSM SRAQFLEAWQ TREGNLAGKI LAVVPKKAEA ISNKLFFTHH PKRQTEFAVG QIRQGRAE // ID Q5FAG4_NEIG1 Unreviewed; 146 AA. AC Q5FAG4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 75. DE SubName: Full=Homoprotocatechuate degradative operon repressor {ECO:0000313|EMBL:AAW88823.2}; GN ORFNames=NGO_0058 {ECO:0000313|EMBL:AAW88823.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88823.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88823.2; -; Genomic_DNA. DR RefSeq; WP_003687296.1; NC_002946.2. DR RefSeq; YP_207235.2; NC_002946.2. DR ProteinModelPortal; Q5FAG4; -. DR EnsemblBacteria; AAW88823; AAW88823; NGO_0058. DR GeneID; 3282324; -. DR KEGG; ngo:NGO0058; -. DR PATRIC; 20332966; VBINeiGon24812_0067. DR HOGENOM; HOG000221451; -. DR OMA; RMESMEL; -. DR OrthoDB; EOG6TN46N; -. DR BioCyc; NGON242231:GI2G-52-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000702, KW ECO:0000256|SAAS:SAAS00487313}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 16615 MW; A4548DDAA8791D47 CRC64; MPTQSKHASI NIGLIQAREA LMTQFRPILN QANITDQQWR IIRLLAENGT LDFQDLANQA CILRPSLTGI LTRLEKAGLV VRLKPSNDQR RVYLKLTSEG EKLYEEIGEE VDERYDAIEE VLGREKMLLL KDLLAELAKI EDALNS // ID Q5F524_NEIG1 Unreviewed; 309 AA. AC Q5F524; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Polyphosphate kinase {ECO:0000313|EMBL:AAW90713.1}; GN ORFNames=NGO_2113 {ECO:0000313|EMBL:AAW90713.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90713.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90713.1; -; Genomic_DNA. DR RefSeq; WP_003705040.1; NC_002946.2. DR RefSeq; YP_209125.1; NC_002946.2. DR ProteinModelPortal; Q5F524; -. DR EnsemblBacteria; AAW90713; AAW90713; NGO_2113. DR GeneID; 3282805; -. DR KEGG; ngo:NGO2113; -. DR PATRIC; 20338067; VBINeiGon24812_2556. DR HOGENOM; HOG000176512; -. DR OMA; APWFTVE; -. DR OrthoDB; EOG6BPDJX; -. DR BioCyc; NGON242231:GI2G-2007-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016898; Polyphosphate_kinase-2. DR InterPro; IPR022488; PPK2-related. DR InterPro; IPR022486; PPK2_PA0141. DR Pfam; PF03976; PPK2; 1. DR PIRSF; PIRSF028756; PPK2_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03707; PPK2_P_aer; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Kinase {ECO:0000313|EMBL:AAW90713.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90713.1}. FT DOMAIN 57 280 PPK2. {ECO:0000259|Pfam:PF03976}. SQ SEQUENCE 309 AA; 36085 MW; 6380EDFBFA510104 CRC64; MADRQLQPFE NVELGEKQDQ FQVFEKAVLE HEGKGSAEDS GTVPLPENYP CRKRMLRAAY EAEKAKLQIE LLKVQSWVKD SGQRIVSLFE GRDAAGKGGT IKRFMEHLNP RGARVVALEK PTTTERGQWY FQRYIQNLPT AGEMVFFDRS WYNRAGVERV TGFCEPNEYM LFMCQAPELE RMLVASGIHL FKFWFSVSRE EQLRRFISRR DDALKHWKLS PVDIQSLDRW DDYTEAKNAM FFHTHTGDAP WVIIRSDDKK RARLNCIRYF LHQLDYPGKD VKAIGKVDDK IVLVPDTRYK EKTIDIGHD // ID Q5F8P1_NEIG1 Unreviewed; 182 AA. AC Q5F8P1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Baseplate protein {ECO:0000313|EMBL:AAW89446.1}; GN ORFNames=NGO_0727 {ECO:0000313|EMBL:AAW89446.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89446.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89446.1; -; Genomic_DNA. DR RefSeq; WP_010951114.1; NC_002946.2. DR RefSeq; YP_207858.1; NC_002946.2. DR EnsemblBacteria; AAW89446; AAW89446; NGO_0727. DR GeneID; 3282083; -. DR KEGG; ngo:NGO0727; -. DR PATRIC; 20334590; VBINeiGon24812_0867. DR OrthoDB; EOG61S2XH; -. DR BioCyc; NGON242231:GI2G-686-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 182 AA; 19871 MW; 188E43DFBB2F8614 CRC64; MGNSRLSQLP APAAIEETDF EGIFARKKAA LTALCPESIR ETVAQTLELE SEPLTIDLQQ QAYQELLVRN RINEAVKANL LAYAQGSDLD HIAAQYGLSR KTIRAADPDA NPPVAAEYET DDAFRARVQA HPEKYAAGPR TAYEAHAIDA PPKSHTPAPC AAPPARWRFT SKPKAARPTK PF // ID Q5F9N7_NEIG1 Unreviewed; 274 AA. AC Q5F9N7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89100.1}; GN ORFNames=NGO_0356 {ECO:0000313|EMBL:AAW89100.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89100.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89100.1; -; Genomic_DNA. DR RefSeq; WP_003690807.1; NC_002946.2. DR RefSeq; YP_207512.1; NC_002946.2. DR ProteinModelPortal; Q5F9N7; -. DR REBASE; 12957; NgoAVIII. DR DNASU; 3283035; -. DR EnsemblBacteria; AAW89100; AAW89100; NGO_0356. DR GeneID; 3283035; -. DR KEGG; ngo:NGO0356; -. DR PATRIC; 20333707; VBINeiGon24812_0431. DR OrthoDB; EOG63FVXR; -. DR BioCyc; NGON242231:GI2G-335-MONOMER; -. DR Proteomes; UP000000535; 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; -; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 4 151 N6_Mtase. {ECO:0000259|Pfam:PF02384}. SQ SEQUENCE 274 AA; 31178 MW; 211C115B92683FF9 CRC64; MFALAASNMI LRGDGKANLH QSSCFMTDFQ DLIKNPKPET GLKRPNVGFL NPPYAQSKSD AELHELYFVK EMLDMLAEGG TGIAIIPVSC VIAPSKAKSE IVKYHRLKAV MSMPSELFYP VGTVTCIVVF EAHKPHFQTV VIDPDTQEEI STKKACRKTW FGYWRDDGFE KTKHLGRIDL YDRWQGIKAR WLEHYLNNEV HTGESVTAFV TDNDEWVAEA YLETDYSKIT RADFEQVVRE FALFQLLGAE VGPTENLDNE SYEDDDNNDF GDDE // ID Q5F6R4_NEIG1 Unreviewed; 488 AA. AC Q5F6R4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=C4-dicarboxylate ABC transporter {ECO:0000313|EMBL:AAW90123.1}; GN ORFNames=NGO_1485 {ECO:0000313|EMBL:AAW90123.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90123.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90123.1; -; Genomic_DNA. DR RefSeq; WP_003689366.1; NC_002946.2. DR RefSeq; YP_208535.1; NC_002946.2. DR EnsemblBacteria; AAW90123; AAW90123; NGO_1485. DR GeneID; 3281622; -. DR KEGG; ngo:NGO1485; -. DR PATRIC; 20336421; VBINeiGon24812_1758. DR HOGENOM; HOG000117912; -. DR KO; K03319; -. DR OMA; TSAMFVT; -. DR OrthoDB; EOG6WT8FN; -. DR BioCyc; NGON242231:GI2G-1389-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 50 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; 51558 MW; 5EB8F1F2868DFDE3 CRC64; MMKLGFKPIP LAIAAVLCAL VLALPVPDGV KPQAWTLLAM FVGVIAAIIG KVMPLGALSI IAVGLVAVTG VTADKPGAAM SDALSAFANP LIWLIAIAVM ISRGLLKTGL GMRIGYLFIA VFGRKTLGIG YSLALSELLL APVTPSNTAR GGGIIHPIMQ SIAGSYGSNP AKGTEGKMGK YLALVNYHSN PISSAMFITA TAPNPLIVNL IAENLGSSFR LSWGAWAWAM AVPGVIAFFV MPLILYFLYP PEIKETPNAV QFAKDRLSEM GKMSADEIIM AVIFGILLLL WADVPALITG NHAFSINATA TAFIGLSLLL LSGVLTWDDV LKEKSAWDTI IWFGALIMMA AFLNKLGLIK WFSGVLAESV GGLGVSGTAA GVILVLAYMY AHYMFASTTA HITAMFGAFL AAAVSLNAPA MPTALMMAAA SNIMMTLTHY ATGTSPVIFG SGYTTMGEWW KAGFIMSVVN FLIFSVIGSI WWKVLGYW // ID Q5F9D9_NEIG1 Unreviewed; 395 AA. AC Q5F9D9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 70. DE SubName: Full=Succinyldiaminopimelate aminotransferase {ECO:0000313|EMBL:AAW89198.1}; GN ORFNames=NGO_0460 {ECO:0000313|EMBL:AAW89198.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89198.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89198.1; -; Genomic_DNA. DR RefSeq; WP_003706584.1; NC_002946.2. DR RefSeq; YP_207610.1; NC_002946.2. DR ProteinModelPortal; Q5F9D9; -. DR DNASU; 3282985; -. DR EnsemblBacteria; AAW89198; AAW89198; NGO_0460. DR GeneID; 3282985; -. DR KEGG; ngo:NGO0460; -. DR PATRIC; 20333954; VBINeiGon24812_0551. DR HOGENOM; HOG000223059; -. DR KO; K14267; -. DR OMA; DECYLEL; -. DR OrthoDB; EOG6CP3SM; -. DR BioCyc; NGON242231:GI2G-436-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89198.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89198.1}. FT DOMAIN 33 385 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 395 AA; 44136 MW; 059A329416713CDC CRC64; MNTLLKQLKP YPFARLREAM QGISAPEGME AVPLHIGEPK HPTPKVITDA LTASLRELEK YPLTAGLPEL RQACANWLKR RYDGLTVNPD NEILPVLGSR EALFSFVQTV LNPVSDGLKP VIVSPNPFYQ IYEGATLLGG GEIHFANCPA PSFNPDWRSI SEEVWERTKL VFVCSPNNPS GSVPDLDGWR EVFDLQDKYG FIIASDECYS EIYFDGNKPL GCLQAAAQSG RSRQKLLMFT SLSKRSNVPG LRSGFVAGDA ELLKNFLLYR TYHGSAMSIP VQRASIAAWN DEQHVIDNRR MYQEKFERVI PILQQVFDVK LPDASFYIWL KVPNGDDLAF ARNLWQKAAI QVLPGRFLAR DTEQGNPGEG YVRIALVADV ATCVKAAETI VSLYR // ID Q5F7L7_NEIG1 Unreviewed; 470 AA. AC Q5F7L7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 65. DE SubName: Full=Potassium transporter peripheral membrane component {ECO:0000313|EMBL:AAW89820.1}; GN Name=trkA {ECO:0000313|EMBL:AAW89820.1}; GN ORFNames=NGO_1154 {ECO:0000313|EMBL:AAW89820.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89820.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89820.1; -; Genomic_DNA. DR RefSeq; WP_003689753.1; NC_002946.2. DR RefSeq; YP_208232.1; NC_002946.2. DR ProteinModelPortal; Q5F7L7; -. DR EnsemblBacteria; AAW89820; AAW89820; NGO_1154. DR GeneID; 3282230; -. DR KEGG; ngo:NGO1154; -. DR PATRIC; 20335575; VBINeiGon24812_1352. DR HOGENOM; HOG000227130; -. DR KO; K03499; -. DR OMA; IACQVAY; -. DR OrthoDB; EOG6ZH2G8; -. DR BioCyc; NGON242231:GI2G-1066-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 51074 MW; 86E0E1E47CB09EE9 CRC64; MKILILGNGQ VGSTVAQNLA AITNNDVTVI 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 Q5F8E7_NEIG1 Unreviewed; 290 AA. AC Q5F8E7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Phytoene synthase {ECO:0000313|EMBL:AAW89540.1}; GN ORFNames=NGO_0830 {ECO:0000313|EMBL:AAW89540.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89540.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89540.1; -; Genomic_DNA. DR RefSeq; WP_003688576.1; NC_002946.2. DR RefSeq; YP_207952.1; NC_002946.2. DR ProteinModelPortal; Q5F8E7; -. DR DNASU; 3282287; -. DR EnsemblBacteria; AAW89540; AAW89540; NGO_0830. DR GeneID; 3282287; -. DR KEGG; ngo:NGO0830; -. DR PATRIC; 20334818; VBINeiGon24812_0979. DR HOGENOM; HOG000220849; -. DR KO; K02291; -. DR OMA; RKFWLAW; -. DR OrthoDB; EOG63FW00; -. DR BioCyc; NGON242231:GI2G-782-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 290 AA; 32851 MW; FD392BE814D7C220 CRC64; MKGLDYCRQK AEESRSSFLS GFRFLTQEKQ DAVTVLYAFC RELDDVVDEC SNPDVAQATL NWWRGDLDNA FGGAMPEHPV NQALRQVKET FKLPKYELEA LIDGMQMDLV QARYGSFEEL KLYCRRVAGV VGCLIARILG FSDGKTLEYA DKMGLALQLT NIIRDVGEDA RRGRIYLPME EMQRFDVPAS VILQCSPTGN FAELMAFQIK RARETYREAV SLLPDADKKA QKVGLVMAAV YYALLNEIDR DGAQNVLKYK IALPSPRKKR IALKTWLFGF KPRPGTPERA // ID Q5F8T5_NEIG1 Unreviewed; 243 AA. AC Q5F8T5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Restriction endonuclease NlaIV {ECO:0000313|EMBL:AAW89402.1}; GN ORFNames=NGO_0675 {ECO:0000313|EMBL:AAW89402.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89402.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89402.1; -; Genomic_DNA. DR RefSeq; WP_003697156.1; NC_002946.2. DR RefSeq; YP_207814.1; NC_002946.2. DR REBASE; 10856; NgoAXVP. DR EnsemblBacteria; AAW89402; AAW89402; NGO_0675. DR GeneID; 3282048; -. DR KEGG; ngo:NGO0675; -. DR PATRIC; 20334448; VBINeiGon24812_0796. DR HOGENOM; HOG000027816; -. DR OMA; KIRLGVW; -. DR OrthoDB; EOG6T7N5S; -. DR BioCyc; NGON242231:GI2G-642-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:InterPro. DR InterPro; IPR019064; Restrct_endonuc_II_NlaIV. DR Pfam; PF09564; RE_NgoBV; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89402.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89402.1}; KW Nuclease {ECO:0000313|EMBL:AAW89402.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 243 AA; 28814 MW; 3079E86E60664CC0 CRC64; MIKLTAQQIF DKLLDEEKIL SANGQIRFFL GDVDIIVKQK DVVGNIIQEW LGGWLRKREI EFDVSTNTQM PPDFFLNKKD RSRELLEVKA FNRNACPGFD IADFKMYSDE IIHKPYMLDV DYLIFGYDMD DNGNVTIKDL WLKKVWQITR SMDGWAINLQ VKKGVVHKIR PGVWYSINKK NMPMFECLED FVSAIEETVY QNPATRHNAS LWKKKFEEAY KKHYNRSISI PRWHEIAHKY KKK // ID Q5F7Z7_NEIG1 Unreviewed; 69 AA. AC Q5F7Z7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Phage/conjugal plasmid C-4 type zinc finger protein, TraR family {ECO:0000313|EMBL:AAW89690.1}; GN ORFNames=NGO_1007 {ECO:0000313|EMBL:AAW89690.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89690.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89690.1; -; Genomic_DNA. DR RefSeq; WP_003688249.1; NC_002946.2. DR RefSeq; YP_208102.1; NC_002946.2. DR ProteinModelPortal; Q5F7Z7; -. DR EnsemblBacteria; AAW89690; AAW89690; NGO_1007. DR GeneID; 3281988; -. DR KEGG; ngo:NGO1007; -. DR PATRIC; 20335222; VBINeiGon24812_1179. DR HOGENOM; HOG000141758; -. DR OMA; KMRRQNY; -. DR OrthoDB; EOG6F81VH; -. DR BioCyc; NGON242231:GI2G-933-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR012783; Znf_C4_TraR. DR InterPro; IPR000962; Znf_DskA_TraR. DR Pfam; PF01258; zf-dskA_traR; 1. DR TIGRFAMs; TIGR02419; C4_traR_proteo; 1. DR PROSITE; PS51128; ZF_DKSA_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 69 DksA C4-type. FT {ECO:0000259|PROSITE:PS51128}. SQ SEQUENCE 69 AA; 7723 MW; 3CB948E274D1E609 CRC64; MTDFADRASE REAEFLVEAL AKHQPPSENT AGFSHCEDCG DPIPEAKRKA VRGCTRCVVC HEYIQLKTK // ID Q5F9Q9_NEIG1 Unreviewed; 287 AA. AC Q5F9Q9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000313|EMBL:AAW89078.1}; GN ORFNames=NGO_0332 {ECO:0000313|EMBL:AAW89078.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89078.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89078.1; -; Genomic_DNA. DR RefSeq; WP_003692740.1; NC_002946.2. DR RefSeq; YP_207490.1; NC_002946.2. DR ProteinModelPortal; Q5F9Q9; -. DR EnsemblBacteria; AAW89078; AAW89078; NGO_0332. DR GeneID; 3281736; -. DR KEGG; ngo:NGO0332; -. DR PATRIC; 20333657; VBINeiGon24812_0406. DR HOGENOM; HOG000227711; -. DR KO; K00067; -. DR OMA; IRTAWVY; -. DR OrthoDB; EOG6HTP2V; -. DR BioCyc; NGON242231:GI2G-313-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 286 RmlD_sub_bind. FT {ECO:0000259|Pfam:PF04321}. SQ SEQUENCE 287 AA; 31260 MW; 6EEE227141F3C9C2 CRC64; MRILLTGSKS QLAHCLRDRL PEDWETIATD SASLDITDAD AVCNMVKSFQ PDAIVNTAAY TAVDKAEGDA AAAFAVNASA VYNLALAAHR AHARFIHIST DYVFDGKGKI PYQESDFTNP SNVYGQSKTA GELLALSANP DSLILRTSWL FSEYGDNFVR TMLNLARERS PLSAVHNQIG CPTYAGDLSA AIIRLLQQSN PVRGIYHYAG GKSVSWYEFA RHIFQTALQQ DASFPVPELK AVSDEGSAAA APRPAYSILD CRKIENDFGI KPSDWQKALA QVVSKLL // ID Q5FAL1_NEIG1 Unreviewed; 323 AA. AC Q5FAL1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 53. DE SubName: Full=Iron ABC transporter substrate-binding protein {ECO:0000313|EMBL:AAW88792.1}; GN ORFNames=NGO_0023 {ECO:0000313|EMBL:AAW88792.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88792.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88792.1; -; Genomic_DNA. DR RefSeq; WP_010356564.1; NC_002946.2. DR RefSeq; YP_207204.1; NC_002946.2. DR ProteinModelPortal; Q5FAL1; -. DR EnsemblBacteria; AAW88792; AAW88792; NGO_0023. DR GeneID; 3283066; -. DR KEGG; ngo:NGO0023; -. DR PATRIC; 20332876; VBINeiGon24812_0023. DR HOGENOM; HOG000099140; -. DR OMA; PRATSKY; -. DR OrthoDB; EOG61VZ9F; -. DR BioCyc; NGON242231:GI2G-20-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 323 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255581. FT DOMAIN 58 318 Fe/B12 periplasmic-binding. FT {ECO:0000259|PROSITE:PS50983}. SQ SEQUENCE 323 AA; 34299 MW; 0FF403015F22FB7C CRC64; MKPRFYWAAC AVLPAACSPE PAAEKTVSAA SQAASTPVAT LTVPTARGDA VVPKNPERVA VYDWAALDTL TEPGVNVGAT TAPVRVDYLQ PAFDKAATVG TLFEPDCESL HRHNPQFVIT GGPGAEAYEQ LAKNATTIDL TVDNGNIRTS GEKQMETLSR IFGKEARVAE LNAQIDALFA QKREAAKGKG RGLVLSVTGN KVSAFGTQSR LASWIHGDIG LPPVDESLRN EGHGQPVSFE YIKEKNPGWI FIIDRTAAIG QEGPAAVEVL DNALVCGTNA WKRKQIIVMP AANYIVAGGA RQLIQAAEQL KAAFEKAEPV AAQ // ID Q5F7T0_NEIG1 Unreviewed; 431 AA. AC Q5F7T0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89757.1}; GN ORFNames=NGO_1090 {ECO:0000313|EMBL:AAW89757.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89757.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89757.1; -; Genomic_DNA. DR RefSeq; WP_003695011.1; NC_002946.2. DR RefSeq; YP_208169.1; NC_002946.2. DR EnsemblBacteria; AAW89757; AAW89757; NGO_1090. DR GeneID; 3281713; -. DR KEGG; ngo:NGO1090; -. DR PATRIC; 20335432; VBINeiGon24812_1282. DR HOGENOM; HOG000225127; -. DR OMA; EKELDHG; -. DR OrthoDB; EOG60KN3R; -. DR BioCyc; NGON242231:GI2G-1002-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025267; DUF4043. DR Pfam; PF13252; DUF4043; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 431 AA; 46400 MW; 282318376ABF3AB1 CRC64; MAQKTNTAYG DPQAMMKQAA GLFAMHMQRN STLNRLAGKM PAGTAGAEAT LRKQTTQHMP VVRCQDLTRG MGDEIRFNLV NPVSALPIMG DNTAEGRGVG MSLSEAGLRV NQARFPVDGG GTMTNQRSPA DYRALIRPAA QSLMDRYADQ TLLVHMAGAR GFHDNIEWGV PLAGDPKFND YAVNPVKAPS KNRHFTASGD AVTGVGDNGG ELKIASTDLF TMDTVDSMRT VLDQIPLPPP IVKFEGDKAA GDSPLRVWLL SPAQYNRFAA DPKFRQLQAS AIARASQANQ NPLFLGDAGL WNGFILVKMP RPIRFYAGDE MKYCADKFSE AESGLKIPAS FADKFAVDRS VILGGQAVLE AFANTGKHGG MPFFWSEKEL DHGNRVETLV GTIRGVAKTR FAVDVGGGAK EITDYGVTVV DTVVPLHGGI R // ID Q5FAH5_NEIG1 Unreviewed; 153 AA. AC Q5FAH5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:AAW88812.1}; DE EC=6.4.1.2 {ECO:0000313|EMBL:AAW88812.1}; GN ORFNames=NGO_0045 {ECO:0000313|EMBL:AAW88812.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88812.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88812.1; -; Genomic_DNA. DR RefSeq; WP_003687267.1; NC_002946.2. DR RefSeq; YP_207224.1; NC_002946.2. DR ProteinModelPortal; Q5FAH5; -. DR SMR; Q5FAH5; 81-152. DR EnsemblBacteria; AAW88812; AAW88812; NGO_0045. DR GeneID; 3282340; -. DR KEGG; ngo:NGO0045; -. DR PATRIC; 20332930; VBINeiGon24812_0050. DR HOGENOM; HOG000008875; -. DR KO; K02160; -. DR OMA; KMFNQIE; -. DR OrthoDB; EOG6CVV6Z; -. DR BioCyc; NGON242231:GI2G-40-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC. 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:UP000000535}; KW Ligase {ECO:0000313|EMBL:AAW88812.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 71 153 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 153 AA; 15795 MW; 05E2A7BD06E875EB CRC64; MDLRKLKKLI DLVEESGIAE IEVTEGEEKV RITRTIAAAA APVYAAPVPA AAPAVTPAAA PVAASAPAAA PAARDLSDAQ KSPMVGTFYR APGPNAAAFV EVGQQVKAGD TLCIIEAMKL MNEIEAEKSG TVKEILVENG TPVEFGEPLF IIG // ID Q5F9P6_NEIG1 Unreviewed; 325 AA. AC Q5F9P6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 63. DE SubName: Full=DNA polymerase III subunit delta {ECO:0000313|EMBL:AAW89091.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAW89091.1}; GN ORFNames=NGO_0347 {ECO:0000313|EMBL:AAW89091.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89091.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89091.1; -; Genomic_DNA. DR RefSeq; WP_003696824.1; NC_002946.2. DR RefSeq; YP_207503.1; NC_002946.2. DR ProteinModelPortal; Q5F9P6; -. DR EnsemblBacteria; AAW89091; AAW89091; NGO_0347. DR GeneID; 3281191; -. DR KEGG; ngo:NGO0347; -. DR PATRIC; 20333691; VBINeiGon24812_0423. DR HOGENOM; HOG000192592; -. DR KO; K02341; -. DR OMA; FAQGNHP; -. DR OrthoDB; EOG6W9X5M; -. DR BioCyc; NGON242231:GI2G-326-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; 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; 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:UP000000535}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW89091.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89091.1}. SQ SEQUENCE 325 AA; 37012 MW; 9BC28672754678DB CRC64; MIYPWHQEQW RQIAEHWTSR PNAWLFVGKK GTGKTAFARF AAKALLCETP APGCKPCGEC MSCHLFGRGS HPDFYEITPL ADEPENGRKL LRIKIDAVRE IIDNVYLTSV RGGLRVILIH PAESMNVQAA NSLLKVLEEP PPQVVFLLVS HAADKVLPTI KSRCRKMVLP APSHGEALAY LRDRGVAEPE ERLAFHSGAP LFQEEGELRE LRAKLLEILA EPRLLKILDY AALFDKEKLP LAVFVGWMQK WLVDLGLCLQ HMKPVYYPAY EDRLLQTASG FRPRNVFAAE DMLKQLAPYG FHTLNVKMQI EHLLINYLEL KKENR // ID Q5F8E2_NEIG1 Unreviewed; 47 AA. AC Q5F8E2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89545.1}; GN ORFNames=NGO_0836 {ECO:0000313|EMBL:AAW89545.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89545.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89545.1; -; Genomic_DNA. DR RefSeq; WP_003688567.1; NC_002946.2. DR RefSeq; YP_207957.1; NC_002946.2. DR EnsemblBacteria; AAW89545; AAW89545; NGO_0836. DR GeneID; 3282331; -. DR KEGG; ngo:NGO0836; -. DR PATRIC; 20334832; VBINeiGon24812_0986. DR HOGENOM; HOG000071284; -. DR OrthoDB; EOG68SW4N; -. DR BioCyc; NGON242231:GI2G-787-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 47 AA; 5398 MW; 31EE4D7978607E5B CRC64; MRILILASRT AQNQATGFNI RTRFGFCILQ NPNLLFKFKL NSGVVVW // ID Q5F8T9_NEIG1 Unreviewed; 261 AA. AC Q5F8T9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 57. DE SubName: Full=Inositol monophosphatase {ECO:0000313|EMBL:AAW89398.1}; GN ORFNames=NGO_0671 {ECO:0000313|EMBL:AAW89398.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89398.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89398.1; -; Genomic_DNA. DR RefSeq; WP_003688815.1; NC_002946.2. DR RefSeq; YP_207810.1; NC_002946.2. DR ProteinModelPortal; Q5F8T9; -. DR EnsemblBacteria; AAW89398; AAW89398; NGO_0671. DR GeneID; 3282051; -. DR KEGG; ngo:NGO0671; -. DR PATRIC; 20334440; VBINeiGon24812_0792. DR HOGENOM; HOG000282238; -. DR KO; K01092; -. DR OMA; YILATNG; -. DR OrthoDB; EOG6QK4W4; -. DR BioCyc; NGON242231:GI2G-638-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 261 AA; 28573 MW; 2D3ADC2D20A55A36 CRC64; MNPFLNTAFK AARRAGQMMI RAAGNLDAVK TDSKAFNDFV SDVDRNSEII LVEALKEAYP HHKITCEESG FHGKATAEYE WIIDPLDGTT NFLHGHPQYA ISMALLHKGV LQEALVYAPE RNDVYMASRG KGALLNDRRI RVSNRIELNR CLIGTGFPVV DQSMMDKYLA ILKDFLAKTA GGRREGAASL DLCAVATGRF DGFFEFNLKP WDIAAGALIV QEAGGIVTDM SGEDAWLESG DIVAANPKVL AQMLKIISAH V // ID Q5F982_NEIG1 Unreviewed; 78 AA. AC Q5F982; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Multidrug transporter MatE {ECO:0000313|EMBL:AAW89255.1}; GN ORFNames=NGO_0517 {ECO:0000313|EMBL:AAW89255.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89255.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89255.1; -; Genomic_DNA. DR RefSeq; WP_003689049.1; NC_002946.2. DR RefSeq; YP_207667.1; NC_002946.2. DR ProteinModelPortal; Q5F982; -. DR EnsemblBacteria; AAW89255; AAW89255; NGO_0517. DR GeneID; 3282931; -. DR KEGG; ngo:NGO0517; -. DR PATRIC; 20334076; VBINeiGon24812_0610. DR HOGENOM; HOG000289070; -. DR KO; K18842; -. DR OMA; CDTKAFF; -. DR OrthoDB; EOG6Z3KS9; -. DR BioCyc; NGON242231:GI2G-495-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 47 SpoVT-AbrB. FT {ECO:0000259|PROSITE:PS51740}. SQ SEQUENCE 78 AA; 8666 MW; 205092CD8F4CA359 CRC64; MLRLQKWGNS AAVRLPARLL TALNAKIGDA LETEIRNGEL LIRPVKRYRL SDLLAETEAA PPRAEGWEEM PDVGQEGV // ID Q5F9M5_NEIG1 Unreviewed; 126 AA. AC Q5F9M5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89112.1}; GN ORFNames=NGO_0368 {ECO:0000313|EMBL:AAW89112.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89112.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89112.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F9M5; -. DR EnsemblBacteria; AAW89112; AAW89112; NGO_0368. DR PATRIC; 20333735; VBINeiGon24812_0445. DR HOGENOM; HOG000101109; -. DR OMA; MQERREI; -. DR OrthoDB; EOG6VB726; -. DR BioCyc; NGON242231:GI2G-347-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 34 94 DUF302. {ECO:0000259|Pfam:PF03625}. SQ SEQUENCE 126 AA; 13767 MW; 8F3AF01625148637 CRC64; MTTHTLTSKY SFDETVSRLE TAIKSKGMDI FAVIDHQEAA RRNGLTMQPA KVIVFGTPKA GTPLMVKDPA FALQLPLRVL VTETDGKVRT AYTDTRALIV GSRISFDEVA NTLANAEKLI QKTVGE // ID Q5FA78_NEIG1 Unreviewed; 334 AA. AC Q5FA78; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 72. 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 ORFNames=NGO_0151 {ECO:0000313|EMBL:AAW88909.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88909.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW88909.1; -; Genomic_DNA. DR RefSeq; WP_010356737.1; NC_002946.2. DR RefSeq; YP_207321.1; NC_002946.2. DR ProteinModelPortal; Q5FA78; -. DR EnsemblBacteria; AAW88909; AAW88909; NGO_0151. DR GeneID; 3281316; -. DR KEGG; ngo:NGO0151; -. DR PATRIC; 20333223; VBINeiGon24812_0194. DR HOGENOM; HOG000217855; -. DR KO; K05540; -. DR OMA; WLFREIE; -. DR OrthoDB; EOG6VHZFQ; -. DR BioCyc; NGON242231:GI2G-139-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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 334 AA; 36136 MW; B379343D0541035F CRC64; MHIGGYFIDN PIALAPMAGI ADKPFRRLCR AFGAGWAVCE MLASDPTLRN TGKTLHRSDF ADEGGIVAVQ IAGSDPEQMA DAARYNVGLG AQVIDINMGC PAKKVCNVQA GSALMQDEPL VAAILEAVVK AAGVPVTLKT RLGWHDDHQN LPAIAKIAED CGIAALAVHG RARTQMYKGE ARYELIAETK SRLNIPAWVN GDITSPQKAA AVLKQTAADG IMIGRGAQGR PWFFRDLKHY AEHGVLPPAL SLAECRAAIL NHIRAMHAFY GETVGVRIAR KHIGWYIGEM PDGEQARREI NRLDNAAAQY DTLAGYLERL AGKTDRWACG YREG // ID Q5FA05_NEIG1 Unreviewed; 129 AA. AC Q5FA05; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88982.1}; GN ORFNames=NGO_0229 {ECO:0000313|EMBL:AAW88982.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88982.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88982.1; -; Genomic_DNA. DR RefSeq; WP_003692667.1; NC_002946.2. DR RefSeq; YP_207394.1; NC_002946.2. DR EnsemblBacteria; AAW88982; AAW88982; NGO_0229. DR GeneID; 3281469; -. DR KEGG; ngo:NGO0229; -. DR PATRIC; 20333403; VBINeiGon24812_0283. DR HOGENOM; HOG000218830; -. DR OMA; IDNIYNI; -. DR OrthoDB; EOG62ZHWC; -. DR BioCyc; NGON242231:GI2G-213-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 129 AA; 14877 MW; 30DAC86F098DCC82 CRC64; MWKIIKEDSD DLGFAIKCLF SQSIDLNEFK LWIEQVIRDM PIEDIPFYIF DLADFNGGIG DIDNIVGFVS SYSLSKSKKN ALTGIAFLRG IDVYDPPISK EKALKALKKH PEIYHKFKRF FPFVELPLL // ID Q5F5R8_NEIG1 Unreviewed; 80 AA. AC Q5F5R8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90469.1}; GN ORFNames=NGO_1848 {ECO:0000313|EMBL:AAW90469.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90469.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90469.1; -; Genomic_DNA. DR RefSeq; WP_010951359.1; NC_002946.2. DR RefSeq; YP_208881.1; NC_002946.2. DR PRIDE; Q5F5R8; -. DR EnsemblBacteria; AAW90469; AAW90469; NGO_1848. DR GeneID; 3282422; -. DR KEGG; ngo:NGO1848; -. DR PATRIC; 20337372; VBINeiGon24812_2221. DR HOGENOM; HOG000218663; -. DR OMA; SKNIFFM; -. DR OrthoDB; EOG6QP14J; -. DR BioCyc; NGON242231:GI2G-1749-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 80 AA; 8319 MW; A1DFD00D172D5551 CRC64; MKSKNIFFMG YLIASATFAE DIGVPVEPIN VGSRAAMPSE GESLALLPFA EDVPPVRDAM PSEVPKSAAG GDVRGGRSIP // ID Q5F957_NEIG1 Unreviewed; 979 AA. AC Q5F957; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 64. DE SubName: Full=Restriction endonuclease EcoPI subunit R {ECO:0000313|EMBL:AAW89280.1}; GN ORFNames=NGO_0546 {ECO:0000313|EMBL:AAW89280.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89280.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89280.1; -; Genomic_DNA. DR RefSeq; WP_003689015.1; NC_002946.2. DR RefSeq; YP_207692.1; NC_002946.2. DR ProteinModelPortal; Q5F957; -. DR REBASE; 5865; NgoAX. DR EnsemblBacteria; AAW89280; AAW89280; NGO_0546. DR GeneID; 3282114; -. DR KEGG; ngo:NGO0546; -. DR PATRIC; 20334144; VBINeiGon24812_0644. DR HOGENOM; HOG000218980; -. DR KO; K01156; -. DR OMA; CIIRFGA; -. DR OrthoDB; EOG6MPWQ7; -. DR BioCyc; NGON242231:GI2G-520-MONOMER; -. DR BRENDA; 3.1.21.5; 3590. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89280.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89280.1}; KW Nuclease {ECO:0000313|EMBL:AAW89280.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 11 254 ResIII. {ECO:0000259|Pfam:PF04851}. SQ SEQUENCE 979 AA; 111427 MW; C0E1E3DFD10ECC1A 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 FSDGIIDDNE NFAEDGYDKL KAAYPEAFPK GLDKGKVSNA KDEGKDTIIM REGKYEELKA LWELIHHKAV LQYKIKDEAE FVDLFTAYLR ENAAKFPQAG ICTAVNEAYI NNGLMLSRRI DSIEDEDFIR FNTMTYREFL EKLAQTAKIQ MQTLHQAFYR VRDELNIGDF LNMQTIAQIK NGFNRFLLHH SFHKFELDYR LVGSKIHPTK FTNKDGKPRA VKKADLGRFE DTEHRPAAGY LFGEIFYDSD IEHENVANNQ IEGVIVFTKI PRNSIKIPVA GGGTYSPDFA YIVKTKSGEI LNFVIEAKGT DGAEDLRKSE ERKIKHAEKL FAEISKEIKV VFKTQFDGER IAELIGQNMP AGGHSENGH // ID Q5F619_NEIG1 Unreviewed; 157 AA. AC Q5F619; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 74. DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:AAW90368.1}; GN ORFNames=NGO_1747 {ECO:0000313|EMBL:AAW90368.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90368.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90368.1; -; Genomic_DNA. DR RefSeq; WP_003689950.1; NC_002946.2. DR RefSeq; YP_208780.1; NC_002946.2. DR ProteinModelPortal; Q5F619; -. DR EnsemblBacteria; AAW90368; AAW90368; NGO_1747. DR GeneID; 3281407; -. DR KEGG; ngo:NGO1747; -. DR PATRIC; 20337096; VBINeiGon24812_2088. DR HOGENOM; HOG000257748; -. DR KO; K00334; -. DR OMA; CYLTGYE; -. DR OrthoDB; EOG689HX9; -. DR BioCyc; NGON242231:GI2G-1643-MONOMER; -. DR Proteomes; UP000000535; 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:0016491; F:oxidoreductase activity; IEA:InterPro. 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:UP000000535}; KW Iron {ECO:0000256|PIRSR:PIRSR000216-1}; KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR000216-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000216-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 17146 MW; 78BD15C4FF965338 CRC64; MLSAKSLKQI DIELAKYPAD QRRSAIMGAL RIAQTEKGWL APETIAFVAD YIGITPAQAY EVATFYNMYD LEPVGKYKLT VCTNLPCALR GGMATGEYLK QKLGIGYGET TPDGKFTLVE GECMGACGDA PVMLVNNHSM CSFMTEEAIE KKLAELE // ID Q5F8P9_NEIG1 Unreviewed; 282 AA. AC Q5F8P9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAW89438.1}; GN ORFNames=NGO_0718 {ECO:0000313|EMBL:AAW89438.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89438.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89438.1; -; Genomic_DNA. DR RefSeq; WP_003688727.1; NC_002946.2. DR RefSeq; YP_207850.1; NC_002946.2. DR ProteinModelPortal; Q5F8P9; -. DR EnsemblBacteria; AAW89438; AAW89438; NGO_0718. DR GeneID; 3282115; -. DR KEGG; ngo:NGO0718; -. DR PATRIC; 20334564; VBINeiGon24812_0854. DR HOGENOM; HOG000027158; -. DR KO; K19337; -. DR OMA; GRTRDLM; -. DR OrthoDB; EOG6HMXHM; -. DR BioCyc; NGON242231:GI2G-678-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; A9D11180A04B55F5 CRC64; MLSKISESLA DLSGAERKVA ECALAEPKWF VHAAVAEIAD RASVSQPTVI RFCRSLGYKG LPEFKLSLSA SIGHEGMPYV HEELNADDDM ANVVEKVLGN AAAALLGERR FLKESELENG IATLMHARRV EFYGVGNSGI VAQDAQHKFF RFGMSTVAYV DTHTQLMAAS VLSDQDVLVA ISNTGSSIEL LDAVSIAKEN GASVIALTRN DSPLAQLADC VLSVATQENA ELYTPMVSRL LQLAVIDILA IGLALRLGDA ASLQLQKSKK SIHNKHIDYD KD // ID Q5FAE8_NEIG1 Unreviewed; 1144 AA. AC Q5FAE8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00057170}; DE EC=2.7.7.7 {ECO:0000256|SAAS:SAAS00057170}; GN ORFNames=NGO_0078 {ECO:0000313|EMBL:AAW88839.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88839.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|SAAS:SAAS00057091}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00290998}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW88839.1; -; Genomic_DNA. DR RefSeq; WP_010356628.1; NC_002946.2. DR RefSeq; YP_207251.1; NC_002946.2. DR ProteinModelPortal; Q5FAE8; -. DR EnsemblBacteria; AAW88839; AAW88839; NGO_0078. DR GeneID; 3282282; -. DR KEGG; ngo:NGO0078; -. DR PATRIC; 20333037; VBINeiGon24812_0102. DR HOGENOM; HOG000021784; -. DR KO; K02337; -. DR OMA; DFCMDGR; -. DR OrthoDB; EOG6CZQGR; -. DR BioCyc; NGON242231:GI2G-68-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00444691}; KW DNA replication {ECO:0000256|SAAS:SAAS00444682}; KW DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00444810}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00444810}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|SAAS:SAAS00444810}. FT DOMAIN 7 74 POLIIIAc. {ECO:0000259|SMART:SM00481}. SQ SEQUENCE 1144 AA; 127000 MW; F6D0A6FBED6A8B05 CRC64; MTEPTYIPLR LHTEFSITDG MVRIKKLIAK AQEYGLPALG ISDLMNEFGL VKFYKACRGA GIKPVGAADV WIGNPNAPDK PFRAMLVIRN DAGYLRLSEL LTEAYVGQDR NIHHAELNPE WLENGDNSGL ICLSGAHYGE VGVNLLNGNE DAARAAALKY AAWFPDTFYL ELQRLPERPE WEACVSGSVK LAEELGLPVV ATHPTQFMNR DDFNAHEARV CIAGGWVLTD KKRPRDFTPS QFFIPPETML ERFADLPEAL ENTVEIAKRC NLHITLGKNF LPLFPTPDGL SLDDCLIKLS NEGLQERMVQ LYPDEAERAA KMPEYQERLD FELNIIIQMK FPGYFLIVQD FINWAKTHGC PVGPGRGSGA GSLVAYSLKI TDLDPLKYAL LFERFLNPER VSMPDFDVDF CQANRGRVIE YVREKYGAQA VSQIVTFGTM SSKAVIRDVG RVLELPFMLC DKLSKLIPLE ANKPLSLDDA MKAQPQIQEL LEAEEADELI TLAKKLEDLT RGLGMHAGGV LIAPGKISDY SPVYQADESA SPVSMYDKGD VEDVGLVKFD FLGLRNLTII EMAQNNIKNT AGDIVDVGKI PLDDQTAYQI FRDANTTAVF QFESTGMKKM LKTAHTTKFE ELIAFVSLYR PGPMDNIPDF VARMKGQEFQ YIHPLLEGIL APTYGIMVYQ EQVMQAAQII GGYSLGGADL LRRAMGKKKP EEMVKHREIF AEGAAKQGIS REKSDEIFNY MEKFAGYGFN KSHAAAYALI SYQTAWLKAH YPAEFMAATM SSELDNTDQL KHFYDDCRAN GIEFLPPDIN ESDYRFTPYP DMKIRYALGA IKGTGEAAVE SIIAARQSGG KFTGLLDFCE RVGKEHMNRR TLEALIRGGA FDSIEPNRAM LLANIDLAMD NADQKAANAN QGGLFDMMED AIEPVRLIDA PMWSESEKLA EEKTVIGFYL SGHPFGPYAQ EVRQIAPTKL GRLKPQDSVR LAGFVTAVRT MMGKRGKIAF VSLEDSSGQA EIMVGGQTLE NCADCLKADQ VLIIESKVSR DDYGGGDGLR IMANQVMTLQ TARERYARSL SLALAPHHDI GGLVRLLAAH QLPDTPRIPL QLSYANEKAS GRLQVPPKWT VTPSSALFGE LETLLGSRSV RVNW // ID Q5F9K5_NEIG1 Unreviewed; 221 AA. AC Q5F9K5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=NAD(P)H nitroreductase {ECO:0000313|EMBL:AAW89132.1}; GN ORFNames=NGO_0388 {ECO:0000313|EMBL:AAW89132.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89132.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89132.1; -; Genomic_DNA. DR RefSeq; WP_003687816.1; NC_002946.2. DR RefSeq; YP_207544.1; NC_002946.2. DR ProteinModelPortal; Q5F9K5; -. DR EnsemblBacteria; AAW89132; AAW89132; NGO_0388. DR GeneID; 3283020; -. DR KEGG; ngo:NGO0388; -. DR PATRIC; 20333783; VBINeiGon24812_0469. DR HOGENOM; HOG000146738; -. DR OMA; CLAEEGL; -. DR OrthoDB; EOG65QWJJ; -. DR BioCyc; NGON242231:GI2G-367-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 14 180 Nitroreductase. FT {ECO:0000259|Pfam:PF00881}. SQ SEQUENCE 221 AA; 24823 MW; 990D89ADFE0001F1 CRC64; MTVLSKEQVL SAFKNRKSCR HYDAARKISA EDFQFILELG RLSPSSVGSE PWQFVVVQNP EIRQAIKLFS WGMADALDTA SHLVVFLAKK NARFDSPFML ESLKRRGVTE PDAVEKSLAR YQAFQADDIK ILDDSRALFD WCCRQTYIAL ANMMTGAAMA GIDSCPVEGF NYADMERVLS GQFGLFDAAE WGVSVAATFG YRVQEIVTKA RRPLEETVIW A // ID Q5FAA4_NEIG1 Unreviewed; 424 AA. AC Q5FAA4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 56. DE SubName: Full=Hemolysin D {ECO:0000313|EMBL:AAW88883.1}; GN ORFNames=NGO_0123 {ECO:0000313|EMBL:AAW88883.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88883.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88883.1; -; Genomic_DNA. DR RefSeq; WP_003696697.1; NC_002946.2. DR RefSeq; YP_207295.1; NC_002946.2. DR ProteinModelPortal; Q5FAA4; -. DR EnsemblBacteria; AAW88883; AAW88883; NGO_0123. DR GeneID; 3282391; -. DR KEGG; ngo:NGO0123; -. DR PATRIC; 20333149; VBINeiGon24812_0158. DR HOGENOM; HOG000146441; -. DR KO; K13408; -. DR OMA; LIRYQAY; -. DR OrthoDB; EOG6KMB4H; -. DR BioCyc; NGON242231:GI2G-112-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009306; P:protein secretion; IEA:InterPro. DR InterPro; IPR003997; Rtx_secretion_protD_GmN_bac. DR PRINTS; PR01490; RTXTOXIND. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33 53 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 137 171 {ECO:0000256|SAM:Coils}. FT COILED 196 223 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 424 AA; 47725 MW; 3EDBD8BFF02C1C3E CRC64; MNRPKQPFFR PEVAIARQTS LTGKVILTRP LSFSLWTTFA SISALLIILF LIFGNYTRKT TMEGQILPAS GVIRVYAPDT GTITAKFVED GEKVKAGDKL FALSTSRFGA GGSVQQQLKT EAVLKKTLAE QELGRLKLIH ENETRSLKAT VERLENQKLH ISQQIDGQKR RIRLAEEMLR KYRFLSANDA VSKQEMMNVE AELLEQKAKL DAYRREEAGL LQEIRTQNLT LASLPKRHET EQSQLERTIA DISQEVLDFE MRSEQIIRAG RSGYIAIPNV EVGRQVDPSK LLLSIVPERT ELYAHLYIPS SAAGFIKPKD KVVLRYQAYP YQKFGLASGS VVSVAKTALG RQELSGLGMV SSDLAKSNEP VYLVKIKPDK PTITAYGEEK PLQIGMTLEA DILHEKRRLY EWVLEPIYSM SGRL // ID Q5F5W4_NEIG1 Unreviewed; 228 AA. AC Q5F5W4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 48. DE SubName: Full=Abi-like family protein {ECO:0000313|EMBL:AAW90423.1}; GN ORFNames=NGO_1805 {ECO:0000313|EMBL:AAW90423.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90423.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90423.1; -; Genomic_DNA. DR RefSeq; WP_010951353.1; NC_002946.2. DR RefSeq; YP_208835.1; NC_002946.2. DR EnsemblBacteria; AAW90423; AAW90423; NGO_1805. DR GeneID; 3282294; -. DR KEGG; ngo:NGO1805; -. DR PATRIC; 20337260; VBINeiGon24812_2165. DR HOGENOM; HOG000218659; -. DR OMA; WIFRELS; -. DR OrthoDB; EOG69PQ2H; -. DR BioCyc; NGON242231:GI2G-1703-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011664; Abi_system_AbiD/AbiF-like. DR Pfam; PF07751; Abi_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 228 AA; 26298 MW; 85E180D5F4F85977 CRC64; MERYKNAVRK DKAAELYLLN LSLSRELFHV VSIFEIVLRN KIDICFRQEF KDRNRLYDSI QPQTNPALKY QGCFLRNGTK ESAELIKVAL SKIQNNSGGK FDHNQLVAGL GFGFWRYLFA GGKDAQFDAA GKVLMKVFPK KPKSTPSVQY NQKWIFRELS NINNFRNRLA HHEPICFSFK GAIKDTGYAR NIHQSIFELL NYMDVDTASV FSHFSDQVIA VCDEIDKL // ID Q5F9M7_NEIG1 Unreviewed; 85 AA. AC Q5F9M7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89110.1}; GN ORFNames=NGO_0366 {ECO:0000313|EMBL:AAW89110.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89110.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89110.1; -; Genomic_DNA. DR RefSeq; WP_010951033.1; NC_002946.2. DR RefSeq; YP_207522.1; NC_002946.2. DR EnsemblBacteria; AAW89110; AAW89110; NGO_0366. DR GeneID; 3283026; -. DR KEGG; ngo:NGO0366; -. DR OrthoDB; EOG6MH5P4; -. DR BioCyc; NGON242231:GI2G-345-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 85 AA; 9792 MW; F7AD9D1C38054499 CRC64; MIKILVWILK VNYALNATQR NATQRNATQR NATQRNATQR NATQRNATQR NSTIIFNGKV IVWDSCFVFS VIMPQNNRKP PLFVS // ID Q5F7Q4_NEIG1 Unreviewed; 236 AA. AC Q5F7Q4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 66. DE SubName: Full=Repressor {ECO:0000313|EMBL:AAW89783.2}; GN ORFNames=NGO_1116 {ECO:0000313|EMBL:AAW89783.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89783.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89783.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F7Q4; -. DR DNASU; 3281858; -. DR EnsemblBacteria; AAW89783; AAW89783; NGO_1116. DR PATRIC; 20335486; VBINeiGon24812_1309. DR HOGENOM; HOG000127685; -. DR OMA; WLTTGNT; -. DR OrthoDB; EOG61KBMJ; -. DR BioCyc; NGON242231:GI2G-1028-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; 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; PF01381; HTH_3; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51306; SSF51306; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 61 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. FT COILED 1 28 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 236 AA; 26314 MW; 901C83AFF6E45C72 CRC64; MSEFKDRLKE ARKNKNLSQE NLAKLAEVSQ STIAALESGR NKKATNIAKL AKILDVSAFW LETGEGSRTA PALINPDLPH EVKDIHRPMM WSSNDPLPDD DYVFVPYLKE SCFKGGAGAY EIPDYNGYRL PFGKSTLRRK GINPDNVFCC TLTGDSMEEK IAEDAAIAVD TGETAIRDGK IYAFAQDGMF RVKYLIRQPG NSVLIRSHNS GFYPDETAPL DSLTVIGRVF WWSVLD // ID Q5F804_NEIG1 Unreviewed; 83 AA. AC Q5F804; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89683.2}; GN ORFNames=NGO_1000 {ECO:0000313|EMBL:AAW89683.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89683.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89683.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89683; AAW89683; NGO_1000. DR PATRIC; 20335202; VBINeiGon24812_1169. DR HOGENOM; HOG000071271; -. DR OMA; EVCQPEL; -. DR OrthoDB; EOG6KDM0R; -. DR BioCyc; NGON242231:GI2G-926-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR022765; Dna2/Cas4_DUF83. DR Pfam; PF01930; Cas_Cas4; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 25 63 Cas_Cas4. {ECO:0000259|Pfam:PF01930}. SQ SEQUENCE 83 AA; 9311 MW; 613B858AB6A00A71 CRC64; MKIFWRIFMR QISLTDYFCK GLGLRAQTLA TIAAVRELLN SGQTPPPDYG KRCKACSLVE ICQPELLAKR DGSVGYVEAL FIV // ID Q5FA86_NEIG1 Unreviewed; 459 AA. AC Q5FA86; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 54. DE SubName: Full=Sodium:proton antiporter {ECO:0000313|EMBL:AAW88901.1}; GN ORFNames=NGO_0143 {ECO:0000313|EMBL:AAW88901.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88901.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88901.1; -; Genomic_DNA. DR RefSeq; WP_003694793.1; NC_002946.2. DR RefSeq; YP_207313.1; NC_002946.2. DR EnsemblBacteria; AAW88901; AAW88901; NGO_0143. DR GeneID; 3281299; -. DR KEGG; ngo:NGO0143; -. DR PATRIC; 20333199; VBINeiGon24812_0182. DR HOGENOM; HOG000283662; -. DR KO; K03315; -. DR OMA; TCGAYMA; -. DR OrthoDB; EOG61GG5F; -. DR BioCyc; NGON242231:GI2G-131-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 49173 MW; 2A547398AF8E4EC2 CRC64; MFAFKSLLDM PRGEALAVVV ALIAAMGYTI ISLEWLPHMS IIAAIVVLIL YGLARGLKYN DMQAGMIGAL NQGMGAVYLF FFIGLMVSAL MMSGAIPTLM YYGFGLISPT YFYFSAFALC SVIGVSIGSS LTACATVGVA FMGMAAAFQA DMAMTAGAIV SGVFFGDKMS PLSDTTGISA SIVGIDLFEH IKNMMYTTIP AWLISAALML WLLPSVAAQD LNSVESFRSQ LEATGLVHGY SLIPFALLVV LALMRVNAVV AMLFTVIAAV AVTYLHSTPD LRQLGAWFYG GYKLEGEAFK DIAKLISRGG LESMFFTQTI VILGMSLGGL LFALGVIPSL LEAVRTFLTN AGRATFSVAM TSVGVNFLIG EQYLSILLSG ETFKPVYDKL GLHSCNLSRT LEDAGTVINP LVPWSVCGVF ISHALGVPVW EYLPYAFFCY LSLALTLLFG WTGLTLSKK // ID Q5F8Q8_NEIG1 Unreviewed; 122 AA. AC Q5F8Q8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89429.1}; GN ORFNames=NGO_0709 {ECO:0000313|EMBL:AAW89429.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89429.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89429.1; -; Genomic_DNA. DR RefSeq; WP_010951111.1; NC_002946.2. DR RefSeq; YP_207841.1; NC_002946.2. DR EnsemblBacteria; AAW89429; AAW89429; NGO_0709. DR GeneID; 3281989; -. DR KEGG; ngo:NGO0709; -. DR BioCyc; NGON242231:GI2G-669-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 122 AA; 13995 MW; 7D3625EB6BC7919E CRC64; MYDKIHKSCR FFAGSFCFMF GAVPDNRVKF PLAHYFKIEI LYFISLLLKR CSHFFIGFII HHLIYGFWRQ GLTAFAAVID FWNRGNAFKE SKAIRPDADG GAIIHLLEFV AIGADSCDDY VG // ID Q5F9C1_NEIG1 Unreviewed; 145 AA. AC Q5F9C1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89216.1}; GN ORFNames=NGO_0478 {ECO:0000313|EMBL:AAW89216.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89216.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89216.1; -; Genomic_DNA. DR RefSeq; WP_003687967.1; NC_002946.2. DR RefSeq; YP_207628.1; NC_002946.2. DR EnsemblBacteria; AAW89216; AAW89216; NGO_0478. DR GeneID; 3282970; -. DR KEGG; ngo:NGO0478; -. DR PATRIC; 20333992; VBINeiGon24812_0568. DR OMA; DANHPIS; -. DR OrthoDB; EOG69KV3Q; -. DR BioCyc; NGON242231:GI2G-456-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 145 AA; 17008 MW; 3485D63DC2ED35B0 CRC64; MELTVHFNAE QDLDRLFEKD EEAVGYLENV IAMIQADSAI FDGLYKNRYF REYGEPIGPI DLEVKPILSL WGKDIKVLRV RFDSEEAAGY RIIYAPCHEK QPNGTYIRRI DILAVVNKKT DEFDYQAEHP ITKRIIKDYE ELYSN // ID Q5F6T8_NEIG1 Unreviewed; 134 AA. AC Q5F6T8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90099.1}; GN ORFNames=NGO_1458 {ECO:0000313|EMBL:AAW90099.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90099.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90099.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90099; AAW90099; NGO_1458. DR OrthoDB; EOG6W7299; -. DR BioCyc; NGON242231:GI2G-1364-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 24 42 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 134 AA; 14282 MW; 390E444FF5B7E7AC CRC64; MTKYKFPCGQ IRIPACAGMT DGNGARTFAG IFYVSILILF LMRYSKKIGC AGCFYFSDDL KSTVVNPICF SNRLQPPNLL QPAPSPVGEG RGGGILQVAA TFPNNLTAPI QALRLVALSP ALSHGERGRG GCWG // ID Q5F650_NEIG1 Unreviewed; 334 AA. AC Q5F650; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 71. DE SubName: Full=Aminoglycoside phosphotransferase {ECO:0000313|EMBL:AAW90337.1}; GN ORFNames=NGO_1716 {ECO:0000313|EMBL:AAW90337.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90337.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90337.1; -; Genomic_DNA. DR RefSeq; WP_003689901.1; NC_002946.2. DR RefSeq; YP_208749.1; NC_002946.2. DR ProteinModelPortal; Q5F650; -. DR DNASU; 3281371; -. DR EnsemblBacteria; AAW90337; AAW90337; NGO_1716. DR GeneID; 3281371; -. DR KEGG; ngo:NGO1716; -. DR PATRIC; 20337024; VBINeiGon24812_2052. DR HOGENOM; HOG000264348; -. DR KO; K07102; -. DR OMA; YGPVTYD; -. DR OrthoDB; EOG6VMTGR; -. DR BioCyc; NGON242231:GI2G-1612-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90337.1}. FT DOMAIN 23 249 APH. {ECO:0000259|Pfam:PF01636}. SQ SEQUENCE 334 AA; 38854 MW; 8AC65BEEEFC2AE72 CRC64; MQRQTELKNW LQTVYPERDF DLSFAAADAD FRRYFRAAFS DGGSVVCMDA PPDKMSVAPY LKVQKLFDMV NVPQVLHADT DLGFVVLNDL GNTTFLTAML QEQGEAAHKA LLLEAIGELV GLQKASREGV LPEYDRETML REINLFPEWF VAKELGRELT FKQRQLWQQT ADTLLPPLLA QPKVYVHRDF IVRNLMLTRG RPGVLDFQDA LYGPISYDLV SLLRDAFIEW EEEFVLDLVI RYWEKARAAG LPVPAEFDEF YRRFEWMGVQ RHLKVAGIFA RLYYRDGKDK YRPEIPRFLN YLRRVSRRYA ELAPLYALLV ELVGDEELET GFTF // ID Q5F7R0_NEIG1 Unreviewed; 453 AA. AC Q5F7R0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. DE SubName: Full=DNA helicase {ECO:0000313|EMBL:AAW89777.1}; GN ORFNames=NGO_1110 {ECO:0000313|EMBL:AAW89777.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89777.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89777.1; -; Genomic_DNA. DR RefSeq; WP_010951190.1; NC_002946.2. DR RefSeq; YP_208189.1; NC_002946.2. DR ProteinModelPortal; Q5F7R0; -. DR EnsemblBacteria; AAW89777; AAW89777; NGO_1110. DR GeneID; 3281865; -. DR KEGG; ngo:NGO1110; -. DR PATRIC; 20335472; VBINeiGon24812_1302. DR HOGENOM; HOG000113196; -. DR OMA; ESHADIF; -. DR OrthoDB; EOG6T4RW5; -. DR BioCyc; NGON242231:GI2G-1022-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 1.10.860.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR007694; DNA_helicase_DnaB-like_C. DR InterPro; IPR007693; DNA_helicase_DnaB-like_N. DR InterPro; IPR019889; DNA_helicase_DnaB-like_phg. 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 SUPFAM; SSF48024; SSF48024; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03600; phage_DnaB; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 4: Predicted; KW ATP-binding {ECO:0000313|EMBL:AAW89777.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA replication {ECO:0000256|SAAS:SAAS00435671}; KW DNA-binding {ECO:0000256|SAAS:SAAS00435659}; KW Helicase {ECO:0000313|EMBL:AAW89777.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89777.1}; KW Nucleotide-binding {ECO:0000313|EMBL:AAW89777.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 179 439 SF4 helicase. FT {ECO:0000259|PROSITE:PS51199}. SQ SEQUENCE 453 AA; 49533 MW; B6361CE3DAE24923 CRC64; MNRIEETEAV QSLASVGAEQ NILGGILIEP TAIARCAILT PEKFYQAQHR IIFRALLDMA AANEPIDIIT LNDKLEARGE AENAGGLAYL IDLNQNTPSA KNISRYVGIV NDRFVERGLL KASAAIEKIA VSKDGGTVAE KLSKAADELA AVGKDAVKRE TKTFGQTVED LIGGLDKRLD GVRFGLPTGL MKLDGMTGGL PDGNLIVIAA RPSMGKTVLA ENIARFALKQ GKAVHFQSYE MSAVELARRG MAAECNIPMQ NLKTGNLTQS DYANMPIYVS QAKEWKFDVN CDLLNVDELC FLAKEKKLTT GLDLLVVDHL HIMPRAGRDE VAELGNISRR LKNLAAELNT PVVLVAQLNR GNTKQADKRP NMADIRGSGA IEQDANIIIM PHRESYYDGN ENPSIAELII AKNRDGEMGT VVCGWKGQFM KFEEEPDLAW QAPKHDEYDP YSV // ID Q5F843_NEIG1 Unreviewed; 49 AA. AC Q5F843; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89644.1}; GN ORFNames=NGO_0955 {ECO:0000313|EMBL:AAW89644.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89644.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89644.1; -; Genomic_DNA. DR RefSeq; WP_003691061.1; NC_002946.2. DR RefSeq; YP_208056.1; NC_002946.2. DR EnsemblBacteria; AAW89644; AAW89644; NGO_0955. DR GeneID; 3282096; -. DR KEGG; ngo:NGO0955; -. DR PATRIC; 20335095; VBINeiGon24812_1117. DR HOGENOM; HOG000071276; -. DR OrthoDB; EOG69D3P9; -. DR BioCyc; NGON242231:GI2G-886-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 49 AA; 5543 MW; 3B22E4282574452A CRC64; MFHGLKRTTA LPLSGSAVLS AARTFGRHIL TLEQKIKYPK KLTIYDKLK // ID Q5F6I9_NEIG1 Unreviewed; 293 AA. AC Q5F6I9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 61. DE SubName: Full=Nicotinate-nucleotide pyrophosphorylase {ECO:0000313|EMBL:AAW90198.1}; DE EC=2.4.2.19 {ECO:0000313|EMBL:AAW90198.1}; GN ORFNames=NGO_1565 {ECO:0000313|EMBL:AAW90198.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90198.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90198.1; -; Genomic_DNA. DR RefSeq; WP_003689485.1; NC_002946.2. DR RefSeq; YP_208610.1; NC_002946.2. DR ProteinModelPortal; Q5F6I9; -. DR EnsemblBacteria; AAW90198; AAW90198; NGO_1565. DR GeneID; 3281431; -. DR KEGG; ngo:NGO1565; -. DR PATRIC; 20336640; VBINeiGon24812_1866. DR HOGENOM; HOG000224022; -. DR KO; K00767; -. DR OMA; LYDMIML; -. DR OrthoDB; EOG6KT2XH; -. DR BioCyc; NGON242231:GI2G-1466-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AAW90198.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|PIRNR:PIRNR006250, KW ECO:0000313|EMBL:AAW90198.1}. FT DOMAIN 29 117 QRPTase_N. {ECO:0000259|Pfam:PF02749}. FT DOMAIN 119 290 QRPTase_C. {ECO:0000259|Pfam:PF01729}. SQ SEQUENCE 293 AA; 31191 MW; A5E41F9A0C65C99C CRC64; MPSENPLFAL PDTLLRPMVE QALSEDLGRR GDITSAAVIA PDKTAKLFLV SREDGVIAGM DLARLAFQTM DPCVRFQAEI QDGQAVRAGQ TLAAVEGNAR ALLAAERTAL NYLTHLSGIA TATARAVAEV AEYGTDIVCS RKTIPLLRVL QKYAVRAGGG ANHRMGLDDA VLIKDNHLAY CGSIAQAVRQ AKQAVGPLTC VEIEVDTLAQ LDEAIAAGAE RILLDNMDDE TLKEAANRCH TQTAHPHTVY CEASGGIGFD RLKRVAQTGV DGIALGYLTH SSRSLDIGLD FVA // ID Q5F7E3_NEIG1 Unreviewed; 163 AA. AC Q5F7E3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AAW89894.1}; GN ORFNames=NGO_1235 {ECO:0000313|EMBL:AAW89894.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89894.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89894.1; -; Genomic_DNA. DR RefSeq; WP_002212817.1; NC_002946.2. DR RefSeq; YP_208306.1; NC_002946.2. DR ProteinModelPortal; Q5F7E3; -. DR SMR; Q5F7E3; 1-163. DR EnsemblBacteria; AAW89894; AAW89894; NGO_1235. DR GeneID; 3282490; -. DR KEGG; ngo:NGO1235; -. DR PATRIC; 20335787; VBINeiGon24812_1452. DR HOGENOM; HOG000046747; -. DR KO; K01653; -. DR OMA; PYGIREI; -. DR OrthoDB; EOG6X3W8W; -. DR BioCyc; NGON242231:GI2G-1146-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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 Q5F7G2_NEIG1 Unreviewed; 127 AA. AC Q5F7G2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=DeoR faimly transcriptional regulator {ECO:0000313|EMBL:AAW89875.1}; GN ORFNames=NGO_1216 {ECO:0000313|EMBL:AAW89875.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89875.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89875.1; -; Genomic_DNA. DR RefSeq; WP_010951219.1; NC_002946.2. DR RefSeq; YP_208287.1; NC_002946.2. DR EnsemblBacteria; AAW89875; AAW89875; NGO_1216. DR GeneID; 3281842; -. DR KEGG; ngo:NGO1216; -. DR PATRIC; 20335741; VBINeiGon24812_1429. DR HOGENOM; HOG000014819; -. DR KO; K00901; -. DR OMA; IGHEIHP; -. DR OrthoDB; EOG60W7XM; -. DR BioCyc; NGON242231:GI2G-1127-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 13783 MW; B0379B9795B036FE CRC64; MEPSSYAAEK KGKSGIRRVI NAFGYSIDGI AAAYRYEVAF RQVLWLNALL VCAAFFWVSE TAVRLPLIIA SFVSVIVELF NTAVEAAVDH TSTEKHELAK RAKDAGSAAQ LVAMLMLAAV WLSALFG // ID Q5F8Q7_NEIG1 Unreviewed; 346 AA. AC Q5F8Q7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 76. DE SubName: Full=Adenine glycosylase {ECO:0000313|EMBL:AAW89430.2}; GN ORFNames=NGO_0710 {ECO:0000313|EMBL:AAW89430.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89430.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89430.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F8Q7; -. DR EnsemblBacteria; AAW89430; AAW89430; NGO_0710. DR PATRIC; 20334548; VBINeiGon24812_0846. DR HOGENOM; HOG000028744; -. DR OMA; EADWLWY; -. DR OrthoDB; EOG6RNQH0; -. DR BioCyc; NGON242231:GI2G-670-MONOMER; -. DR Proteomes; UP000000535; 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; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 39 192 ENDO3c. {ECO:0000259|SMART:SM00478}. SQ SEQUENCE 346 AA; 39215 MW; 7D189390E2FD1373 CRC64; MNTPIPFSER LIRWQKQHGR HHLPWQVKNP YCVWLSEIML QQTQVAAVLD YYPRFLEKFP TVQTLAAAPQ DEVLSLWAGL GYYGRARNLH KAAQQIVGQF GGTFPSERKD LETLCGVGRS TAAAISAFAF NRRETILDGN VKRVLCRVFA QDGNPQDKKF ENSLWTLAES LMPSENADMP TYTQGLMDLG ATVCKRTKPL CRQCPMADIC EAKKQNRTAE LPRKKTALEV QTLPLYWLIV RNRDGAILLE KRTAKGIWGG LYCVPCFESL NGLSDFAAKL SLTMADMDEQ TALTHRLTHR LLMITPFEGQ MPSEHHSDGI WIKPGHLKDY GLPKPLEIYL NGNRLE // ID Q5F9L9_NEIG1 Unreviewed; 251 AA. AC Q5F9L9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 82. DE SubName: Full=Amino acid ABC transporter ATPase {ECO:0000313|EMBL:AAW89118.1}; GN ORFNames=NGO_0374 {ECO:0000313|EMBL:AAW89118.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89118.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89118.1; -; Genomic_DNA. DR RefSeq; WP_003687790.1; NC_002946.2. DR RefSeq; YP_207530.1; NC_002946.2. DR ProteinModelPortal; Q5F9L9; -. DR SMR; Q5F9L9; 1-246. DR EnsemblBacteria; AAW89118; AAW89118; NGO_0374. DR GeneID; 3282185; -. DR KEGG; ngo:NGO0374; -. DR PATRIC; 20333751; VBINeiGon24812_0453. DR KO; K10010; -. DR OMA; DLFDHPK; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-353-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 243 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 251 AA; 27996 MW; 10891161787DA31D CRC64; MIKIRNIHKT FGENTILRGI DLDVGKGQVV VILGPSGSGK TTFLRCLNAL EMPEDGQIEF DNARPLRIDF SKKTSKHDIL ALRRKSGMVF QQYNLFPHKT VLENVMEGPV AVQGKPAAQA REEALKLLEK VGLGDKVDLY PYQLSGGQQQ RVGIARALAI QPELMLFDEP TSALDPELVQ DVLDAMKELA REGWTMVVVT HEIKFTLEVA TNVVVMDGGV IVEQGSPKEL FDHLKHERTR RFLSQIQSAK I // ID Q5F7I9_NEIG1 Unreviewed; 484 AA. AC Q5F7I9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE RecName: Full=Magnesium transporter MgtE {ECO:0000256|RuleBase:RU362011}; GN ORFNames=NGO_1188 {ECO:0000313|EMBL:AAW89848.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89848.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89848.1; -; Genomic_DNA. DR RefSeq; WP_003696042.1; NC_002946.2. DR RefSeq; YP_208260.1; NC_002946.2. DR ProteinModelPortal; Q5F7I9; -. DR EnsemblBacteria; AAW89848; AAW89848; NGO_1188. DR GeneID; 3281981; -. DR KEGG; ngo:NGO1188; -. DR PATRIC; 20335673; VBINeiGon24812_1395. DR HOGENOM; HOG000280153; -. DR KO; K06213; -. DR OMA; RAIQRYD; -. DR OrthoDB; EOG60GRRN; -. DR BioCyc; NGON242231:GI2G-1100-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 53051 MW; 0B81B879F9618EF0 CRC64; MSIEHTPPTH DGETGQNHAE RPSADFDRVH SLCEILEPAF EQIENGTPLE DAPLRDKLTE LTVLLAELHP ADVADVLESL PPRERNIVWL LVKPEDDGEV LLEVSDAVRE TLIESMDKDE LLAAVDDLDA DELAELADDL PHQVVYEALQ TRDEEERAQV KAAMSYEDNQ VGAIMDFELV SIRADVACEV VLRYLRRFDS LPDHTDKIFV VDENDVLQGV LPIRKLLVAD PEDLVENVMA KDVVRFRAED DVEEAAQAFE RYDLVTAPVV DENKKLIGRI TIDEMVDVIR EESEADMLNM AGLQEEEDLF APVLDSVKNR WMWLAVNLCT AFLASRVIGA FEGSIEKIVA LAALMPIVAG IGGNSGNQTI TMIVRAMAMG QLTDMQAGRL LKKEVGVALV NGIIWGTVMG AVSWLLYGSL GIGLVMVAAM TLNLLLAATV GVLIPVVMEK FGRDPALGSS VLITAVTDSG GFLIFLSLAT LFLL // ID Q5F563_NEIG1 Unreviewed; 413 AA. AC Q5F563; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Tryptophan permease {ECO:0000313|EMBL:AAW90674.1}; GN ORFNames=NGO_2073 {ECO:0000313|EMBL:AAW90674.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90674.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90674.1; -; Genomic_DNA. DR RefSeq; WP_010951398.1; NC_002946.2. DR RefSeq; YP_209086.1; NC_002946.2. DR EnsemblBacteria; AAW90674; AAW90674; NGO_2073. DR GeneID; 3282844; -. DR KEGG; ngo:NGO2073; -. DR PATRIC; 20337977; VBINeiGon24812_2511. DR HOGENOM; HOG000269674; -. DR KO; K03835; -. DR OMA; IWLLGTM; -. DR OrthoDB; EOG60394J; -. DR BioCyc; NGON242231:GI2G-1968-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 60 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 81 101 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 121 141 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 282 303 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 323 342 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 348 365 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 399 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 413 AA; 44013 MW; C759780D6ACEB906 CRC64; MSAKTPSLFG GAMIIAGTVI GAGMLANPTA TSGVWFTGSL IVLLYTWFSM LSGGLMILEV NTHYPRGASF DTMVKDLLGR GWNIINGIAV AFVLYLLTYA YIFVGGDLTA KGIGSAVGGK ISLTVGQLVF FGILAFCVWA SARLVDRFTG VLIGGMVLTF IWATGGLVAD AKPSVLFDTQ APVGTGYWIY AATALPVCLA SFGFHGNVSS LLKYFKGDAP KVAKSIWAGT LVALVIYVLW QTAIQGNLPR NEFAPVIAAE GQVSVLIETL SKFAQTGNMD KILSLFSYMA IATSFLGVTL GLFDYIADIF KWNDSMSGRT KTAALTFLPP LISCLLFPTG FVTAIGCVGL AATVWTGIIP AMLLYRSRKK FGAGKTYKVY GGLWLMVWVF LFGIANIAAQ VLSQMELVPV FKG // ID Q5F7E9_NEIG1 Unreviewed; 356 AA. AC Q5F7E9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Permease {ECO:0000313|EMBL:AAW89888.1}; GN ORFNames=NGO_1229 {ECO:0000313|EMBL:AAW89888.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89888.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89888.1; -; Genomic_DNA. DR RefSeq; WP_010951221.1; NC_002946.2. DR RefSeq; YP_208300.1; NC_002946.2. DR DNASU; 3282044; -. DR EnsemblBacteria; AAW89888; AAW89888; NGO_1229. DR GeneID; 3282044; -. DR KEGG; ngo:NGO1229; -. DR PATRIC; 20335773; VBINeiGon24812_1445. DR HOGENOM; HOG000263593; -. DR KO; K11720; -. DR OMA; FAYLHAR; -. DR OrthoDB; EOG6J1D9D; -. DR BioCyc; NGON242231:GI2G-1140-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 39117 MW; E461D75D0CBC927E CRC64; MNLISRYIIR QMAVMAVYAL LAFLALYSFF EILYETGNLG KGSYGIWEML GYTALKMPAR AYELMPLAVL IGGLASLSQL AAGSELAVIK ASGMSTKKLL LILSQFGFIF AIAAVALGEW VAPTLSQKAE NIKAAAINGK ISTGNTGLWL KEKTSIINVR GMLPDHTLLG IKIWARNDKN ELAEAVEADS AVLNSDGSWQ LKNIRRSIMG TDKIETSAAA EETWPIAVRR NLMDVLLVKP DQMSVGELTT YIRHLQNNSQ NTQIYAIAWW RKLVYPVAAW VMALVAFAFT PQTTRHGNMG LKLFGGICLG LLFHLAGRLF GFTSQLYGTP PFLAGALPTI AFALLAVWLI RKQEKR // ID Q5FAE3_NEIG1 Unreviewed; 636 AA. AC Q5FAE3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 63. DE SubName: Full=Protein-PII uridylyltransferase {ECO:0000313|EMBL:AAW88844.1}; GN ORFNames=NGO_0083 {ECO:0000313|EMBL:AAW88844.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88844.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88844.1; -; Genomic_DNA. DR RefSeq; WP_003692533.1; NC_002946.2. DR RefSeq; YP_207256.1; NC_002946.2. DR ProteinModelPortal; Q5FAE3; -. DR DNASU; 3282320; -. DR EnsemblBacteria; AAW88844; AAW88844; NGO_0083. DR GeneID; 3282320; -. DR KEGG; ngo:NGO0083; -. DR PATRIC; 20333053; VBINeiGon24812_0110. DR HOGENOM; HOG000257078; -. DR OMA; FNPTDGI; -. DR OrthoDB; EOG6WQD59; -. DR BioCyc; NGON242231:GI2G-73-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW88844.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW88844.1}; 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 282 575 Polysacc_synt_2. FT {ECO:0000259|Pfam:PF02719}. SQ SEQUENCE 636 AA; 70704 MW; D939569038334A66 CRC64; MNLETLIALP RNIKKICFLI HDFLMIFTAF WFTQSLKADY SDEWFDFANW QSFLLTALLT ITLFIRMGLY RAVTRFVSFH VLTTAFAGSL ASAVLFFLNT LIFEERLRLA LPIVYFLLLF VSVTGSRMVL RGLLSDHQKK THDPVIIYGA GRSGRQLLEA VKQMREYSAA AFVDDNPKLW HTVIYDLAVY QPDAIAFLIE RYGVEKILLA IPSATQEQRR RIISKLKAYP CEVLTIPGMK DLMDGKISIG TLKKISVSDL LGRDSVAPDD RLMNADTEGK TVMVTGAGGS IGSELCRQII RRRPERLLLF ELSEFALYTV EKELCEYCAR NGIAAEILPF LGSVQNRTLL THIMTAFSVA TVYHAAAYKH VPMVEFNTVE GIRNNIFGTL ECALAATASG VETFVLISTD KAVRPANTMG AGKRMAELCL QALAAEPGQK TRFSMVRFGN VLGSSGSVVP LFEKQIAEGG PITLTHPDIT RYFMTIPEAA QLVIQAGAMG RGGDVFVLDM GESVKITDLA RQMITLSGLK PKTPEQPDGD IEILITGLRP GEKLYEELLI GDNVRKTGHP RIMTADETML PWHELSALLD RIRTACDRYD QQAIRDLLVN APTGFTPTGG ICDLLWVCET HRKNAV // ID Q5F825_NEIG1 Unreviewed; 99 AA. AC Q5F825; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89662.1}; GN ORFNames=NGO_0976 {ECO:0000313|EMBL:AAW89662.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89662.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89662.1; -; Genomic_DNA. DR RefSeq; WP_003688314.1; NC_002946.2. DR RefSeq; YP_208074.1; NC_002946.2. DR EnsemblBacteria; AAW89662; AAW89662; NGO_0976. DR GeneID; 3282872; -. DR KEGG; ngo:NGO0976; -. DR PATRIC; 20335146; VBINeiGon24812_1142. DR HOGENOM; HOG000219022; -. DR OMA; QWGRHIG; -. DR OrthoDB; EOG6CVVFD; -. DR BioCyc; NGON242231:GI2G-904-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 99 AA; 11304 MW; 240F8B78C6C3E1C0 CRC64; MHYFSIHDQS GRHIGFFILL ADDESEARLQ SGRFAVKLED GTGNHVLSPF GQTEIPQYWR VVKDRIELFF DEAPVGTLRN EYLTVSGQTF VLNDLIGNM // ID Q5F964_NEIG1 Unreviewed; 124 AA. AC Q5F964; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89273.1}; GN ORFNames=NGO_0537 {ECO:0000313|EMBL:AAW89273.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89273.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89273.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F964; -. DR EnsemblBacteria; AAW89273; AAW89273; NGO_0537. DR PATRIC; 20334122; VBINeiGon24812_0633. DR HOGENOM; HOG000038877; -. DR OMA; FAQVHAP; -. DR OrthoDB; EOG6742RM; -. DR BioCyc; NGON242231:GI2G-513-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 57 123 HMA. {ECO:0000259|PROSITE:PS50846}. SQ SEQUENCE 124 AA; 13165 MW; F5D875D970C6E0F7 CRC64; MKIVPYVETL PPPDWARLPL CRKHPCRTVS AFAQVHAPTY NNARQIAVPT KGKIVETLLL DIGGMSCGGC VKSVTRILES VKGVASVEVS LENKSATVGY DPAQTAAEAL IEAVEDGGYD AALK // ID Q5F875_NEIG1 Unreviewed; 393 AA. AC Q5F875; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 79. 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 ORFNames=NGO_0916 {ECO:0000313|EMBL:AAW89612.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89612.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89612.1; -; Genomic_DNA. DR RefSeq; WP_003691081.1; NC_002946.2. DR RefSeq; YP_208024.1; NC_002946.2. DR ProteinModelPortal; Q5F875; -. DR SMR; Q5F875; 161-393. DR EnsemblBacteria; AAW89612; AAW89612; NGO_0916. DR GeneID; 3281365; -. DR KEGG; ngo:NGO0916; -. DR PATRIC; 20335015; VBINeiGon24812_1077. DR HOGENOM; HOG000281563; -. DR KO; K00658; -. DR OMA; HRYYDIG; -. DR OrthoDB; EOG610413; -. DR BioCyc; NGON242231:GI2G-854-MONOMER; -. DR UniPathway; UPA00868; UER00840. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Lipoyl {ECO:0000256|RuleBase:RU003765, ECO:0000256|SAAS:SAAS00065550}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU003765}; KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}. FT DOMAIN 2 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 393 AA; 41685 MW; 02BA310A7CEC3547 CRC64; MIIDVKVPML SESVSEGTLL EWKKKVGEAV ARDEILIDIE TDKVVLEVPS PQAGVLVEIV AQDGETVVAD QVLARIDTAA TVAAEAPAAA PAEAAPAAVP AAAQNNAAMP AAAKLAAETG VDVNVLQGSG RDGRVLKEDV QNAAAKPAAA VAPAVALPAG ARPEERVPMS RLRARVAERL LASQQENAIL TTFNEVNMKP IMDLRAKYKE KFEKEHGVKL GFMSFFVKAA VTALKKYPVV NASVDGKDIV YHGYFDIGIA IGSPRGLVVP ILRDADQMSI ADIEQAIVDY AKKAKDGKIA IEDLTGGTFS ITNGGTFGSM MSTPIINPPQ SAILGMHATK ERAVVENGQV VVRPMMYLAL SYDHRIIDGR EAVLTLVAIK DALEDPVRLL LDL // ID Q5FAK6_NEIG1 Unreviewed; 142 AA. AC Q5FAK6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=MJ0042 family finger-like domain protein {ECO:0000313|EMBL:AAW88797.1}; GN ORFNames=NGO_0028 {ECO:0000313|EMBL:AAW88797.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88797.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88797.1; -; Genomic_DNA. DR RefSeq; WP_003690500.1; NC_002946.2. DR RefSeq; YP_207209.1; NC_002946.2. DR EnsemblBacteria; AAW88797; AAW88797; NGO_0028. DR GeneID; 3282486; -. DR KEGG; ngo:NGO0028; -. DR PATRIC; 20332886; VBINeiGon24812_0028. DR HOGENOM; HOG000218758; -. DR OMA; EGFNWTI; -. DR OrthoDB; EOG6TXQTR; -. DR BioCyc; NGON242231:GI2G-25-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118 141 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 142 AA; 15444 MW; 33D4B52DF2F7399B CRC64; MPACFCPHCK TRLWVKETQL NVAQGFVVCQ KCEGLFKAKD HLASTKEPIF NDLPEAVSDV KLVHRIGTHA ISKKQISRDE IADILNGGTT LHDTPPATAA AAPAAAPQVS VPPARQEGLN WTIATLFALI VLIMQLSYLF IL // ID Q5F795_NEIG1 Unreviewed; 446 AA. AC Q5F795; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89942.1}; GN ORFNames=NGO_1288 {ECO:0000313|EMBL:AAW89942.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89942.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89942.1; -; Genomic_DNA. DR RefSeq; WP_003694038.1; NC_002946.2. DR RefSeq; YP_208354.1; NC_002946.2. DR EnsemblBacteria; AAW89942; AAW89942; NGO_1288. DR GeneID; 3282082; -. DR KEGG; ngo:NGO1288; -. DR PATRIC; 20335919; VBINeiGon24812_1514. DR HOGENOM; HOG000219060; -. DR OMA; YGFVWET; -. DR OrthoDB; EOG6D8B6H; -. DR BioCyc; NGON242231:GI2G-1200-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021296; DUF2868. DR Pfam; PF11067; DUF2868; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 69 90 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 122 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 171 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 244 267 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 446 AA; 50102 MW; 13404D8224FE6931 CRC64; MLNPSRKLVE LVRILDEGGF IFSGDPVQAT EALRRVDGST EEKIIRRAEM IDRDRMLRDT LERVRAGSFW LWVVVASMMF TAGFSGTYLL MDNQGLNFFL VLAGVLGMNT LMLAVWLATL FLRVKVGRFF SSPATWFRGK GPVNQAVLRL YADQWRQPSV RWKIGATAHS LWLCTLLGML VSVLLLLLVR QYTFNWESTL LSNAASVRAV EMLAWLPSKL GFPVPDARAV IEGRLNGNIA DARAWSGLLV GSIVCYGILP RLLAWVVCKI LLKTSENGLD LEKTYYQAVI RRWQNKITDA DTRRETVSAV SPKIVLNDAP KWALMLETEW QDGQWFEGRL AQEWLDKGVA ANREQVAALE TELKQKPAQL LIGVRAQTVP DRGVLRQIVR LSEAAQGGAV VQLLAEQGLS DDLSEKLEHW RNALTECGAA WLEPDRVAQE GRLKDQ // ID Q5F716_NEIG1 Unreviewed; 203 AA. AC Q5F716; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 65. DE SubName: Full=Cbb3-type cytochrome c oxidase subunit II {ECO:0000313|EMBL:AAW90021.1}; GN ORFNames=NGO_1373 {ECO:0000313|EMBL:AAW90021.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90021.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90021.1; -; Genomic_DNA. DR RefSeq; WP_002212596.1; NC_002946.2. DR RefSeq; YP_208433.1; NC_002946.2. DR ProteinModelPortal; Q5F716; -. DR EnsemblBacteria; AAW90021; AAW90021; NGO_1373. DR GeneID; 3282491; -. DR KEGG; ngo:NGO1373; -. DR PATRIC; 20336135; VBINeiGon24812_1616. DR HOGENOM; HOG000277919; -. DR KO; K00405; -. DR OMA; YAWLSKT; -. DR OrthoDB; EOG6RZB37; -. DR BioCyc; NGON242231:GI2G-1286-MONOMER; -. DR Proteomes; UP000000535; 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 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 Q5F7T6_NEIG1 Unreviewed; 55 AA. AC Q5F7T6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89751.1}; GN ORFNames=NGO_1084 {ECO:0000313|EMBL:AAW89751.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89751.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89751.1; -; Genomic_DNA. DR RefSeq; WP_003688002.1; NC_002946.2. DR RefSeq; YP_208163.1; NC_002946.2. DR EnsemblBacteria; AAW89751; AAW89751; NGO_1084. DR GeneID; 3281793; -. DR KEGG; ngo:NGO1084; -. DR PATRIC; 20335418; VBINeiGon24812_1275. DR HOGENOM; HOG000218942; -. DR OMA; SFNNEAE; -. DR OrthoDB; EOG63RGXV; -. DR BioCyc; NGON242231:GI2G-996-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 55 AA; 6701 MW; 248DE05444E9C2CC CRC64; MVNEKLAENR KRYEQKRVIK KVSFNAETEK ELLEYAQNLD FSQWVKSIIK EKIKK // ID Q5F8Y2_NEIG1 Unreviewed; 668 AA. AC Q5F8Y2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Recombinase {ECO:0000313|EMBL:AAW89355.1}; GN ORFNames=NGO_0627 {ECO:0000313|EMBL:AAW89355.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89355.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89355.1; -; Genomic_DNA. DR RefSeq; WP_003688896.1; NC_002946.2. DR RefSeq; YP_207767.1; NC_002946.2. DR EnsemblBacteria; AAW89355; AAW89355; NGO_0627. DR GeneID; 3282890; -. DR KEGG; ngo:NGO0627; -. DR PATRIC; 20334338; VBINeiGon24812_0741. DR HOGENOM; HOG000218986; -. DR OMA; RTGEHYI; -. DR OrthoDB; EOG6WDSC3; -. DR BioCyc; NGON242231:GI2G-595-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 436 457 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 485 505 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; 74772 MW; 01854A533A073D20 CRC64; MADMKKITPQ NLRPLLSESL GHTDFVNVLN ALIKFLRRGG KKCAGERFDL IIDTFKQDRE LLSRFSRCFY IWLAQIHIYP ALIKLGIFSR HSFAREMGIR IYERFNPSYK DFANLGEVFL YLFHSENDDK WLQTLNIRQW LVLYELIRSH AEPSKLQTAG IRLADARLRA IEMLSVWTAS EAIEPDLIRI APRLLEADSS FVALQRETAK LVEHYRNGTA PYDTAHLEVM FDQCFSQIDY LRRKGTGAGS GSSVKVAHLL ERLRQTVGRL KLLTDIQTGA GNSNRLTIAL MNSLIYAAVE QYSTRHLRRS SIRMLARSIT ENKSHHGEHY ITRNRKEYFK MFYSAAGGGG IIALMALLKI RIGTLDLSPF LASLSAGFNY GIGFMIIHML HCTVATKQPA MTAASFAEQV DLNEGGKAVD NKLSKLLIDV CRSQSVAVFG NVSIAILLAC AISFGYAHLY RLPILDAHTA AYQFKSIDII NHPTLWYAAI AGLWLFCSGI IAGFFDNRAD YLNLRQRLPF NPLLRKIMRP GPRRVLAAYI HKHYGSLVGN FIFGMLLGMT GYFGHLLGLP LDIRHVAFSS ANLGYAAVSG NVGFGTFVLG IFSVLAIGLV NLCVSFSLAL FVALRSRGTK IGSIRNLIKS FWNQIKSNPC ILFLPPAKGQ GHPPSDKP // ID Q5F9L6_NEIG1 Unreviewed; 471 AA. AC Q5F9L6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 58. DE SubName: Full=Anion:sodium symporter {ECO:0000313|EMBL:AAW89121.1}; GN ORFNames=NGO_0377 {ECO:0000313|EMBL:AAW89121.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89121.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89121.1; -; Genomic_DNA. DR RefSeq; WP_010359883.1; NC_002946.2. DR RefSeq; YP_207533.1; NC_002946.2. DR EnsemblBacteria; AAW89121; AAW89121; NGO_0377. DR GeneID; 3281910; -. DR KEGG; ngo:NGO0377; -. DR PATRIC; 20333757; VBINeiGon24812_0456. DR HOGENOM; HOG000278433; -. DR KO; K14445; -. DR OMA; RTNFSIC; -. DR OrthoDB; EOG6GN72M; -. DR BioCyc; NGON242231:GI2G-356-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 269 288 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 300 317 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; 50660 MW; DD3E1E935EA3906C CRC64; MNLHAKDKTQ HPENVELLSA QKPITDFKGL LTTIISAVVC FGIYHILPYS PDANKGIALL IFVAALWFTE AVHITVTALM VPILAVVLGF PDMDIKKAMA DFSNPIIYIF FGGFALATAL HMQRLDRKIA VSLLRLSRGN MKVAVLMLFL VTAFLSMWIS NTATAAMMLP LAMGMLSHLD REKEHKTYVF LLLGIAYCAS IGGLGTLVGS PPNLIAAKAL NLDFVGWMKL GLPMMLLILP LMLLSLYVIL KPNLNERVEI KAESIPWTLH RVIALLIFLA TAAAWIFGSK IKTAFGISNP DTVIALSAAV AVVVFGVAQW KEVARNTDWG VLMLFGGGIS LSTLLKTSGA SEALGQQVAA TFSGAPAFLV ILIVAAFIIF LTEFTSNTAS AALLVPIFSG IAMQMGLPEQ VLVFVIGIAA SCAFMLPVAT PPNAIVFGTG LIKQREMMNV GILLNILCVV LVALWAYAVL M // ID Q5F5E1_NEIG1 Unreviewed; 291 AA. AC Q5F5E1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 68. DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000256|HAMAP-Rule:MF_01877}; DE EC=2.1.1.198 {ECO:0000256|HAMAP-Rule:MF_01877}; DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01877}; DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000256|HAMAP-Rule:MF_01877}; GN Name=rsmI {ECO:0000256|HAMAP-Rule:MF_01877}; GN ORFNames=NGO_1988 {ECO:0000313|EMBL:AAW90596.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90596.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine CC 1402 (C1402) in 16S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01877}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01877}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI CC family. {ECO:0000256|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; AE004969; AAW90596.1; -; Genomic_DNA. DR RefSeq; WP_010951377.1; NC_002946.2. DR RefSeq; YP_209008.1; NC_002946.2. DR ProteinModelPortal; Q5F5E1; -. DR EnsemblBacteria; AAW90596; AAW90596; NGO_1988. DR GeneID; 3282636; -. DR KEGG; ngo:NGO1988; -. DR PATRIC; 20337743; VBINeiGon24812_2398. DR HOGENOM; HOG000195941; -. DR KO; K07056; -. DR OMA; IALHDHN; -. DR OrthoDB; EOG6677TH; -. DR BioCyc; NGON242231:GI2G-1886-MONOMER; -. DR Proteomes; UP000000535; 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 {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01877}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01877, KW ECO:0000313|EMBL:AAW90596.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01877}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01877}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01877, KW ECO:0000313|EMBL:AAW90596.1}. FT DOMAIN 17 216 TP_methylase. {ECO:0000259|Pfam:PF00590}. SQ SEQUENCE 291 AA; 31259 MW; F255CD3E9C74A0C0 CRC64; MFQKHLQKAS DSVVGGTLYV VATPIGNLAD ITLRALAVLQ KADIICAEDT RVTAQLLSAY GIQGRLVSVR EHNERQMADK VIGFLSDGLV VAQVSDAGTP AVCDPGAKLA RRVREAGFKV VPVVGASAVM AALSVAGVAE SDFYFNGFVP PKSGERRKLF AKWVRAAFPV VMFETPHRIG ATLADMAELF PERRLMLARE ITKTFETFLS GTVGEIQTAL AADGNQSRGE MVLVLYPAQD EKHEGLSESA QNAMKILAAE LPTKQAAELA AKITGEGKKA LYDLALSWKN K // ID Q5F6D3_NEIG1 Unreviewed; 215 AA. AC Q5F6D3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Putative phage associated protein {ECO:0000313|EMBL:AAW90254.1}; GN ORFNames=NGO_1626 {ECO:0000313|EMBL:AAW90254.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90254.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90254.1; -; Genomic_DNA. DR RefSeq; WP_003703843.1; NC_002946.2. DR RefSeq; YP_208666.1; NC_002946.2. DR EnsemblBacteria; AAW90254; AAW90254; NGO_1626. DR GeneID; 3281393; -. DR KEGG; ngo:NGO1626; -. DR PATRIC; 20336790; VBINeiGon24812_1940. DR HOGENOM; HOG000289753; -. DR OMA; VSMPHGP; -. DR OrthoDB; EOG6NWBT5; -. DR BioCyc; NGON242231:GI2G-1523-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR025272; DUF4065. DR Pfam; PF13274; DUF4065; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 55 165 DUF4065. {ECO:0000259|Pfam:PF13274}. SQ SEQUENCE 215 AA; 24302 MW; 534ABFB91466116D CRC64; MYGNVPDLDC LLYRKPHIIK SMKPHNDTIF QEPKAAQAAA FLLYKANGRL EVLKLMKLMY LAERESFLRF GEGLTGDALV SMPHGPVLSM TLDFINGGHE SVPNGWATWV SDRENRMLAL RDPSMIRTPG QDLSALSEAD LEVLESVWEN YGHYSAWDLR NMTHNGLCPE WEDPHGSSRP IPIKKLLSVL GYDDEQAVAI VERLEEQAYI NRAFG // ID Q5F6N3_NEIG1 Unreviewed; 384 AA. AC Q5F6N3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 55. DE SubName: Full=NnrS protein {ECO:0000313|EMBL:AAW90154.2}; GN ORFNames=NGO_1516 {ECO:0000313|EMBL:AAW90154.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90154.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90154.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6N3; -. DR EnsemblBacteria; AAW90154; AAW90154; NGO_1516. DR PATRIC; 20336514; VBINeiGon24812_1805. DR HOGENOM; HOG000284064; -. DR OMA; GINGTKH; -. DR OrthoDB; EOG6VHZ9K; -. DR BioCyc; NGON242231:GI2G-1420-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 98 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 150 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 182 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 244 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 256 276 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 282 304 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; 41739 MW; 36F4454097644EB1 CRC64; MKFTKHPVWA MAFRPFYSLA ALYGALSVLL WGFGYTGTHE LSGFYWHAHE MIWGYAGLVV IAFLLTAVAT WTGQPPTRGG VLVGLTAFWL AARIAAFIPG WGAAASGILG TLFFWYGAVC MALPVIRSQN RRNYVAVFAI FVLGGTHAAF HVQLHNGNLG GLLSGLQSGL VMVSGFIGLI GMRIISFFTS KRLNVPQIPS PKWVAQASLW LPMLTAILMA HGVMPWLSAA FAFAAGVIFT VQVYRWWYKP VLKEPMLWIL FAGYLFTGLG LIAVGASYFK PAFLNLGVHL IGVGGIGVLT LGMMARTALG HTGNSIYPPP KAVPVAFWLM MAATAVRMVA VFSSGTAYTH SIRTSSVLFA LALLVYAWKY IPWLIRPRSD GRPG // ID Q5F9A7_NEIG1 Unreviewed; 168 AA. AC Q5F9A7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89230.1}; GN ORFNames=NGO_0492 {ECO:0000313|EMBL:AAW89230.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89230.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89230.1; -; Genomic_DNA. DR RefSeq; WP_003706020.1; NC_002946.2. DR RefSeq; YP_207642.1; NC_002946.2. DR DNASU; 3282956; -. DR EnsemblBacteria; AAW89230; AAW89230; NGO_0492. DR GeneID; 3282956; -. DR KEGG; ngo:NGO0492; -. DR PATRIC; 20334024; VBINeiGon24812_0584. DR OMA; INSVECF; -. DR OrthoDB; EOG615VQX; -. DR BioCyc; NGON242231:GI2G-470-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011993; PH_dom-like. DR SUPFAM; SSF50729; SSF50729; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 168 AA; 19127 MW; 73C2A273786CA253 CRC64; MSKAINKLNE KEKEKIRLLF AQREKFYRIL ENPEQGFTPP TALLKSGETC FLIDYVNMGE VVTERVRTYT GTRLKLGSTP VYLGGGKSVA NEKQKNVAYG ELVLTNFRLI FVGNMRSIDL PLDKINSVEC FQSSIRISQS GKNKPIFFNT VFNPQLWKEA ILVLSDKK // ID Q5F5N4_NEIG1 Unreviewed; 140 AA. AC Q5F5N4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90503.1}; GN ORFNames=NGO_1886 {ECO:0000313|EMBL:AAW90503.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90503.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90503.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90503; AAW90503; NGO_1886. DR PATRIC; 20337472; VBINeiGon24812_2267. DR OMA; QMFNRIP; -. DR OrthoDB; EOG6PP9W4; -. DR BioCyc; NGON242231:GI2G-1787-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 40 67 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 140 AA; 16211 MW; 3EB2C7C90BB367E1 CRC64; MAGCLTDLEN CLEKYLEQFG PVSESIEACT AKLQEQPSFF NRLMKANDKL NRQIDVLQKQ SAAIHNEAYI EMNTLLYRHR EVVSIHNRKA DYAEKGKERI ALFPRGLNGI TKLPAAVLLP ERPYHFDMKE VLYIFSRIPR // ID Q5F958_NEIG1 Unreviewed; 687 AA. AC Q5F958; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Type III restriction endonuclease subunit M {ECO:0000313|EMBL:AAW89279.1}; GN ORFNames=NGO_0545 {ECO:0000313|EMBL:AAW89279.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89279.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89279.1; -; Genomic_DNA. DR RefSeq; WP_010951079.1; NC_002946.2. DR RefSeq; YP_207691.1; NC_002946.2. DR ProteinModelPortal; Q5F958; -. DR REBASE; 10623; M.NgoAX. DR EnsemblBacteria; AAW89279; AAW89279; NGO_0545. DR GeneID; 3282907; -. DR KEGG; ngo:NGO0545; -. DR PATRIC; 20334140; VBINeiGon24812_0642. DR HOGENOM; HOG000253523; -. DR KO; K07316; -. DR OMA; FRTICDI; -. DR OrthoDB; EOG6W9X8K; -. DR BioCyc; NGON242231:GI2G-519-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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; -; 3. DR InterPro; IPR002295; D21N6_MeTrfase. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1. DR PRINTS; PR00506; D21N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 3. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89279.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89279.1}; KW Nuclease {ECO:0000313|EMBL:AAW89279.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 149 509 N6_N4_Mtase. {ECO:0000259|Pfam:PF01555}. SQ SEQUENCE 687 AA; 77483 MW; 29A5EDC04EFE2F20 CRC64; MLPTQPNPTQ PNPTQPNPTQ PNPSPDLSDT AGANTEAIYT SDGITANSTQ LEQLKKLFPA CFDADGNFLI DRLQAEIAPQ TDIGREFYEM NWLGKSYARL LRNLPPETLI SEDKTHNAKP ENAGSQNLLI RGDNLEVLKH LKNAYANSVK MIYIDPPYNT GSDGFVYQDD RKFTPAELAL LANIDEDEAA RILDFTDKGS NSHSAWLTFM YPRLYIAREL LKDDGVIFIS IDDNEAAQLK LLCDEVFGEG NFVAQLPWRK RTAKSDVPFG ISQDYEWIFV FAKSCQFIAA TKGKERRYYE TDDFPDRPWR THDLTKQTTA AERPNSFFTM VDPKTGKKYP ANPNATWRVT KDTFQDYYNK GKIVFPDDYD FLNISNPVMR YFKDDDMKKA GEDFGKVAVS SRLPENVGTL ADAVAEYLAI FSRTLPENIG MTKEGTKEIT DLFGSKIFTF PKPSQLIKFL VSISSKSNDL ILDFFAGSGT TAHAVMQLNA EGQNGNRRYI CVQLPEKTAE KSEARKAGYP TIFDITKARI EKAAAKIRVE HPDYTGDSGF KIFQTADNFR QHPDKDFSPE QPDLPLNDEL SEEQLQTLLT TWTLYDGAAL TTPVEPVRLG SYTAYLCEKR LYLLNKGFTS ADLLAFIKKL DDDADFNPNR VIVFGSNMAS AMQHELDQAV RGYTNKKEIE LNVIIRV // ID Q5F8R9_NEIG1 Unreviewed; 171 AA. AC Q5F8R9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89418.1}; GN ORFNames=NGO_0693 {ECO:0000313|EMBL:AAW89418.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89418.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89418.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89418; AAW89418; NGO_0693. DR BioCyc; NGON242231:GI2G-658-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 171 AA; 19149 MW; 7D4EA74191813053 CRC64; MLKNEIRGGL GIPPDWATMR GQAKKTNVFA DAEKRVFRRE KRIVQHPLIR FPSVWLNDIG AAPLFGRPHF IATHCLPDSR FNSKPFQYFV QTWIAADGGV QAPQGFFGFY GTARISPNGK IALTELKTFG IVQNGICVSL TAFPKGILSR IRENADGVFS VFSVIKFKFL F // ID Q5F6P4_NEIG1 Unreviewed; 140 AA. AC Q5F6P4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90143.1}; GN ORFNames=NGO_1505 {ECO:0000313|EMBL:AAW90143.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90143.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90143.1; -; Genomic_DNA. DR RefSeq; WP_003689388.1; NC_002946.2. DR RefSeq; YP_208555.1; NC_002946.2. DR EnsemblBacteria; AAW90143; AAW90143; NGO_1505. DR GeneID; 3281572; -. DR KEGG; ngo:NGO1505; -. DR PATRIC; 20336484; VBINeiGon24812_1790. DR HOGENOM; HOG000219092; -. DR OMA; WQAARIR; -. DR OrthoDB; EOG6BPDPM; -. DR BioCyc; NGON242231:GI2G-1409-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 140 AA; 15649 MW; D214E3D032CF358E CRC64; MNKNRKLLLA ALLLTAFAAF KLVLLQWWQA QQPQAVAAQC DLTEGCTLPD GSRVRAAAVS TKKPFDIYIE HAPAGTEQVS ISFSMKNMDM GFNRYMFERQ PSGTWQAARI RLPVCVEGRR DFTADITIGS RTFQTAFTAE // ID Q5F813_NEIG1 Unreviewed; 282 AA. AC Q5F813; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 73. DE SubName: Full=AraC family transcriptional regulator {ECO:0000313|EMBL:AAW89674.2}; GN ORFNames=NGO_0990 {ECO:0000313|EMBL:AAW89674.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89674.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89674.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F813; -. DR DNASU; 3281628; -. DR EnsemblBacteria; AAW89674; AAW89674; NGO_0990. DR PATRIC; 20335184; VBINeiGon24812_1160. DR HOGENOM; HOG000071272; -. DR OMA; CRANHAL; -. DR OrthoDB; EOG62ZHT7; -. DR BioCyc; NGON242231:GI2G-917-MONOMER; -. DR Proteomes; UP000000535; 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 Gene3D; 2.60.120.280; -; 1. DR InterPro; IPR003313; AraC-bd. 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; 1. DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000700, KW ECO:0000256|SAAS:SAAS00503812}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 167 264 HTH araC/xylS-type DNA-binding. FT {ECO:0000259|PROSITE:PS01124}. SQ SEQUENCE 282 AA; 30836 MW; 9EA8C32CCC4A741D CRC64; MPSNYFHTRE RLGALGGIVQ HHTALYRSVA VYEPTVVIVR RGCKKLRWAG RELRIAAGEA VGLAGGQTLD VINIPDSDGL YQAQWIAFEQ ETVERFAAQY GTAQAVCDAV KLPHPGRMGA AFDYAAAVLA DEEVPHNAAE AALCGVLAWL QHDGIGFAVY GGVNLMRQIR KLITADMAAD WSSAMLAQRL NCSEAALRRR LARQDTNFRT LLTDVRMMRA LTLLQVTQWS VAQIAGAVGY DCPSRFSARF KELFGCVPSV VRSEAEPAAY RRTGQVSVGV RP // ID Q5F7T2_NEIG1 Unreviewed; 161 AA. AC Q5F7T2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Phage associated protein {ECO:0000313|EMBL:AAW89755.1}; GN ORFNames=NGO_1088 {ECO:0000313|EMBL:AAW89755.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89755.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89755.1; -; Genomic_DNA. DR RefSeq; WP_003706423.1; NC_002946.2. DR RefSeq; YP_208167.1; NC_002946.2. DR EnsemblBacteria; AAW89755; AAW89755; NGO_1088. DR GeneID; 3281133; -. DR KEGG; ngo:NGO1088; -. DR PATRIC; 20335428; VBINeiGon24812_1280. DR HOGENOM; HOG000071259; -. DR OMA; LYAKANY; -. DR OrthoDB; EOG61CM1N; -. DR BioCyc; NGON242231:GI2G-1000-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 161 AA; 17753 MW; 7CBB19E3ABD7479A CRC64; MKRRPGICLC GVAVFDNAVR TAAGGWMDKV FIKYIGGRAV WRDRIYHTGL VFEDGQVREV SAGAAAKLLR HGDVFAAVPG KRVEKADDTE ALEKAGASEL EREAAAFDAV QDVILQINRM GKDELELYAK ANYGQGLDKR KSAENLREAV VRMVRQFGIV Q // ID Q5F6L2_NEIG1 Unreviewed; 452 AA. AC Q5F6L2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 88. 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 ORFNames=NGO_1539 {ECO:0000313|EMBL:AAW90175.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90175.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90175.1; -; Genomic_DNA. DR RefSeq; WP_010358960.1; NC_002946.2. DR RefSeq; YP_208587.1; NC_002946.2. DR ProteinModelPortal; Q5F6L2; -. DR EnsemblBacteria; AAW90175; AAW90175; NGO_1539. DR GeneID; 3281501; -. DR KEGG; ngo:NGO1539; -. DR PATRIC; 20336574; VBINeiGon24812_1835. DR HOGENOM; HOG000268120; -. DR KO; K01929; -. DR OMA; YTALHMP; -. DR OrthoDB; EOG6PKFCR; -. DR BioCyc; NGON242231:GI2G-1441-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02019}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02019, KW ECO:0000256|RuleBase:RU003630, ECO:0000313|EMBL:AAW90175.1}; 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:UP000000535}. FT DOMAIN 24 96 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 106 296 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 316 398 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 108 114 ATP. {ECO:0000256|HAMAP-Rule:MF_02019}. SQ SEQUENCE 452 AA; 47774 MW; EB1AAFACA6202C6F CRC64; MKPLDLNFIC QALKLPMPSE NKPVSRIVTD SRDIREGDVF FALAGGRFDA HDFVGGVLSA GAAAVVVSRE DCAALGGALK VDDTLAALQT LAKAWRDNVN PFVFGITGSG GKTTVKEMLA AVLRRRFGDD AVSATAGNFN NHIGLPLTLL KLNEKHRYAV IEMGMNHFGE LAVLTQIAKP DAALVNNALR AHVGCGFDGV GDIAKAKSEI YAGLCSDGMA LIPQEDANMA VFKTATFNLN TCTFGVDSGD VRAENIVLKP LSCEFDLVCG DERTAVVLPV PGRHNVHNAA AAAALALAAG LSLNDVAEGL QGFSNIKGRL NVKAGIKGAT LIDDTYNANP DSMKAAVDVL ARMPAPRIFV MGDMGELGED EAAAMHAEVG AYARDQGIEA AYFVGDNSVE AAEKFGADGL WFAAKDPLIQ VLSHDLPERA TVLVKGSRFM QMEEVVEALE DK // ID Q5F5G0_NEIG1 Unreviewed; 119 AA. AC Q5F5G0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90577.1}; GN ORFNames=NGO_1967 {ECO:0000313|EMBL:AAW90577.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90577.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90577.1; -; Genomic_DNA. DR RefSeq; WP_002215099.1; NC_002946.2. DR RefSeq; YP_208989.1; NC_002946.2. DR EnsemblBacteria; AAW90577; AAW90577; NGO_1967. DR GeneID; 3282655; -. DR KEGG; ngo:NGO1967; -. DR PATRIC; 20337695; VBINeiGon24812_2374. DR HOGENOM; HOG000218645; -. DR OrthoDB; EOG6GTZM7; -. DR BioCyc; NGON242231:GI2G-1867-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR028964; Imm8. DR Pfam; PF15586; Imm8; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 14200 MW; 6465624063C18745 CRC64; MIKLDLKSIN LYDIDFEKFT PEIPDNFHRW IDLDIGIEGE QGSSIFSLCI CSPKWISHHC NKEGFFWSNA LILEQFDHKI IKSEIDKILE YCSKETWDLT LSNLLRFFSW EFEDYNPNT // ID Q5F7W8_NEIG1 Unreviewed; 404 AA. AC Q5F7W8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAW89719.1}; DE EC=2.6.1.2 {ECO:0000313|EMBL:AAW89719.1}; GN ORFNames=NGO_1047 {ECO:0000313|EMBL:AAW89719.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89719.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89719.1; -; Genomic_DNA. DR RefSeq; WP_003695054.1; NC_002946.2. DR RefSeq; YP_208131.1; NC_002946.2. DR ProteinModelPortal; Q5F7W8; -. DR PRIDE; Q5F7W8; -. DR EnsemblBacteria; AAW89719; AAW89719; NGO_1047. DR GeneID; 3282573; -. DR KEGG; ngo:NGO1047; -. DR PATRIC; 20335318; VBINeiGon24812_1225. DR HOGENOM; HOG000223042; -. DR KO; K14260; -. DR OMA; RIVFLPH; -. DR OrthoDB; EOG6X9MJ6; -. DR BioCyc; NGON242231:GI2G-964-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004021; F:L-alanine: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 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:AAW89719.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89719.1}. FT DOMAIN 56 381 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 404 AA; 45426 MW; C77347B34FFD1028 CRC64; MDKFPKSAKL DHVCYDIRGP VHKKALQLEE EGNKILKLNI GNPAPFGFEA PDEILVDVIR NLPTSQGYCD SKGLYSARKA IVHYYQNKGL RDITVNDVYI GNGVSELIAM SMQALLNDGD EILIPAPDYP LWTAAATLAG GTVRHYLCDE ENGWFPNLAD MEAKITSKTK AIVVINPNNP TGAVYSKEIL LEIAELARKH GLIIFADEIY DKILYDGAVH YHIAALAPDL LTVTFNGLSK AYRVAGFRQG WMVLNGPKHH AKGYIEGLDM LSSMRLCANT PMQHAIQTAL GGYQSINEFI LPGGRLLEQR NRAWELVNQI PGVSCVKPMG AMYMFPKIDT EMYRIRDDMK FVYDLLVREK VLLVQGTGFN WIKPDHFRIV TLPYVHQIEE AMGRLARFLQ TYHQ // ID Q5F9F3_NEIG1 Unreviewed; 389 AA. AC Q5F9F3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=Cytochrome C550 {ECO:0000313|EMBL:AAW89184.1}; GN ORFNames=NGO_0443 {ECO:0000313|EMBL:AAW89184.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89184.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89184.1; -; Genomic_DNA. DR RefSeq; WP_003687902.1; NC_002946.2. DR RefSeq; YP_207596.1; NC_002946.2. DR ProteinModelPortal; Q5F9F3; -. DR EnsemblBacteria; AAW89184; AAW89184; NGO_0443. DR GeneID; 3282456; -. DR KEGG; ngo:NGO0443; -. DR PATRIC; 20333912; VBINeiGon24812_0530. DR HOGENOM; HOG000086623; -. DR KO; K07258; -. DR OMA; GTIDFKL; -. DR OrthoDB; EOG6RJV2H; -. DR BioCyc; NGON242231:GI2G-422-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256630. FT DOMAIN 285 375 PBP5_C. {ECO:0000259|SMART:SM00936}. SQ SEQUENCE 389 AA; 42701 MW; F9721757E6D87B62 CRC64; MTAHKILPVL LPIILGVSHA TAASPAPNRP TVHAAPTLQT PETLTAAHIV IDLQSRQTLS AKNTNTPVEP AALTQLMTAY LVFKNMKSGN IQSEENLKIP ESAWASEGSR MFVRPGDTVS TDKLLKGMIA LCANDAALTL ADRLGNGSIE NFVQQMNKEA RRLGMKNTVF KNPTGLGREG QVSTAKDLSL LSEALMRDFP EYYPLFSIKS FKFENIEQNN RNILLYRDNN VNGLKAGHTE SGGYNLAVSY SGNGRHILVI TLGSESAETR ASDNSKLLNR ALQAFDTPKI YPKGKTVAQI QISGGSKKTV RAGFLKEAYI TLPHKEAKMA EQILETIQPI PAPVKKGQIL GKIKIRQNGH TIAEKEIVAL ENVEKRSRWQ RLWTRLTGQ // ID Q5F6A4_NEIG1 Unreviewed; 288 AA. AC Q5F6A4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 61. 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 ORFNames=NGO_1656 {ECO:0000313|EMBL:AAW90283.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90283.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90283.1; -; Genomic_DNA. DR RefSeq; WP_003689790.1; NC_002946.2. DR RefSeq; YP_208695.1; NC_002946.2. DR ProteinModelPortal; Q5F6A4; -. DR EnsemblBacteria; AAW90283; AAW90283; NGO_1656. DR GeneID; 3281308; -. DR KEGG; ngo:NGO1656; -. DR PATRIC; 20336858; VBINeiGon24812_1974. DR HOGENOM; HOG000219115; -. DR OMA; MGDQNWQ; -. DR OrthoDB; EOG62G5KP; -. DR BioCyc; NGON242231:GI2G-1552-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU363014, KW ECO:0000256|SAAS:SAAS00522988}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5006528990. FT DOMAIN 152 246 PpiC. {ECO:0000259|PROSITE:PS50198}. SQ SEQUENCE 288 AA; 31528 MW; 63E2698833677BB9 CRC64; MKAKILTSVA LLACSGSLFA QTLATVNGQK IDSSVIDAQV AAFRAENSRA EDTPQLRQSL LENEVVNTVV AQEVKRLKLD RSAEFKDALA KLRAEAKKSG DDKKPSFKTV WQAVKYGLNG EAYALHIAKT QPVSEQEVKA VYDNISGFYK GTQEVQLGEI LTDKEENAKK AVADLKAKKG FDAVLKQYSL NDRTKRTGAP DGYVPLKDLE QGVPPLYQAI KDLKKGEFTA TPLKNGDFYG VYYVNDSREV KVPSFDEMKG QIAGNLQAER IDRAVGALLG KANIKPAK // ID Q5F6A8_NEIG1 Unreviewed; 280 AA. AC Q5F6A8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 13-APR-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90279.2}; GN ORFNames=NGO_1652 {ECO:0000313|EMBL:AAW90279.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90279.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90279.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90279; AAW90279; NGO_1652. DR PATRIC; 20336850; VBINeiGon24812_1970. DR HOGENOM; HOG000122546; -. DR OMA; QELLFIN; -. DR OrthoDB; EOG66XBBZ; -. DR BioCyc; NGON242231:GI2G-1548-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003497; BRO_N_domain. DR Pfam; PF02498; Bro-N; 1. DR SMART; SM01040; Bro-N; 1. DR PROSITE; PS51750; BRO_N; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 103 Bro-N. {ECO:0000259|PROSITE:PS51750}. SQ SEQUENCE 280 AA; 30878 MW; 01BD04E138056A5B CRC64; MQNTISVFSF KSQNVRTQIL GAEPWFCLGD VAEILQIQNA RQLPLKDQGI QKSSVATKKG NQELLFINEP NLYRVIFRSR KAEAVKFQDW IFEEVIPQIR KTGGYQITPK TTADDRTGLR RAVAALVGRK RIGYSSAYSM IHQRFNVEAV EGIPADKLPE AVAYVHALTL HTGLAGEVPD REPLPAPQPA LPISGNALAD IAAMVYYGTR MIELGKDVSA PLKQLGCKQA VTMWTVWHET RSILKRSVAA LEVLRGYADK DASGRIAACL EGIYGKAAAR // ID Q5F5W7_NEIG1 Unreviewed; 166 AA. AC Q5F5W7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 59. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90420.2}; GN ORFNames=NGO_1802 {ECO:0000313|EMBL:AAW90420.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90420.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90420.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F5W7; -. DR EnsemblBacteria; AAW90420; AAW90420; NGO_1802. DR PATRIC; 20337254; VBINeiGon24812_2162. DR HOGENOM; HOG000261755; -. DR OMA; ESKQARN; -. DR OrthoDB; EOG6F297R; -. DR BioCyc; NGON242231:GI2G-1700-MONOMER; -. DR Proteomes; UP000000535; 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 Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5005364410. SQ SEQUENCE 166 AA; 19089 MW; 0CC9B51FC2F6E69C CRC64; MIRLTRAFAA ALIGLCCTTG AHADTFQKIG FINTERIYLE SKQARNIQKT LDGEFSARQD ELQKLQREGL DLERQLAGGK LKDAKKAQAE EKWRGLVEAF RKKQAQFEED YNLRRNEEFA SLQQNANRVI VKIAKQEGYD VILQDVIYVN TQYDVTDSVI KEMNAR // ID Q5F7M3_NEIG1 Unreviewed; 74 AA. AC Q5F7M3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89814.1}; GN ORFNames=NGO_1147 {ECO:0000313|EMBL:AAW89814.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89814.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89814.1; -; Genomic_DNA. DR RefSeq; WP_003689739.1; NC_002946.2. DR RefSeq; YP_208226.1; NC_002946.2. DR EnsemblBacteria; AAW89814; AAW89814; NGO_1147. DR GeneID; 3282143; -. DR KEGG; ngo:NGO1147; -. DR PATRIC; 20335554; VBINeiGon24812_1342. DR OrthoDB; EOG6KQ6KK; -. DR BioCyc; NGON242231:GI2G-1060-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 74 AA; 8934 MW; 494FD4B4695BFF23 CRC64; MFIFYTVNPE HVYFPKAYIM KVFKDKGYES QCITTVSFYI CNPTLKQKTE NEAYEYGRLF VKELMHKECN RESL // ID Q5F8B2_NEIG1 Unreviewed; 286 AA. AC Q5F8B2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Restriction endonuclease NgoMIV {ECO:0000313|EMBL:AAW89575.1}; GN ORFNames=NGO_0874 {ECO:0000313|EMBL:AAW89575.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89575.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89575.1; -; Genomic_DNA. DR RefSeq; WP_010951140.1; NC_002946.2. DR RefSeq; YP_207987.1; NC_002946.2. DR ProteinModelPortal; Q5F8B2; -. DR SMR; Q5F8B2; 1-285. DR REBASE; 1326; NgoAIV. DR EnsemblBacteria; AAW89575; AAW89575; NGO_0874. DR GeneID; 3281831; -. DR KEGG; ngo:NGO0874; -. DR PATRIC; 20334921; VBINeiGon24812_1030. DR HOGENOM; HOG000229809; -. DR OMA; HASISCK; -. DR OrthoDB; EOG63Z75P; -. DR BioCyc; NGON242231:GI2G-817-MONOMER; -. DR Proteomes; UP000000535; Chromosome. 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; 3.40.50.10010; -; 1. DR InterPro; IPR015105; NgoMIV. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF09015; NgoMIV_restric; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89575.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89575.1}; KW Nuclease {ECO:0000313|EMBL:AAW89575.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 286 AA; 31793 MW; 7D09772EF210817C CRC64; MNPLFTQERR IFHKKLLDGN ILATNNRGVV SNADGSNTRS FNIAKGIADL LHSETVSERL PGQTSGNAFE AICSEFVQSA FEKLQHIRPG DWNVKQVGSR NRLEIARYQQ YAHLTALAKA AEENPELAAA LGSDYTITPD IIVTRNLIAD AEINRNEFLV DENIATYASL RAGNGNMPLL HASISCKWTI RSDRAQNARS EGLNLVRNRK GRLPHIVVVT AEPTPSRISS IALGTGEIDC VYHFALYELE QILQSLNYED ALDLFYIMVN GIRLKDISDL PLDLAF // ID Q5FAG5_NEIG1 Unreviewed; 169 AA. AC Q5FAG5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:AAW88822.1}; GN ORFNames=NGO_0057 {ECO:0000313|EMBL:AAW88822.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88822.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88822.1; -; Genomic_DNA. DR RefSeq; WP_003687293.1; NC_002946.2. DR RefSeq; YP_207234.1; NC_002946.2. DR ProteinModelPortal; Q5FAG5; -. DR EnsemblBacteria; AAW88822; AAW88822; NGO_0057. DR GeneID; 3282274; -. DR KEGG; ngo:NGO0057; -. DR PATRIC; 20332964; VBINeiGon24812_0066. DR HOGENOM; HOG000283395; -. DR OMA; WLTRKKM; -. DR OrthoDB; EOG6QG8RK; -. DR BioCyc; NGON242231:GI2G-51-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 30 167 Thioredoxin. FT {ECO:0000259|PROSITE:PS51352}. SQ SEQUENCE 169 AA; 18378 MW; 79969B62318F8841 CRC64; MKKKLLSGIK FAVRTALVFL LVSLFLDWVR KPDEPAGAAG RPLTLLSGQR LTLGQFSRDR TVLVYFWGSW CGVCRYQSPI IDDLAADGVP VVGVAVRSGS ASEVAAYMAK RGLGFPTVSD EDGGLARSWR IAATPAVVLV KNGKMVRYTT GISSYWGLRA RIFQADFFG // ID Q5F6U5_NEIG1 Unreviewed; 67 AA. AC Q5F6U5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90092.1}; GN ORFNames=NGO_1450 {ECO:0000313|EMBL:AAW90092.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90092.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90092.1; -; Genomic_DNA. DR RefSeq; WP_003689327.1; NC_002946.2. DR RefSeq; YP_208504.1; NC_002946.2. DR ProteinModelPortal; Q5F6U5; -. DR EnsemblBacteria; AAW90092; AAW90092; NGO_1450. DR GeneID; 3281700; -. DR KEGG; ngo:NGO1450; -. DR PATRIC; 20336317; VBINeiGon24812_1707. DR HOGENOM; HOG000263985; -. DR OMA; PYCGTEY; -. DR OrthoDB; EOG6TTVTH; -. DR BioCyc; NGON242231:GI2G-1357-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 19 55 zf-CHCC. {ECO:0000259|Pfam:PF10276}. SQ SEQUENCE 67 AA; 7535 MW; B082B4D9CA3BCD3C CRC64; MDNLNPQEIS VLPENLPLYC SGPDNEQWNG HPRVFLPLGE GESGSVACPY CGTRYRLDGK MPHHYYA // ID Q5F5P5_NEIG1 Unreviewed; 65 AA. AC Q5F5P5; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90492.1}; GN ORFNames=NGO_1872 {ECO:0000313|EMBL:AAW90492.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90492.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90492.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90492; AAW90492; NGO_1872. DR PATRIC; 20337438; VBINeiGon24812_2250. DR HOGENOM; HOG000071365; -. DR OMA; IEQGYNT; -. DR OrthoDB; EOG6MWNH4; -. DR BioCyc; NGON242231:GI2G-1776-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 65 AA; 7478 MW; FF9B9BF231991ED2 CRC64; MKNRRRIRRR KEKIMALLNI EQGYNTTLHN RSPYLINFGL SCLIGLEKAA AAPRDVPCDN KCSAF // ID Q5F7Q0_NEIG1 Unreviewed; 66 AA. AC Q5F7Q0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89787.1}; GN ORFNames=NGO_1120 {ECO:0000313|EMBL:AAW89787.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89787.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89787.1; -; Genomic_DNA. DR RefSeq; WP_003692842.1; NC_002946.2. DR RefSeq; YP_208199.1; NC_002946.2. DR EnsemblBacteria; AAW89787; AAW89787; NGO_1120. DR GeneID; 3282167; -. DR KEGG; ngo:NGO1120; -. DR PATRIC; 20335494; VBINeiGon24812_1313. DR HOGENOM; HOG000071222; -. DR OMA; SINHTAF; -. DR OrthoDB; EOG6NWC07; -. DR BioCyc; NGON242231:GI2G-1032-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 66 AA; 7482 MW; 53349638CB293404 CRC64; MNELISRINR FGARAKDEQS LLLKVGEICR DAAATWTTRK SESINHTAFT FTVKKDGLKE KVMIVL // ID Q5FAJ9_NEIG1 Unreviewed; 94 AA. AC Q5FAJ9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW88784.1}; GN ORFNames=NGO_0015 {ECO:0000313|EMBL:AAW88784.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88784.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88784.1; -; Genomic_DNA. DR EnsemblBacteria; AAW88784; AAW88784; NGO_0015. DR HOGENOM; HOG000071337; -. DR OrthoDB; EOG6P33FR; -. DR BioCyc; NGON242231:GI2G-11-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 94 AA; 10698 MW; 4AB5F517C7844E60 CRC64; MRFGFSFRYA PTAKTVKNRK TPKVVTDSLP FVTAFVTNFL SFSYFYSELN LNRYGVASPC RTICTVCGSP PCPDLNLIHY ISYTYLSNFS PVTR // ID Q5F9K2_NEIG1 Unreviewed; 188 AA. AC Q5F9K2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89135.1}; GN ORFNames=NGO_0391 {ECO:0000313|EMBL:AAW89135.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89135.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89135.1; -; Genomic_DNA. DR RefSeq; WP_003690844.1; NC_002946.2. DR RefSeq; YP_207547.1; NC_002946.2. DR EnsemblBacteria; AAW89135; AAW89135; NGO_0391. DR GeneID; 3283018; -. DR KEGG; ngo:NGO0391; -. DR PATRIC; 20333789; VBINeiGon24812_0472. DR HOGENOM; HOG000218866; -. DR OMA; VERFCHE; -. DR OrthoDB; EOG6BS8R4; -. DR BioCyc; NGON242231:GI2G-370-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT COILED 157 184 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 188 AA; 20135 MW; 12B208B5E44D5A26 CRC64; MSALLPIINR LILQSPDSRS ELTSFAGKTL TLNIAGLKLA GRITEDGLLS AGNGFADTEI TFRNSAIRKI LQGGEPGAGD IRLEGDLILG IAVLSLLGSL RSRASDELAR IFGTQAGIGS RATDIGHGIK QIGRNIAEQI GGFSREPESA NTGNEALADC LDEISRLRDG VERLNERLDR LERDIWID // ID Q5F7Z6_NEIG1 Unreviewed; 96 AA. AC Q5F7Z6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89691.1}; GN ORFNames=NGO_1008 {ECO:0000313|EMBL:AAW89691.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89691.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89691.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89691; AAW89691; NGO_1008. DR PATRIC; 20335224; VBINeiGon24812_1180. DR HOGENOM; HOG000071270; -. DR OMA; LNHAVRY; -. DR OrthoDB; EOG6Z9B56; -. DR BioCyc; NGON242231:GI2G-934-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 10683 MW; 4177D8AF62050171 CRC64; MKRQTKTATV LTALARTACT STTVPSDTPI KTVAVAEIPP VPSGLLVEYE RPERPAGGSP EQLLNHAVRY GGYYRKLEIQ IEGWQNWHTK GRLKHD // ID Q5F8C9_NEIG1 Unreviewed; 45 AA. AC Q5F8C9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89558.1}; GN ORFNames=NGO_0854 {ECO:0000313|EMBL:AAW89558.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89558.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89558.1; -; Genomic_DNA. DR RefSeq; WP_003688547.1; NC_002946.2. DR RefSeq; YP_207970.1; NC_002946.2. DR EnsemblBacteria; AAW89558; AAW89558; NGO_0854. DR GeneID; 3282249; -. DR KEGG; ngo:NGO0854; -. DR PATRIC; 20334878; VBINeiGon24812_1009. DR HOGENOM; HOG000027804; -. DR OrthoDB; EOG6NKR64; -. DR BioCyc; NGON242231:GI2G-800-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 45 AA; 5339 MW; 514891FD60BDFC1A CRC64; MNIFVTDFSY WFMSLLTLSY IPSVHSSDDD IDFGKRIMTV TFLHF // ID Q5F631_NEIG1 Unreviewed; 298 AA. AC Q5F631; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 64. DE SubName: Full=Geranyl transferase {ECO:0000313|EMBL:AAW90356.1}; GN ORFNames=NGO_1735 {ECO:0000313|EMBL:AAW90356.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90356.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90356.1; -; Genomic_DNA. DR RefSeq; WP_003697633.1; NC_002946.2. DR RefSeq; YP_208768.1; NC_002946.2. DR ProteinModelPortal; Q5F631; -. DR EnsemblBacteria; AAW90356; AAW90356; NGO_1735. DR GeneID; 3281265; -. DR KEGG; ngo:NGO1735; -. DR PATRIC; 20337068; VBINeiGon24812_2074. DR HOGENOM; HOG000009101; -. DR KO; K00795; -. DR OMA; LQMEREN; -. DR OrthoDB; EOG6TN43W; -. DR BioCyc; NGON242231:GI2G-1631-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU004466, KW ECO:0000313|EMBL:AAW90356.1}. SQ SEQUENCE 298 AA; 31721 MW; 80600BBA979210E2 CRC64; MNPTNDLKAW QQRAQAQTEL LLERFLPSGN EIPHTLHEAM RYAALDGGKR LRPMLVLAAS ELGGAMADAV GQAMAAIEMI HVYSLVHDDM PAMDNDSLRR GKPTCHIKYG EATALLTGDA LQTQAFDVLS RPTELPAARQ LAMLSVLAKA GGSAGMAGGQ AIDLANVGKQ MVQADLERMH SLKTGALIRA AVLLGATACP DLSDAELAVL DAYAAKLGLA FQVIDDVLDC EADTATLGKT AGKDADNDKP TYVKLMGLEA ARSYAHKLVA EAVALLEPFG DKALRLRQLA EFAVARKY // ID Q5F6S9_NEIG1 Unreviewed; 277 AA. AC Q5F6S9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 67. DE SubName: Full=Phosphoserine phosphatase {ECO:0000313|EMBL:AAW90108.1}; GN ORFNames=NGO_1468 {ECO:0000313|EMBL:AAW90108.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90108.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90108.1; -; Genomic_DNA. DR RefSeq; WP_003693646.1; NC_002946.2. DR RefSeq; YP_208520.1; NC_002946.2. DR ProteinModelPortal; Q5F6S9; -. DR EnsemblBacteria; AAW90108; AAW90108; NGO_1468. DR GeneID; 3281663; -. DR KEGG; ngo:NGO1468; -. DR PATRIC; 20336369; VBINeiGon24812_1733. DR HOGENOM; HOG000231114; -. DR KO; K01079; -. DR OMA; RVAFCAK; -. DR OrthoDB; EOG6ZPT4H; -. DR BioCyc; NGON242231:GI2G-1373-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:InterPro. 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 277 AA; 30485 MW; B18E9AE775C5E751 CRC64; MPQALVLQFP SAEALPSDFP SRLPEPDYAD EKRMRFIVEE GFSLSEKDAA LLDSRQIDHA VLPNMAFGEL GLIVSDMDST LITIECIDEI AAGVGLKGKV AEITERAMRG ELDFGQSLRS RVALLAGLDE QILADIYENV LKLSPGAEFL LDECKRHNVK FLLVSGGFTF FTERLQQRLG FEYQHANILE IENGRLTGRL KGRIIDAQAK ADLLREYRSR LGLQPHQVLA MGDGANDIPI LKEAGIGVAY RAKPKARAAA DACINFGGLE RVRGLFG // ID Q5FA53_NEIG1 Unreviewed; 117 AA. AC Q5FA53; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW88934.1}; GN ORFNames=NGO_0179 {ECO:0000313|EMBL:AAW88934.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88934.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88934.1; -; Genomic_DNA. DR RefSeq; WP_003687481.1; NC_002946.2. DR RefSeq; YP_207346.1; NC_002946.2. DR EnsemblBacteria; AAW88934; AAW88934; NGO_0179. DR GeneID; 3283046; -. DR KEGG; ngo:NGO0179; -. DR PATRIC; 20333285; VBINeiGon24812_0225. DR HOGENOM; HOG000259406; -. DR OMA; EWFISPL; -. DR OrthoDB; EOG6HF642; -. DR BioCyc; NGON242231:GI2G-164-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 13256 MW; 32FEC787BF3A709D CRC64; MNRQTAYFLA SFSLIALIAL SLSWELWIAP LRPGGSWLAL KALPLCLPLS GILKKKIYTY QYSSMLVLIY FAEAVMRLFN AYPAEKICAA LSAVFSIIFF ISCLSFVKQY KETNNVR // ID Q5F5I4_NEIG1 Unreviewed; 171 AA. AC Q5F5I4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90553.1}; GN ORFNames=NGO_1941 {ECO:0000313|EMBL:AAW90553.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90553.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90553.1; -; Genomic_DNA. DR RefSeq; WP_003688109.1; NC_002946.2. DR RefSeq; YP_208965.1; NC_002946.2. DR EnsemblBacteria; AAW90553; AAW90553; NGO_1941. DR GeneID; 3282679; -. DR KEGG; ngo:NGO1941; -. DR PATRIC; 20337627; VBINeiGon24812_2340. DR HOGENOM; HOG000071362; -. DR OMA; THKNENA; -. DR OrthoDB; EOG615VJ7; -. DR BioCyc; NGON242231:GI2G-1843-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 171 AA; 20141 MW; C06387F13AA51E22 CRC64; MKTFLHTQRK NFLDGISLHD CYRTAIKVEG RNVCFDFEDG FVVLDNNPNN QAGKHLKTDF SRVVLTHENR NAEDDYLVDI FEDIVFLGKR LFTVRKFLDF SELLEMINAQ GYFLEFLYLY ECIGVKTSDY FLEAVLVTGR SRECKKCFIK IMRASSFVYQ WNNLRLNSEI V // ID Q5F8B9_NEIG1 Unreviewed; 129 AA. AC Q5F8B9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 56. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAW89568.1}; GN ORFNames=NGO_0867 {ECO:0000313|EMBL:AAW89568.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89568.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89568.1; -; Genomic_DNA. DR RefSeq; WP_003688532.1; NC_002946.2. DR RefSeq; YP_207980.1; NC_002946.2. DR ProteinModelPortal; Q5F8B9; -. DR EnsemblBacteria; AAW89568; AAW89568; NGO_0867. DR GeneID; 3281889; -. DR KEGG; ngo:NGO0867; -. DR PATRIC; 20334906; VBINeiGon24812_1023. DR HOGENOM; HOG000025367; -. DR OMA; RVMREIN; -. DR OrthoDB; EOG6FV87D; -. DR BioCyc; NGON242231:GI2G-810-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 61 HTH cro/C1-type DNA-binding. FT {ECO:0000259|PROSITE:PS50943}. SQ SEQUENCE 129 AA; 15056 MW; 156870551982AB88 CRC64; MEVHDKIRTL REVNQWTQEE MAEKLEMSVN GYSKIERGKS GINLDKLRQI AQIFNIDVVE LLAEQNRSFF FSIGDNTNNH HNIIGSDEML VFENEKLRSL LDAKDELIRQ KDSEIAVLKK LVILLEEKK // ID Q5F8H4_NEIG1 Unreviewed; 487 AA. AC Q5F8H4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 85. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928}; DE EC=1.1.1.205 {ECO:0000256|RuleBase:RU003928}; GN ORFNames=NGO_0799 {ECO:0000313|EMBL:AAW89513.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89513.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89513.1; -; Genomic_DNA. DR RefSeq; WP_003697062.1; NC_002946.2. DR RefSeq; YP_207925.1; NC_002946.2. DR ProteinModelPortal; Q5F8H4; -. DR SMR; Q5F8H4; 2-486. DR EnsemblBacteria; AAW89513; AAW89513; NGO_0799. DR GeneID; 3282011; -. DR KEGG; ngo:NGO0799; -. DR PATRIC; 20334746; VBINeiGon24812_0945. DR HOGENOM; HOG000165755; -. DR KO; K00088; -. DR OMA; SSMGYCG; -. DR OrthoDB; EOG6GTZPV; -. DR BioCyc; NGON242231:GI2G-753-MONOMER; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000535; 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:UP000000535}; 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 Potassium {ECO:0000256|PIRSR:PIRSR000130-4, KW ECO:0000256|RuleBase:RU003928}; KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. 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; 52439 MW; 400F005FF119B8C2 CRC64; MRIVEKAYTF DDVLLVPAHS TVLPRDVKLQ TKLTREITLN LPLLSAAMDT VTEARLAISM AQEGGIGIIH KNMPPEMQAR AVSKVKRHES GVVKDPVTVA PTTLIREVLE MRAQRKRKMS GLPVVENGKV VGIVTNRDLR FENRVDLPVS AIMTPRERLV TVPEGTSIDE ARELMHTYKV ERVLVLNEKD ELKGLITIKD ILKTTEFPNA NKDSEGRLRV GAAVGTGGDT DERVKALVEA GADVIVVDTA HGHSQGVIDR VRWVKETYPH IQVIGGNIAT AKAALDLVTV GADAVKVGIG PGSICTTRIV AGVGVPQLTA IHNVAEALKG TGVPLIADGG IRFSGDIAKA LAAGAYSVML GGMFAGTEEA PGEIELYQGR SYKSYRGMGS LGAMSQGSAD RYFQDKTDST DKYVPEGIEG RVPYKGPIVN IIHQLTGGLR SSMGYLGCAN IAEMHEKAEF VEITSAGMSE SHVHDVQITK EAPNYHR // ID Q5F6A2_NEIG1 Unreviewed; 92 AA. AC Q5F6A2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90285.2}; GN ORFNames=NGO_1658 {ECO:0000313|EMBL:AAW90285.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90285.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90285.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F6A2; -. DR EnsemblBacteria; AAW90285; AAW90285; NGO_1658. DR PATRIC; 20336862; VBINeiGon24812_1976. DR HOGENOM; HOG000118146; -. DR OMA; MWYMISS; -. DR OrthoDB; EOG6423NJ; -. DR BioCyc; NGON242231:GI2G-1554-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 1 88 YCII. {ECO:0000259|Pfam:PF03795}. SQ SEQUENCE 92 AA; 10177 MW; 9CAD20DE884CE551 CRC64; MLLATDGEDV HEARMAARPE HFKRLETLKS EGRLLTAGPN LLPDNPERVS GSLIVAQFES LDAAQAWAED DPYVHAGVYS EVLIKPFKAV FK // ID Q5F822_NEIG1 Unreviewed; 156 AA. AC Q5F822; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89665.1}; GN ORFNames=NGO_0979 {ECO:0000313|EMBL:AAW89665.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89665.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89665.1; -; Genomic_DNA. DR RefSeq; WP_003688307.1; NC_002946.2. DR RefSeq; YP_208077.1; NC_002946.2. DR DNASU; 3282868; -. DR EnsemblBacteria; AAW89665; AAW89665; NGO_0979. DR GeneID; 3282868; -. DR KEGG; ngo:NGO0979; -. DR PATRIC; 20335158; VBINeiGon24812_1148. DR HOGENOM; HOG000262950; -. DR OMA; TNPFLHM; -. DR OrthoDB; EOG6S52MS; -. DR BioCyc; NGON242231:GI2G-907-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR014993; DUF1841. DR Pfam; PF08897; DUF1841; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 156 AA; 18218 MW; BA58B3BCB1266FEA CRC64; MYDVNTHDVR RFFARVWQQR LNPLQLGALE QKALRIVEAH PEYHRYLERI EDHLDTDWLP ENGESNPFLH MSLHLSVQEQ AGIDQPHGIR AIHDTLCAKR GWPEAEHEMM EALAETLWTA QRYGTGLDVN FYMTRLRKLI GLGAEDQARL NPHEIA // ID Q5F5J1_NEIG1 Unreviewed; 211 AA. AC Q5F5J1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 59. DE SubName: Full=Amidase {ECO:0000313|EMBL:AAW90546.1}; GN ORFNames=NGO_1933 {ECO:0000313|EMBL:AAW90546.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90546.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90546.1; -; Genomic_DNA. DR RefSeq; WP_003705173.1; NC_002946.2. DR RefSeq; YP_208958.1; NC_002946.2. DR ProteinModelPortal; Q5F5J1; -. DR EnsemblBacteria; AAW90546; AAW90546; NGO_1933. DR GeneID; 3282686; -. DR KEGG; ngo:NGO1933; -. DR PATRIC; 20337606; VBINeiGon24812_2330. DR HOGENOM; HOG000078666; -. DR KO; K08281; -. DR OMA; GACYHDL; -. DR OrthoDB; EOG615VP6; -. DR BioCyc; NGON242231:GI2G-1836-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 5 201 Isochorismatase. FT {ECO:0000259|Pfam:PF00857}. SQ SEQUENCE 211 AA; 23439 MW; D1EFDE053D35A3EC CRC64; MIVSIDVDAQ KTFTPLCPDE LPVNEGHLIV EELNAQAALA DLRVMTKDAH HMAAKWLVDN PVDMLKPTGF SDADLTWVAH AMVGTRGYEL LDGLPSVKEY DYCVWKGVDP ELHPYGACFH DIEEKLSTGL IEWLRCQNTN MVIVGGLATD YCVKTTVLQL LKGGRWQVIV NEAACRGIAP DTIEAAWQEM RSSGAIILKN AEKIKKYINN Q // ID Q5F9V6_NEIG1 Unreviewed; 159 AA. AC Q5F9V6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. 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 ORFNames=NGO_0282 {ECO:0000313|EMBL:AAW89031.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89031.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89031.1; -; Genomic_DNA. DR RefSeq; WP_003687653.1; NC_002946.2. DR RefSeq; YP_207443.1; NC_002946.2. DR ProteinModelPortal; Q5F9V6; -. DR SMR; Q5F9V6; 30-159. DR DNASU; 3281623; -. DR EnsemblBacteria; AAW89031; AAW89031; NGO_0282. DR GeneID; 3281623; -. DR KEGG; ngo:NGO0282; -. DR PATRIC; 20333539; VBINeiGon24812_0350. DR HOGENOM; HOG000218847; -. DR KO; K03643; -. DR OMA; ETLWAEM; -. DR OrthoDB; EOG63RGRX; -. DR BioCyc; NGON242231:GI2G-263-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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_5005078750. 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; 17651 MW; 65C910F958C3897E CRC64; MNKIFLTAAA LVLGACGFHL KGADGISPPL TYRSWHIEGG QALQFPLETA LYQASGRVDD AAGAQMTLRI DSVSQNKETY TVTRAAVINE YLLILTVEAQ VLKRGEPVGK PMTVSVRRIL DYADNEILGK QEEEETLWAE MRQDVAEQIV RRLTFLKAE // ID Q5F6U6_NEIG1 Unreviewed; 528 AA. AC Q5F6U6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 55. DE SubName: Full=Lactate permease {ECO:0000313|EMBL:AAW90091.1}; GN ORFNames=NGO_1449 {ECO:0000313|EMBL:AAW90091.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90091.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90091.1; -; Genomic_DNA. DR RefSeq; WP_003689325.1; NC_002946.2. DR RefSeq; YP_208503.1; NC_002946.2. DR EnsemblBacteria; AAW90091; AAW90091; NGO_1449. DR GeneID; 3281635; -. DR KEGG; ngo:NGO1449; -. DR PATRIC; 20336315; VBINeiGon24812_1706. DR HOGENOM; HOG000278977; -. DR KO; K03303; -. DR OMA; WPARRAM; -. DR OrthoDB; EOG6Q8J3Z; -. DR BioCyc; NGON242231:GI2G-1356-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 56721 MW; BF7C497A66F76EF1 CRC64; MALFLSIFPI VLLIWLMVKK NSMPSYVALP ITAVLIYAIK LFYFGDAGML LNATAASGLV KTLTPITVIF GAIMFNRMME TTGCIDVIRK WLATISPNPV AQLMIIGWAF AFMIEGASGF GTPAAIAAPI LMSLGFNPLK VAIFTLVMNS VPVSFGAVGT PTWFGFAPLN LSAEDILAIG RQTGVMHFFA GFVIPVIGLG FIVPWSEIRK NLGFVAIAVF SCTIPYAALA MVNEEFPSLV AGAIGLMVSV FAANQGWGLS KDHAKDPNAE KVPFAQVAKA LAPLGMLIGM LVVTRIKQLG IKGILTSKEE WFSFQLPFDL SKITVSDSLT ITFGNIFGQD VSASYQTLYV PAWIPFVLTV WICILLYKTK FKDAWTIYAV TFNQTKKPLL ALMGALIMVQ LMLVGGDNSM VKIIGKEFAA MAGEHWVYFS PYLGAIGAFF SGSNTVSNLT FGPIQQQIAL DTGLSVTLIL ALQSVGGAMG NMVCLNNIIA VCTVLDVKNS EGAIIKKTVI PMAIYGVIAV VAAMIFFL // ID Q5F9I6_NEIG1 Unreviewed; 763 AA. AC Q5F9I6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 79. DE SubName: Full=Clp protease ClpX {ECO:0000313|EMBL:AAW89151.1}; GN Name=clpA {ECO:0000313|EMBL:AAW89151.1}; GN ORFNames=NGO_0408 {ECO:0000313|EMBL:AAW89151.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89151.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89151.1; -; Genomic_DNA. DR RefSeq; WP_003701038.1; NC_002946.2. DR RefSeq; YP_207563.1; NC_002946.2. DR ProteinModelPortal; Q5F9I6; -. DR SMR; Q5F9I6; 173-364. DR EnsemblBacteria; AAW89151; AAW89151; NGO_0408. DR GeneID; 3281945; -. DR KEGG; ngo:NGO0408; -. DR PATRIC; 20333827; VBINeiGon24812_0491. DR HOGENOM; HOG000218210; -. DR KO; K03694; -. DR OMA; RTHLKNF; -. DR OrthoDB; EOG65F8SM; -. DR BioCyc; NGON242231:GI2G-386-MONOMER; -. DR Proteomes; UP000000535; 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}; KW Chaperone {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00480820}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW89151.1}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU004433, KW ECO:0000256|SAAS:SAAS00463698}; KW Protease {ECO:0000313|EMBL:AAW89151.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repeat {ECO:0000256|SAAS:SAAS00417491}. FT DOMAIN 211 355 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 492 641 AAA. {ECO:0000259|SMART:SM00382}. FT DOMAIN 658 749 ClpB_D2-small. FT {ECO:0000259|SMART:SM01086}. SQ SEQUENCE 763 AA; 84274 MW; 984ACB4BF2B45C5F CRC64; MLAPELEQIL QQLYREARKA HYEFISLEHL LLVLIEEDAA VPNVLKLCGA DLKAVSEQLA ASVAENTPLI PDHLLDTVET RPTLGFQRVI QRAMVHTQSA GKGLAEPLDV LVALMSETDS HAVYFLGLQS VTRFEVLRCI AHGSPDEDED DGNYFSDGMD DDNENRTKPG KNPLSAYTVN LNAEVKAGRI DPLIGRKHEM ERLVQILCRR RKNNPLLVGE AGVGKTALAD GLAHQIVNDD IPDALKEAEV YALDMGSLLA GTKYRGDFEA RVKSVLKQLE KIPHAILFID EIHTIIGAGS TGGGTMDASN LLKPALAKGS LRCIGATTYD EYRTIFDKDH ALSRRFQKID VVEPTVAETV QILRGLKPMF EAFHQVRYTQ GALEAAAELS ARYINERFLP DKAIDVMDEA GAAQRILPKS KQKKVIGKAQ IETVIAKVAR IPEKTVSHDD KQVLQFLGRD LNNMVYGQED AIDALVSAVK MSRSGLGLPD KPIGSFLFSG PTGVGKTEVA KQLAYSMGVP LQRFDMSEYM ERHAVSRLIG APPGYVGFEQ GGLLTEAVNK QPHCVLLLDE IEKAHPDIFN VLLQVMDAGK LTDNNGKSAD FRNVILIMTT NAGAESLSRP SLGFTAKRER GDEMQAINKL FTPEFRNRLD AIIPFAPLSE PIIVKVVDKF LLQLEHRLLD KKVEAEFTPA LRKYLAEKGF DPQMGARPMH RLIQEKIRKP LADELLFGKL ADGGFVRIDW DAAKEEAVLK FKKSKVKIKT ASA // ID Q5F5Z1_NEIG1 Unreviewed; 52 AA. AC Q5F5Z1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90396.1}; GN ORFNames=NGO_1777 {ECO:0000313|EMBL:AAW90396.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90396.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90396.1; -; Genomic_DNA. DR EnsemblBacteria; AAW90396; AAW90396; NGO_1777. DR PATRIC; 20337196; VBINeiGon24812_2134. DR HOGENOM; HOG000027822; -. DR OrthoDB; EOG62ZJ48; -. DR BioCyc; NGON242231:GI2G-1675-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 52 AA; 5853 MW; 4524BBE6FDD4BEE1 CRC64; MFSSFRRHFS FLTAILPGCR HFQFYSGLNL NRYGVASPCR TICTVCGFAA LS // ID Q5F6F2_NEIG1 Unreviewed; 193 AA. AC Q5F6F2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Lipopolysaccharide-assembly, LptC-related family protein {ECO:0000313|EMBL:AAW90235.1}; GN ORFNames=NGO_1607 {ECO:0000313|EMBL:AAW90235.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90235.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90235.1; -; Genomic_DNA. DR RefSeq; WP_003689544.1; NC_002946.2. DR RefSeq; YP_208647.1; NC_002946.2. DR EnsemblBacteria; AAW90235; AAW90235; NGO_1607. DR GeneID; 3281514; -. DR KEGG; ngo:NGO1607; -. DR PATRIC; 20336752; VBINeiGon24812_1921. DR HOGENOM; HOG000219112; -. DR KO; K11719; -. DR OMA; PENSDIH; -. DR OrthoDB; EOG680X0Z; -. DR BioCyc; NGON242231:GI2G-1504-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 193 AA; 21794 MW; D58914D489AD0CEB CRC64; MKVRWRYGIA FPLILAVALG SLSAWLGRIS EVEIEEVRLN PDEPQYTMDG LDGRRFDEQG YLKEHLSAKG AKQFPENSDI HFDSPHLVFF QEGRLLYEVG SDEAVYHTEN KQVLFKNNVV LTKTADGRRQ AGKVETEKLH VDTESQYAQT DTPVSFQYGA SHGQAGGMTY NHKTGMLNFS SKVKAAIYDT KDM // ID Q5F8Q1_NEIG1 Unreviewed; 231 AA. AC Q5F8Q1; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=6-phosphogluconolactonase {ECO:0000313|EMBL:AAW89436.1}; GN ORFNames=NGO_0716 {ECO:0000313|EMBL:AAW89436.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89436.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000213|PDB:3LHI} RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS). RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of Putative 6-phosphogluconolactonase(YP_207848.1) RT from Neisseria gonorrhoeae FA 1090 at 1.33 A resolution."; RL Submitted (JAN-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; AE004969; AAW89436.1; -; Genomic_DNA. DR RefSeq; WP_003688731.1; NC_002946.2. DR RefSeq; YP_207848.1; NC_002946.2. DR PDB; 3LHI; X-ray; 1.33 A; A=1-231. DR PDBsum; 3LHI; -. DR ProteinModelPortal; Q5F8Q1; -. DR EnsemblBacteria; AAW89436; AAW89436; NGO_0716. DR GeneID; 3283072; -. DR KEGG; ngo:NGO0716; -. DR PATRIC; 20334560; VBINeiGon24812_0852. DR HOGENOM; HOG000256284; -. DR KO; K01057; -. DR OMA; PEANIHG; -. DR OrthoDB; EOG63FW46; -. DR BioCyc; NGON242231:GI2G-676-MONOMER; -. DR EvolutionaryTrace; Q5F8Q1; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3LHI}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 9 220 Glucosamine_iso. FT {ECO:0000259|Pfam:PF01182}. SQ SEQUENCE 231 AA; 24878 MW; 877023E920A7A7D5 CRC64; MFVWHEYENA AEAAQSLADA VADALQGALD EKGGAVLAVS GGRSPIAFFN ALSQKDLDWK NVGITLADER IVPTNHADSN TGLVREYLLK NKAAAAVWIP MVEDGKTETE LHPDAVVDYA LKHYKQPDVL ILGMGNDGHT ASIFPKAPQF QTAIDGSAGV ALVHTTPVTA PHERISMTLD AIAHTGHVFL AIQGEEKKAV FDQAAQGENR EYPISLVLNH QGVNCHVFYA E // ID Q5F738_NEIG1 Unreviewed; 249 AA. AC Q5F738; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89999.1}; GN ORFNames=NGO_1349 {ECO:0000313|EMBL:AAW89999.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89999.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89999.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89999; AAW89999; NGO_1349. DR PATRIC; 20336071; VBINeiGon24812_1585. DR HOGENOM; HOG000282181; -. DR OMA; EGDVSPT; -. DR OrthoDB; EOG6J1DCW; -. DR BioCyc; NGON242231:GI2G-1263-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR014030; Ketoacyl_synth_N. DR Pfam; PF13723; Ketoacyl-synt_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 227 Ketoacyl_synth_N. FT {ECO:0000259|Pfam:PF13723}. SQ SEQUENCE 249 AA; 27740 MW; 57064919F554B72B CRC64; MRDMAQWRQW AECPDFADGL PDVRRELPFL PAMRRRRLSK AARLVCDAAW DIASAHPGSP VVYASHDGEM ARSFDLWLEL LKSHTVSPTS FGLSVHNATA GQWSILRRDM SEQTALAVCA DGVETALAEA ASLLEEGCGS VLVLAADDPL PEGYAVSATR APFAYALAMV LTKGTRYSLT LSASDDMPSE AGMLPEAYWS GLEWVRFLLN GSRECRRVYR NREWLWQPAS CRLKISAMSA PSTTWYRRY // ID Q5F5I3_NEIG1 Unreviewed; 146 AA. AC Q5F5I3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90554.2}; GN ORFNames=NGO_1942 {ECO:0000313|EMBL:AAW90554.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90554.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90554.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90554; AAW90554; NGO_1942. DR PATRIC; 20337629; VBINeiGon24812_2341. DR HOGENOM; HOG000218685; -. DR OMA; MIKETLM; -. DR OrthoDB; EOG6C0178; -. DR BioCyc; NGON242231:GI2G-1844-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 146 AA; 16639 MW; F101580193DD3055 CRC64; MIKETLMRPI FLSFVLLPIL ITACSTPDKS ARWENIGTIS NGNIHTYINK DSVRKNGNLM IFQDKKVVTN LKQERFANTP AYKTAIAEWE IHCNNKTYRL SSLQLFDTKN TEISTQNYTA SSLRPMSILS GTLTEKQYET VCGKKL // ID Q5FAD6_NEIG1 Unreviewed; 150 AA. AC Q5FAD6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 69. DE RecName: Full=Transcriptional repressor NrdR {ECO:0000256|HAMAP-Rule:MF_00440}; GN Name=nrdR {ECO:0000256|HAMAP-Rule:MF_00440}; GN ORFNames=NGO_0090 {ECO:0000313|EMBL:AAW88851.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88851.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Negatively regulates transcription of bacterial CC ribonucleotide reductase nrd genes and operons by binding to NrdR- CC boxes. {ECO:0000256|HAMAP-Rule:MF_00440}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00440}; CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00440}; CC -!- SIMILARITY: Belongs to the NrdR family. {ECO:0000256|HAMAP- CC Rule:MF_00440}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000256|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; AE004969; AAW88851.1; -; Genomic_DNA. DR RefSeq; WP_003704920.1; NC_002946.2. DR RefSeq; YP_207263.1; NC_002946.2. DR EnsemblBacteria; AAW88851; AAW88851; NGO_0090. DR GeneID; 3282251; -. DR KEGG; ngo:NGO0090; -. DR PATRIC; 20333067; VBINeiGon24812_0117. DR HOGENOM; HOG000097653; -. DR KO; K07738; -. DR OMA; RFTTYET; -. DR OrthoDB; EOG6XM7J6; -. DR BioCyc; NGON242231:GI2G-80-MONOMER; -. DR Proteomes; UP000000535; 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 PROSITE; PS51161; ATP_CONE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00440, KW ECO:0000256|SAAS:SAAS00511196}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00440}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00440}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00440, KW ECO:0000256|SAAS:SAAS00511196}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Repressor {ECO:0000256|HAMAP-Rule:MF_00440}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00440}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00440}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00440}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00440}. FT DOMAIN 49 139 ATP-cone. {ECO:0000256|HAMAP- FT Rule:MF_00440, FT ECO:0000259|PROSITE:PS51161}. FT ZN_FING 3 34 {ECO:0000256|HAMAP-Rule:MF_00440}. SQ SEQUENCE 150 AA; 16953 MW; 6E76EFB7F717FA7E CRC64; MKCPFCAHPD TRVVDSRLME ERNAVRRRRQ CPGCGKRFGT LETAELKMPA VIGPDKKRSP FNAQRLRNDL TAAARKSALT PEQIDETVRL TEHRLYTSGQ RDISSSELVE IVLEELFGQN TEAAVRFAAL HKRFDSPEHF ASWLAQGGKT // ID Q5F590_NEIG1 Unreviewed; 313 AA. AC Q5F590; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 79. DE SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:AAW90647.1}; GN ORFNames=NGO_2039 {ECO:0000313|EMBL:AAW90647.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90647.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90647.1; -; Genomic_DNA. DR RefSeq; WP_003686969.1; NC_002946.2. DR RefSeq; YP_209059.1; NC_002946.2. DR ProteinModelPortal; Q5F590; -. DR EnsemblBacteria; AAW90647; AAW90647; NGO_2039. DR GeneID; 3282708; -. DR KEGG; ngo:NGO2039; -. DR PATRIC; 20337861; VBINeiGon24812_2454. DR OMA; NWEHING; -. DR OrthoDB; EOG6T7N3V; -. DR BioCyc; NGON242231:GI2G-1940-MONOMER; -. DR Proteomes; UP000000535; 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:AAW90647.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU363033, KW ECO:0000313|EMBL:AAW90647.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 2 232 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 313 AA; 34109 MW; D407F2BA1031E624 CRC64; MLELNGLCKC FGGKTVADNI CLTVGRGKIL AVLGRSGCGK STLLNMIAGI VRPDGGEIRL NGENITCMPP EKRRISLMFQ DYALFPHMSA LENTAFGLKM QKMPKAEAER LALSALAEVG LENEAHRKPE KLSGGEKQRL ALARALVVRP SLLLLDESFS SLDTHLRDRL RRMTAERIRK GGIPAVLVTH SPEEACTAAD EIAVMHEGKI LQCGTPETLI QTPAGVQVAR LMGLPNTDDD RHIPQNAVCL DNHGTECRLL SLVRLPDSLR LSAVHPEHGE LTLNLTVGQH TDGISGNGTV RIRVDEGRIV RFR // ID Q5F5M4_NEIG1 Unreviewed; 346 AA. AC Q5F5M4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|RuleBase:RU004473}; DE EC=4.2.1.46 {ECO:0000256|RuleBase:RU004473}; GN ORFNames=NGO_1897 {ECO:0000313|EMBL:AAW90513.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90513.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy- CC alpha-D-glucose + H(2)O. {ECO:0000256|RuleBase:RU004473}. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|RuleBase:RU004473}; CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. dTDP-glucose dehydratase subfamily. CC {ECO:0000256|RuleBase:RU004473}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90513.1; -; Genomic_DNA. DR RefSeq; WP_003690169.1; NC_002946.2. DR RefSeq; YP_208925.1; NC_002946.2. DR ProteinModelPortal; Q5F5M4; -. DR SMR; Q5F5M4; 7-341. DR EnsemblBacteria; AAW90513; AAW90513; NGO_1897. DR GeneID; 3282303; -. DR KEGG; ngo:NGO1897; -. DR PATRIC; 20337498; VBINeiGon24812_2280. DR HOGENOM; HOG000168006; -. DR KO; K01710; -. DR OMA; PDEQEGQ; -. DR OrthoDB; EOG6PZXCX; -. DR BioCyc; NGON242231:GI2G-1797-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro. 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 {ECO:0000313|Proteomes:UP000000535}; KW Lyase {ECO:0000256|RuleBase:RU004473}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 10 332 NAD(P)-bd_dom. FT {ECO:0000259|Pfam:PF16363}. SQ SEQUENCE 346 AA; 38785 MW; 8678F0154AEE41CC CRC64; MQTAGKKNIL VTGGAGFIGS AVVRHIIQNT RDSVVNLDKL TYAGNLESLT DIADNPRYAF EQVDICDRAE LDRVFAQYRP DAVMHLAAES HVDRAIGSAG EFIRTNIVGT FDLLEAARAY WQQMPSEKRE AFRFHHISTD EVYGDLHGTD DLFTETTPYA PSSPYSASKA AADHLVRAWQ RTYRLPSIVS NCSNNYGPRQ FPEKLIPLMI LNALSGKPLP VYGDGAQIRD WLFVEDHARA LYQVVTEGVV GETYNIGGHN EKTNLEVIKT ICALLEELAP EKPAGVARYE DLITFVQDRP GHDARYAVDA AKIRRDLGWL PLETFESGLR KTVQWYLDNK TRRQNA // ID Q5F6K9_NEIG1 Unreviewed; 582 AA. AC Q5F6K9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 60. DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AAW90178.1}; GN ORFNames=NGO_1542 {ECO:0000313|EMBL:AAW90178.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90178.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90178.1; -; Genomic_DNA. DR RefSeq; WP_003700340.1; NC_002946.2. DR RefSeq; YP_208590.1; NC_002946.2. DR ProteinModelPortal; Q5F6K9; -. DR DNASU; 3281451; -. DR EnsemblBacteria; AAW90178; AAW90178; NGO_1542. DR GeneID; 3281451; -. DR KEGG; ngo:NGO1542; -. DR PATRIC; 20336582; VBINeiGon24812_1839. DR HOGENOM; HOG000049554; -. DR KO; K03587; -. DR OMA; KRRFIYL; -. DR OrthoDB; EOG6N0HHV; -. DR BioCyc; NGON242231:GI2G-1444-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 71 221 PBP_dimer. {ECO:0000259|Pfam:PF03717}. FT DOMAIN 263 558 Transpeptidase. FT {ECO:0000259|Pfam:PF00905}. SQ SEQUENCE 582 AA; 63765 MW; 241FBEF088160ECF CRC64; MLIKSEYKPR MLPKEEQVKK PMTSNGRISF VLMAMAVLFA CLIARGLYLQ TVTYNFLKEQ GDNRIVRTQA LPATRGTVSD RNGAVLALSA PTESLFAVPK DMKEMPSAAQ LERLSELVDV PVDVLRNKLE QKGKSFIWIK RQLDPKVAEE VKALGLENFV FEKELKRHYP MGNLFAHVIG FTDIDGKGQE GLELSLEDSL YGEDGAEVVL RDRQGNIVDS LDSPRNKAPQ NGKDIILSLD QRIQTLAYEE LNKAVEYHQA KAGTVVVLDA RTGEILALAN TPAYDPNRPG RADSEQRRNR AVTDMIEPGS AIKPFVIAKA LDAGKTDLNE RLNTQPYKIG PSPVRDDTHV YPSLDVRGIM QKSSNVGTSK LSARFGAEEM YDFYHELGIG VRMHSGFPGE TAGLLRNWRR WRPIEQATMS FGYGLQLSLL QLARAYTALT HDGVLLPLSF EKQAVAPQGK RIFKESTARE VRNLMVSVTE PGGTGTAGAV DGFDVGAKTG TARKFVNGRY ADNKHVATFI GFAPAKNPRV IVAVTIDEPT AHGYYGGVVA GPPFKKIMGG SLNILGISPT KPLTAAAVKT PS // ID Q5F899_NEIG1 Unreviewed; 53 AA. AC Q5F899; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89588.1}; GN ORFNames=NGO_0889 {ECO:0000313|EMBL:AAW89588.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89588.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89588.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89588; AAW89588; NGO_0889. DR BioCyc; NGON242231:GI2G-830-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 53 AA; 5969 MW; C2B5727B35D81462 CRC64; MGVDFVWFHR VSFSVETLPF GKVGSDFICE TRARVQTYGL NMPVGEDRSD NAV // ID Q5FAI8_NEIG1 Unreviewed; 245 AA. AC Q5FAI8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 51. DE SubName: Full=DNA polymerase {ECO:0000313|EMBL:AAW88799.1}; GN ORFNames=NGO_0030 {ECO:0000313|EMBL:AAW88799.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88799.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88799.1; -; Genomic_DNA. DR RefSeq; WP_010950975.1; NC_002946.2. DR RefSeq; YP_207211.1; NC_002946.2. DR ProteinModelPortal; Q5FAI8; -. DR EnsemblBacteria; AAW88799; AAW88799; NGO_0030. DR GeneID; 3282003; -. DR KEGG; ngo:NGO0030; -. DR PATRIC; 20332890; VBINeiGon24812_0030. DR HOGENOM; HOG000218759; -. DR KO; K02334; -. DR OMA; AMIETLC; -. DR OrthoDB; EOG63RGQ3; -. DR BioCyc; NGON242231:GI2G-27-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 102 232 UDG. {ECO:0000259|Pfam:PF03167}. SQ SEQUENCE 245 AA; 26262 MW; DD9FFEED6BB04D1A CRC64; MLSARYLHLH EALGLGPMWL KQAAAVLPPK NTPATPAQAR PQTVRAATIR PSQPHNVQTR LETMKALETA AVHTRKPAPE TETPPPGLSD GIAPVPAASG ITKLAVVSLC PPIEDAVYGQ LFHGKAGILL DNILKAAGLD AAYVHKTCWV KTAAVGNPMP SEQAVADALG QIARELDGCR APAVLFLGQA FVNLERQAMI ETLCGSRPFF IIDHPARLLR QPELKARNWQ VLKQLKRALR QGGGS // ID Q5F624_NEIG1 Unreviewed; 223 AA. AC Q5F624; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 62. DE SubName: Full=NADH:ubiquinone oxidoreductase subunit J {ECO:0000313|EMBL:AAW90363.1}; GN ORFNames=NGO_1742 {ECO:0000313|EMBL:AAW90363.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90363.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90363.1; -; Genomic_DNA. DR RefSeq; WP_003689941.1; NC_002946.2. DR RefSeq; YP_208775.1; NC_002946.2. DR EnsemblBacteria; AAW90363; AAW90363; NGO_1742. DR GeneID; 3281102; -. DR KEGG; ngo:NGO1742; -. DR PATRIC; 20337082; VBINeiGon24812_2081. DR HOGENOM; HOG000262592; -. DR KO; K00339; -. DR OMA; DYVFYFQ; -. DR OrthoDB; EOG6Q2SPV; -. DR BioCyc; NGON242231:GI2G-1638-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000256|RuleBase:RU004429}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000313|EMBL:AAW90363.1}. 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; 24462 MW; 649B0A2AC96B082E CRC64; MTFSVILFYI LAAIVLYGAV RTVTAKNPVH AALHLVLTFC VSAMIWMLMQ AEFLGVTLVV VYVGAVMVLF LFVVMMLNID IEEMRAGFWR HAPVAGVVGT LLAVALILIL VNPKTDLAAF GLMKDIPADY NNIRDLGSRI YTDYLLPFEL AAVLLLLGMV AAIALVHRKT TNPKRMDPAD QVKVRADQGR MRLVKMEAVK PQVESAEESE VSDGLKTEGE GKA // ID Q5F6J9_NEIG1 Unreviewed; 508 AA. AC Q5F6J9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 16-MAR-2016, entry version 83. DE SubName: Full=Proline:sodium symporter PutP {ECO:0000313|EMBL:AAW90188.2}; GN ORFNames=NGO_1552 {ECO:0000313|EMBL:AAW90188.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90188.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90188.2; -; Genomic_DNA. DR EnsemblBacteria; AAW90188; AAW90188; NGO_1552. DR PATRIC; 20336608; VBINeiGon24812_1850. DR HOGENOM; HOG000282935; -. DR OMA; VHKFDLS; -. DR OrthoDB; EOG6HB9QC; -. DR BioCyc; NGON242231:GI2G-1456-MONOMER; -. DR Proteomes; UP000000535; 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; PS50283; NA_SOLUT_SYMP_3; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|SAAS:SAAS00431219}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00431219, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 54315 MW; 41E2729BCE1FD996 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 STVVVWAEWV KKPARAAGES GLLTMYEIVP GFIVCLIVAV LVSLFNKEPS REIQERFEKA DADYRAAR // ID Q5F767_NEIG1 Unreviewed; 434 AA. AC Q5F767; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 49. DE SubName: Full=PqiA family protein {ECO:0000313|EMBL:AAW89970.1}; GN ORFNames=NGO_1319 {ECO:0000313|EMBL:AAW89970.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89970.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89970.1; -; Genomic_DNA. DR RefSeq; WP_010951240.1; NC_002946.2. DR RefSeq; YP_208382.1; NC_002946.2. DR EnsemblBacteria; AAW89970; AAW89970; NGO_1319. DR GeneID; 3281916; -. DR KEGG; ngo:NGO1319; -. DR PATRIC; 20336003; VBINeiGon24812_1552. DR HOGENOM; HOG000219070; -. DR KO; K03808; -. DR OMA; CRDEALP; -. DR OrthoDB; EOG661H80; -. DR BioCyc; NGON242231:GI2G-1233-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007498; PqiA. DR Pfam; PF04403; PqiA; 2. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 74 97 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 117 141 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 162 179 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 185 202 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 269 289 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 315 346 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 367 387 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 411 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 434 AA; 47865 MW; FAD358BB160457E7 CRC64; MKPFAENIPH SLRGNCRDEA LPPHTVDCPE CGCRTDVPQL DKGEAAFCPR CGHKLFRVGS HPFSGPPAYA AASLILMAFA YSMTYIEVGI PGAASVLSLP EMMRLMVFQD YGFLAEVMFV LTFGAPVLFL LLCLYVYAAL IRKQAYPALR LATRVMVRLR QAMMVDVFFV STLVAYIKLS SVAKVRFGPA FYLMFALSVM LIRTSVSVPQ HWVYFQIGRL TGNNAVQTAS EGKTCCSRCL YFRDSAESPC GVCGAELYRR RPKSLSISSA FLTAAVVLYF PANILPIMIS SNPAATEANT IFSGIAYMWD EGDRLIAAVI FSASILVPVL KIAAMSVLIA AARFALPAGA KKLSHLYRIT EAVGRWSMID IFVIIILMCS FHTYAARVIP GSAAVYFCLV VILTMLSAYY FDPRLLWDKR ASDGIAFNET EKYD // ID Q5F941_NEIG1 Unreviewed; 96 AA. AC Q5F941; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89296.1}; GN ORFNames=NGO_0563 {ECO:0000313|EMBL:AAW89296.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89296.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89296.1; -; Genomic_DNA. DR RefSeq; WP_003691352.1; NC_002946.2. DR RefSeq; YP_207708.1; NC_002946.2. DR EnsemblBacteria; AAW89296; AAW89296; NGO_0563. DR GeneID; 3282906; -. DR KEGG; ngo:NGO0563; -. DR OMA; DLYDGCY; -. DR OrthoDB; EOG66MQSF; -. DR BioCyc; NGON242231:GI2G-536-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 96 AA; 10987 MW; A06494C14037B43F CRC64; MKNAVYAHQI ETDLYDGCYI STTTDKEIAK KFATSSGIEN GYIYVLNRDL FGQYSIFEYE VEHPENPDEK EVTIRAEDCG CIPEEVIIAK ELIEIN // ID Q5F9F0_NEIG1 Unreviewed; 273 AA. AC Q5F9F0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 78. DE SubName: Full=Sulfate ABC transporter permease {ECO:0000313|EMBL:AAW89187.1}; GN ORFNames=NGO_0446 {ECO:0000313|EMBL:AAW89187.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89187.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89187.1; -; Genomic_DNA. DR RefSeq; WP_003706605.1; NC_002946.2. DR RefSeq; YP_207599.1; NC_002946.2. DR ProteinModelPortal; Q5F9F0; -. DR EnsemblBacteria; AAW89187; AAW89187; NGO_0446. DR GeneID; 3281095; -. DR KEGG; ngo:NGO0446; -. DR PATRIC; 20333920; VBINeiGon24812_0534. DR HOGENOM; HOG000263697; -. DR KO; K02047; -. DR OMA; NEYQFSA; -. DR OrthoDB; EOG654P2T; -. DR BioCyc; NGON242231:GI2G-425-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAAS:SAAS00524216, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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 20 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 273 AA; 29663 MW; E9722A8DC8A39CB8 CRC64; MKPYSANPNL TEPRRLRMLL IAAALGFLLL MLVVPLVAVF YEALKGGWDL YLKSLSDPEA WSAVKLTLIT ALIVVPVNAV LGVAMAWLLT RFDFLGKQLL TTLLDLPFSV SPVVAGLMFV LLFGAHTALG SRLEAQGIQI IFAIPGIVLT ALFVTFPFAA REIIPLMQTQ GDSEEQAALV LGASGWQMFW RVTLPNIKWT LLYGIILTNA RAMGEFGAVS VVSGHIRGET NTIPLLVEIF YNEYNFTGAF SLSGVLALLA LATLAVQNII TKL // ID Q5F5Y3_NEIG1 Unreviewed; 919 AA. AC Q5F5Y3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 64. 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 ORFNames=NGO_1785 {ECO:0000313|EMBL:AAW90404.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90404.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90404.1; -; Genomic_DNA. DR RefSeq; WP_003690003.1; NC_002946.2. DR RefSeq; YP_208816.1; NC_002946.2. DR ProteinModelPortal; Q5F5Y3; -. DR SMR; Q5F5Y3; 1-486. DR EnsemblBacteria; AAW90404; AAW90404; NGO_1785. DR GeneID; 3282472; -. DR KEGG; ngo:NGO1785; -. DR PATRIC; 20337214; VBINeiGon24812_2143. DR HOGENOM; HOG000258027; -. DR KO; K08300; -. DR OMA; HVLRMVQ; -. DR OrthoDB; EOG6PCPTH; -. DR BioCyc; NGON242231:GI2G-1683-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; 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:UP000000535}; 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; 101666 MW; 8B41C053578C354B CRC64; MKRMLFNATQ AEELRVAIVD GQNLLDLDIE TLGKEQRKGN IYKGIITRIE PSLEACFVDY GTDRHGFLPF KEVSRSYFLG YEGGRARIQD VLKEGMEVIV QVEKDERGNK GAALTTFISL AGRYLVLMPN NPRGGGVSRR IEGEERQELK AAMAQLDIPN GMSIIARTAG IGRSAEELEW DLNYLKQLWQ AIEEAGKAHH DPYLLFMESS LLIRAIRDYF RPDIGEILVD NQEVYDQVAE FMSYVMPGNA GRLKLYEDHT PLFSRFQIEH QIESAFSRSV SLPSGGAIVI DHTEALVSID VNSARATRGA DIEDTAFKTN MEAAEEVARQ MRLRDLGGLV VIDFIDMENP KHQRDVENVL RDALKKDRAR VQMGKLSRFG LLELSRQRLK PALGESSHAA CPRCAGTGVI RGIESTALHV LRMVQEEAMK DNTGEVRAQV PVDVATFLLN EKRAELFAME ERLDVNVVLI PNIHLENPHY EINRIRTDDV EEDGEPSYKR VAEPEEDESA KPFGGEKAKA ARPEPAVKGV RHTSPAPTAA PEKKTSWWDS FKAWLKRIFG GSETQAVPAA ETSEKRSTAN RSGSRANNRR QNPRRSKREG SKIEVREAAG KTAGQKARAD KAETRNNGNR RRNERGDRAT ERANEAEIQS RNVQPAAPVA DAAPPETEGQ TGKRRRNGSR NERGQTAPET AAVAETAVQT AENTPPEPYT AEDKGSKPKS ERNRRERDSR DAKERRERNN QRDRRQNGKK RNIPSAAKIE QYLNIHDTAD KVRSAAAHVF GETDANAPIT VSIADPLIAT PVQTASSAVS NGDALIYDAA EKIRRAAADI LPEGAAPKAA AQEMPSETAT FTAAAEQARE TAQTGGLVLI ETDPAALKAW AAQPEVQAGR GLRRSEQPKP SEAATVPAEE MIQVETRQG // ID Q5F6B4_NEIG1 Unreviewed; 94 AA. AC Q5F6B4; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90273.1}; GN ORFNames=NGO_1646 {ECO:0000313|EMBL:AAW90273.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90273.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90273.1; -; Genomic_DNA. DR RefSeq; WP_003689770.1; NC_002946.2. DR RefSeq; YP_208685.1; NC_002946.2. DR EnsemblBacteria; AAW90273; AAW90273; NGO_1646. DR GeneID; 3281344; -. DR KEGG; ngo:NGO1646; -. DR PATRIC; 20336832; VBINeiGon24812_1961. DR HOGENOM; HOG000219042; -. DR OrthoDB; EOG6J1DHC; -. DR BioCyc; NGON242231:GI2G-1542-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 9920 MW; ED54EC56F171FB5B CRC64; MKLLAALIPL LMSVAGRILT ALGLMAVTYA GVDRLAAHFQ QAITHSITGA PQAMLQLFYI SGGGTVLNIL FGAIAFILSF KQMTKLATSI GKKK // ID Q5F986_NEIG1 Unreviewed; 156 AA. AC Q5F986; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 38. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89251.1}; GN ORFNames=NGO_0513 {ECO:0000313|EMBL:AAW89251.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89251.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89251.1; -; Genomic_DNA. DR RefSeq; WP_010951069.1; NC_002946.2. DR RefSeq; YP_207663.1; NC_002946.2. DR EnsemblBacteria; AAW89251; AAW89251; NGO_0513. DR GeneID; 3282935; -. DR KEGG; ngo:NGO0513; -. DR PATRIC; 20334068; VBINeiGon24812_0606. DR HOGENOM; HOG000071312; -. DR OMA; FCALAGN; -. DR OrthoDB; EOG6GBMKC; -. DR BioCyc; NGON242231:GI2G-491-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 26 45 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 65 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 95 114 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 126 143 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 156 AA; 17013 MW; DDAC15DED0B72983 CRC64; MLRFLTERRF LPAGFQAWLF GTATRVLEAV IGLGLSGYAA VFALAPDEIY AWRIYYKFQD IPEAWTVGVL AAAGLLQTAL LFARGVRACV ASAYLLLFSG FVWFLVSVAF WGAYPPLNTG MVVPPLLAFF CALAGNNALR FLFSAQKSRG LADEGS // ID Q5F9R8_NEIG1 Unreviewed; 159 AA. AC Q5F9R8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89069.1}; GN ORFNames=NGO_0322 {ECO:0000313|EMBL:AAW89069.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89069.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89069.1; -; Genomic_DNA. DR RefSeq; WP_003687711.1; NC_002946.2. DR RefSeq; YP_207481.1; NC_002946.2. DR EnsemblBacteria; AAW89069; AAW89069; NGO_0322. DR GeneID; 3281749; -. DR KEGG; ngo:NGO0322; -. DR PATRIC; 20333631; VBINeiGon24812_0393. DR HOGENOM; HOG000218857; -. DR OMA; MAVQPFL; -. DR OrthoDB; EOG6BS8R0; -. DR BioCyc; NGON242231:GI2G-304-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 159 AA; 18003 MW; 8A5048F65EFA1F6B CRC64; MPESIFKQIS SDILRLHRDS VYSLLATSGC NCQVHEAAYV NIDGKYYIAL SCEPEVGEVE TGILLIEDES RNLRLSWVGS ARELDRKDNA YKRALSALSR KLGRCKDKLH TAVQPFLLEL VPEKGRFSVG DEEVWISRND LVRALYPVGY SMRQAVLQI // ID Q5F9T7_NEIG1 Unreviewed; 249 AA. AC Q5F9T7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 52. DE SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:AAW89050.1}; GN ORFNames=NGO_0303 {ECO:0000313|EMBL:AAW89050.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89050.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89050.1; -; Genomic_DNA. DR RefSeq; WP_003706646.1; NC_002946.2. DR RefSeq; YP_207462.1; NC_002946.2. DR REBASE; 10870; NgoAXIIIP. DR DNASU; 3281684; -. DR EnsemblBacteria; AAW89050; AAW89050; NGO_0303. DR GeneID; 3281684; -. DR KEGG; ngo:NGO0303; -. DR HOGENOM; HOG000114529; -. DR KO; K07454; -. DR OMA; SHIRPWK; -. DR OrthoDB; EOG6D2KV1; -. DR BioCyc; NGON242231:GI2G-283-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR003615; HNH_nuc. DR Pfam; PF13391; HNH_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89050.1}; KW Hydrolase {ECO:0000313|EMBL:AAW89050.1}; KW Nuclease {ECO:0000313|EMBL:AAW89050.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 146 197 HNHc. {ECO:0000259|Pfam:PF13391}. SQ SEQUENCE 249 AA; 28630 MW; 0BE4ADCC3AEF9FAA CRC64; MKKWTRDETL VALYLYYIIP FQKVSKDNPV IQEYAEILGR TPSALGMKIG NLGRLDPTLK VKNISGLSNG SKMDVVVWNE FSGDWEQLNK EFEGVISQYQ SNDENSNIEI ESPEIPKGRE RFARISVRVN QGFFRSSVLA AYNNQCCITG LKQPELLVAS HIKPWGEDKD NRLNPRNGLC LNALHDKAFD RGLLGIDENF KIIFSPLLAK TEGFDDLFKP YENRMIRLPE RLNPSLEFLK FHRENIFQS // ID Q5F7Z0_NEIG1 Unreviewed; 97 AA. AC Q5F7Z0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89697.1}; GN ORFNames=NGO_1014 {ECO:0000313|EMBL:AAW89697.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89697.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89697.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89697; AAW89697; NGO_1014. DR PATRIC; 20335236; VBINeiGon24812_1186. DR HOGENOM; HOG000071268; -. DR OMA; RSEWARY; -. DR OrthoDB; EOG6J1DHZ; -. DR BioCyc; NGON242231:GI2G-940-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR026365; BcepMu_gp16. DR TIGRFAMs; TIGR04111; BcepMu_gp16; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 97 AA; 11026 MW; 2BB066773723765B CRC64; MFIVQRGLKL NTLYHTKGIN NIEKPLNFKP IPYLQTRGST AVWFKRNGVC KTHRAKHFNL ERTAVEHPLR GKLKGNFGKS HEAAVKLGLK EDADGDE // ID Q5F7L9_NEIG1 Unreviewed; 83 AA. AC Q5F7L9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89818.1}; GN ORFNames=NGO_1151 {ECO:0000313|EMBL:AAW89818.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89818.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89818.1; -; Genomic_DNA. DR RefSeq; WP_003689748.1; NC_002946.2. DR RefSeq; YP_208230.1; NC_002946.2. DR EnsemblBacteria; AAW89818; AAW89818; NGO_1151. DR GeneID; 3282163; -. DR KEGG; ngo:NGO1151; -. DR PATRIC; 20335564; VBINeiGon24812_1347. DR HOGENOM; HOG000219046; -. DR OrthoDB; EOG6J1DHR; -. DR BioCyc; NGON242231:GI2G-1064-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 83 AA; 9532 MW; 2C6AED3709B0AAEA CRC64; MGSIEQRLEY LEEANDVLRM QNHVLSTAFK ALIRALPADT AEIAVESIQL AFEDALAELS YEDSPHTDLF HDVTYAFFRE KER // ID Q5F8Y8_NEIG1 Unreviewed; 100 AA. AC Q5F8Y8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89349.1}; GN ORFNames=NGO_0621 {ECO:0000313|EMBL:AAW89349.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89349.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89349.1; -; Genomic_DNA. DR EnsemblBacteria; AAW89349; AAW89349; NGO_0621. DR PATRIC; 20334326; VBINeiGon24812_0735. DR HOGENOM; HOG000071301; -. DR OMA; MDYMPAN; -. DR OrthoDB; EOG696BWX; -. DR BioCyc; NGON242231:GI2G-589-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018546; DUF2004. DR Pfam; PF09406; DUF2004; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 100 AA; 11429 MW; F03987F69F9C9043 CRC64; MDAFAAFLSE LEKADDAARA ALTEYLKRDS RYIDFHTEDT QTSRDAAKFV RTMQLIYISL WAKNPAFAVM DYMPANIESD EILAVKLHLD GSIFSIDWES // ID Q5F758_NEIG1 Unreviewed; 397 AA. AC Q5F758; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 67. DE SubName: Full=Aromatic amino acid aminotransferase {ECO:0000313|EMBL:AAW89979.1}; DE EC=2.6.1.57 {ECO:0000313|EMBL:AAW89979.1}; GN ORFNames=NGO_1329 {ECO:0000313|EMBL:AAW89979.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89979.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89979.1; -; Genomic_DNA. DR RefSeq; WP_003697336.1; NC_002946.2. DR RefSeq; YP_208391.1; NC_002946.2. DR ProteinModelPortal; Q5F758; -. DR SMR; Q5F758; 1-396. DR EnsemblBacteria; AAW89979; AAW89979; NGO_1329. DR GeneID; 3282024; -. DR KEGG; ngo:NGO1329; -. DR PATRIC; 20336027; VBINeiGon24812_1563. DR HOGENOM; HOG000185898; -. DR KO; K00832; -. DR OMA; FPDSGVW; -. DR OrthoDB; EOG6C2WBK; -. DR BioCyc; NGON242231:GI2G-1243-MONOMER; -. DR Proteomes; UP000000535; 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:AAW89979.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:AAW89979.1}. FT DOMAIN 27 392 Aminotran_1_2. FT {ECO:0000259|Pfam:PF00155}. SQ SEQUENCE 397 AA; 44506 MW; F36C50DC4F78EE33 CRC64; MYRHIEYYPG DPILSLVETF KNDPRPEKVN LSIGIYFDDE GRMPVLESVS RAETARAAAP APSPYLPMEG LDVYRSAVQH LLFGKGNPAL AQGRIVTVQT LGGSGALKVG ADFLHRWFPE ARAYVSDPTW DNHRGIFEGA GFEVGTYPYY DPATVGVKFD EMTAFFNTLP ENSVLILHPC CHNPTGVDMS ERQWDEVLQI IKTRKLIPFM DIAYQGFGGD LDSDAYAVRK AVEMDLPLFV SNSFSKNLSL YGERVGGLSV VCPNKEEADL VFGQLKFTVR RIYSSPPAHG AYIAADVMNS SELYALWQNE VYMMRDRIRA MRQKLYGVLT ARIPDRDFTY FIKQRGMFGY TGLSVGQVRR LRDEFAVYLL DSGRMCVAGL NTSNITYVAD ALAEVLK // ID Q5F4Y6_NEIG1 Unreviewed; 279 AA. AC Q5F4Y6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Lacto-N-neotetraose biosynthesis glycosyl transferase {ECO:0000313|EMBL:AAW90751.1}; GN ORFNames=NGO_2156 {ECO:0000313|EMBL:AAW90751.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90751.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90751.1; -; Genomic_DNA. DR RefSeq; WP_010356403.1; NC_002946.2. DR RefSeq; YP_209163.1; NC_002946.2. DR CAZy; GT25; Glycosyltransferase Family 25. DR EnsemblBacteria; AAW90751; AAW90751; NGO_2156. DR GeneID; 3282767; -. DR KEGG; ngo:NGO2156; -. DR PATRIC; 20338164; VBINeiGon24812_2604. DR HOGENOM; HOG000218751; -. DR KO; K07270; -. DR OMA; AQFKRVE; -. DR OrthoDB; EOG6R5C54; -. DR BioCyc; NGON242231:GI2G-2045-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR InterPro; IPR002654; Glyco_trans_25. DR Pfam; PF01755; Glyco_transf_25; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW90751.1}. SQ SEQUENCE 279 AA; 31796 MW; 40A33608685BD991 CRC64; MQNHVISLAS AAERRAHIAA TFGSRGIPFQ FFDALMPSER LEQAMAELVP GLSAHPYLSG VEKACFMSHA VLWEQALDEG LPYIAVFEDD VLLGEGAEQF LAEDTWLEER FDKDSAFIVR LETMFMHVLT SPSGVADYGG RAFPLLESEH CGTAGYIISR KAMRFFLDRF AVLPPERLHP VDLMMFGNPD DREGMPVCQL NPALCAQELH YAKFHDQNSA LGSLIEHDRR LNRKQQWRDS PANTFKHRLI RALTKIGRER EKRRKRREQT IGKIIVPFQ // ID Q5F9L7_NEIG1 Unreviewed; 169 AA. AC Q5F9L7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 13-APR-2016, entry version 82. 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 ORFNames=NGO_0376 {ECO:0000313|EMBL:AAW89120.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89120.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89120.1; -; Genomic_DNA. DR RefSeq; WP_003687796.1; NC_002946.2. DR RefSeq; YP_207532.1; NC_002946.2. DR ProteinModelPortal; Q5F9L7; -. DR SMR; Q5F9L7; 1-167. DR PRIDE; Q5F9L7; -. DR EnsemblBacteria; AAW89120; AAW89120; NGO_0376. DR GeneID; 3281821; -. DR KEGG; ngo:NGO0376; -. DR PATRIC; 20333755; VBINeiGon24812_0455. DR HOGENOM; HOG000065978; -. DR KO; K03768; -. DR OMA; GMDENFK; -. DR OrthoDB; EOG6S26C3; -. DR BioCyc; NGON242231:GI2G-355-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Isomerase {ECO:0000256|RuleBase:RU363019}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Rotamase {ECO:0000256|RuleBase:RU363019}. FT DOMAIN 1 168 PPIase cyclophilin-type. FT {ECO:0000259|PROSITE:PS50072}. SQ SEQUENCE 169 AA; 18880 MW; 16EA51BCD5F7E8EC CRC64; MIILHTNKGD IKIELDFDKA PVTAKNFEQY VKDGFYDGVI FHRVIKGFMI QGGGMDENMN EKETRDPIQN EASNGLPNDK YTIAMARTSD PHSAGAQFFI NTADNAFLNF RSKELYGKTV VQDWGYAVFG KVVDGFDVVD AIESVSTKRH GYHDDVPTEP VIIIKAEAV // ID Q5F4X6_NEIG1 Unreviewed; 123 AA. AC Q5F4X6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 46. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90761.1}; GN ORFNames=NGO_2167 {ECO:0000313|EMBL:AAW90761.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90761.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90761.1; -; Genomic_DNA. DR RefSeq; WP_003687178.1; NC_002946.2. DR RefSeq; YP_209173.1; NC_002946.2. DR DNASU; 3282757; -. DR EnsemblBacteria; AAW90761; AAW90761; NGO_2167. DR GeneID; 3282757; -. DR KEGG; ngo:NGO2167; -. DR PATRIC; 20338190; VBINeiGon24812_2617. DR HOGENOM; HOG000267103; -. DR OMA; PFRRWFF; -. DR OrthoDB; EOG6X6RHM; -. DR BioCyc; NGON242231:GI2G-2055-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 60 76 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 88 111 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 123 AA; 13904 MW; 46755C0B771BEAD8 CRC64; MKRQAFFKPM ACAAFLSAVS LRLPVLGACY AILSLYAFAL YGIDKRRAVR GKRRIPEHRL LLPALFGGWT GAYLGSRMFR HKTAKKRFVV LFRLTVSGNV LATCILIDYF VPPELFVKLG QHL // ID Q5F6I0_NEIG1 Unreviewed; 316 AA. AC Q5F6I0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 76. DE SubName: Full=CysB family transcriptional regulator {ECO:0000313|EMBL:AAW90207.1}; GN Name=cysB {ECO:0000313|EMBL:AAW90207.1}; GN ORFNames=NGO_1578 {ECO:0000313|EMBL:AAW90207.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90207.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90207.1; -; Genomic_DNA. DR RefSeq; WP_003689503.1; NC_002946.2. DR RefSeq; YP_208619.1; NC_002946.2. DR ProteinModelPortal; Q5F6I0; -. DR EnsemblBacteria; AAW90207; AAW90207; NGO_1578. DR GeneID; 3281421; -. DR KEGG; ngo:NGO1578; -. DR PATRIC; 20336682; VBINeiGon24812_1887. DR HOGENOM; HOG000260068; -. DR KO; K13634; -. DR OMA; QGHPLTK; -. DR OrthoDB; EOG6WQD4N; -. DR BioCyc; NGON242231:GI2G-1475-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|RuleBase:RU000709, KW ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 35188 MW; 5B07B5FEBAF3A8BF CRC64; MKLQQLKYAL EVYRHNLNVS EAAEALFTSQ PGISKQIKLL EEEIGIQIFI RSGKRVVSVS QPGKVVLDIA ERILRDVQNI KNIGSEFTGQ DSGSLTVATT HTQARYALPL IVADFVKRYP KVNLTIKQGS PAAIAQMVTS GESDLAIVTE RIDDHPELGR LSCYDWTHAV IVPNDHPLLE CRNPLRIEDL ARFPLITYEF AFNAGSSIAR AFAKARLERP DVALAAADTD VLKTYVRLGL GVGLMAKMAY NPDTDGDLQL VDAAHLFEPS PTWIALRSDT YLRGYAYDFI QAFAPHLTRE KVDRILYTPI SEDFSI // ID Q5F9Q3_NEIG1 Unreviewed; 201 AA. AC Q5F9Q3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 44. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW89084.1}; GN ORFNames=NGO_0339 {ECO:0000313|EMBL:AAW89084.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89084.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89084.1; -; Genomic_DNA. DR RefSeq; WP_003687740.1; NC_002946.2. DR RefSeq; YP_207496.1; NC_002946.2. DR EnsemblBacteria; AAW89084; AAW89084; NGO_0339. DR GeneID; 3281751; -. DR KEGG; ngo:NGO0339; -. DR PATRIC; 20333669; VBINeiGon24812_0412. DR HOGENOM; HOG000218859; -. DR OMA; VSMTFAF; -. DR OrthoDB; EOG68M4FF; -. DR BioCyc; NGON242231:GI2G-319-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 30 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 61 80 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 100 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 159 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 179 197 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 201 AA; 22436 MW; 3ABA4A544F6A4EF8 CRC64; MILLHLDFLS ALLYAAVFLF LIFRAGMLQW FWASIALWLG ISVLGVKLMP GMWGMTRAAP LFIPHFYLTL GSIFFFIGYW NRKTDGNGWQ ADPEHPLLGL FAVSNVSMTL AFVGICALVH YCFSGTVQVF VFAALLKLYA LKPVYWFVLQ FVLMAVAYVH RCGIDRQPPS TFGGSQLRLG VLAAMLMQVA VTAMLLAEIG R // ID Q5FA91_NEIG1 Unreviewed; 499 AA. AC Q5FA91; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 75. DE SubName: Full=Protease Do {ECO:0000313|EMBL:AAW88896.1}; GN ORFNames=NGO_0138 {ECO:0000313|EMBL:AAW88896.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88896.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88896.1; -; Genomic_DNA. DR RefSeq; WP_003687423.1; NC_002946.2. DR RefSeq; YP_207308.1; NC_002946.2. DR ProteinModelPortal; Q5FA91; -. DR EnsemblBacteria; AAW88896; AAW88896; NGO_0138. DR GeneID; 3281276; -. DR KEGG; ngo:NGO0138; -. DR PATRIC; 20333187; VBINeiGon24812_0176. DR HOGENOM; HOG000223640; -. DR KO; K04771; -. DR OMA; IDQKDAS; -. DR OrthoDB; EOG61ZTDN; -. DR BioCyc; NGON242231:GI2G-126-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Hydrolase {ECO:0000313|EMBL:AAW88896.1}; KW Protease {ECO:0000313|EMBL:AAW88896.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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_5004256090. FT DOMAIN 302 381 PDZ (DHR). {ECO:0000259|PROSITE:PS50106}. SQ SEQUENCE 499 AA; 52568 MW; 50D733876EA2CB04 CRC64; MFKKYQYFAL AALCAALLAG CEKAGSFFGA DKKEASFVER IEHTKDDGSV SMLLPDFAQL VQSEGPAVVN IQAAPAPRTQ NGSGNAETDS DPLADSDPFY EFFKRLVPNM PEIPQEEADD GGLNFGSGFI ISKNGYILTN THVVAGMGSI KVLLNDKREY TAKLIGSDVQ SDVALLKIDA TEELPVVKIG NPKNLKPGEW VAAIGAPFGF DNSVTAGIVS AKGRSLPNES YTPFIQTDVA INPGNSGGPL FNLKGQVVGI NSQIYSRSGG FMGISFAIPI DVAMNVAEQL KNTGKVQRGQ LGVIIQEVSY GLAQSFGLDK ASGALIAKIL PGSPAERAGL QAGDIVLSLD GGEIRSSGDL PVMVGAITPG KEVSLGVWRK GEEITIKAKL GNAAEHTGAS SKTDEAPYTE QQSGTFSVES AGITLQTHTD SSGKHLVVVR VSDAAERAGL RRGDEILAVG QVPVNDEAGF RKAMDKAGKN VPLLVMRRGN TLFIALNLQ // ID Q5F934_NEIG1 Unreviewed; 186 AA. AC Q5F934; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=CreA protein {ECO:0000313|EMBL:AAW89303.1}; GN ORFNames=NGO_0570 {ECO:0000313|EMBL:AAW89303.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89303.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89303.1; -; Genomic_DNA. DR RefSeq; WP_003691340.1; NC_002946.2. DR RefSeq; YP_207715.1; NC_002946.2. DR EnsemblBacteria; AAW89303; AAW89303; NGO_0570. DR GeneID; 3282519; -. DR KEGG; ngo:NGO0570; -. DR PATRIC; 20334202; VBINeiGon24812_0673. DR HOGENOM; HOG000257967; -. DR KO; K05805; -. DR OMA; SPQNSVT; -. DR OrthoDB; EOG6MD95K; -. DR BioCyc; NGON242231:GI2G-543-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 186 AA; 19975 MW; DEFAC1AAA7ED0D47 CRC64; MNRLLLLSAA VLPTACGSGE TDKIGRASTV FNMLGKNDRI EVEGFDDPDV QGVACYISYA KKGGLKEMVN LEEDASDASV SCVQTASSIS FDETAVRKPK EVFKRGTGFA FKSRQIVRYY DPKRKAFAYL VYSDKIVQGS PKNSLSAVSC FGSGIPQTDG VQADTSGKLL AGACIISNPI KNPDKR // ID Q5F6M2_NEIG1 Unreviewed; 414 AA. AC Q5F6M2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 58. DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033}; GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033}; GN ORFNames=NGO_1529 {ECO:0000313|EMBL:AAW90165.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90165.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}. CC -!- SUBUNIT: Interacts with ftsZ. {ECO:0000256|PIRNR:PIRNR003101}. CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP- CC Rule:MF_02033}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_02033}; Cytoplasmic side {ECO:0000256|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:0000256|HAMAP-Rule:MF_02033}. CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP- CC Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW90165.1; -; Genomic_DNA. DR RefSeq; WP_003689434.1; NC_002946.2. DR RefSeq; YP_208577.1; NC_002946.2. DR ProteinModelPortal; Q5F6M2; -. DR DNASU; 3281555; -. DR EnsemblBacteria; AAW90165; AAW90165; NGO_1529. DR GeneID; 3281555; -. DR KEGG; ngo:NGO1529; -. DR PATRIC; 20336554; VBINeiGon24812_1825. DR HOGENOM; HOG000049205; -. DR KO; K03590; -. DR OMA; HTAVIPF; -. DR OrthoDB; EOG6TR0B6; -. DR BioCyc; NGON242231:GI2G-1431-MONOMER; -. DR Proteomes; UP000000535; 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 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000256|PIRNR:PIRNR003101, ECO:0000313|EMBL:AAW90165.1}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000256|PIRNR:PIRNR003101, ECO:0000313|EMBL:AAW90165.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000256|PIRNR:PIRNR003101}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 8 194 FtsA. {ECO:0000259|SMART:SM00842}. SQ SEQUENCE 414 AA; 44055 MW; 00BD97F23175D40E CRC64; MEQQKRYISV LDIGTSKVLA LIGEVQDDDK INIIGLGQAP SRGLRAGMVT NIDATVQAIR QAVNDAELMA DTKITHVTTG IAGNHIRSLN SQGVVKIKDG EVTQADIDRA IETAKAINIP PDQKILDAVV QDYIIDTQLG VREPIGMSGV RLDTRVHIIT GASTAVQNVQ KCIELCGLKS DQIMLQPLAS GQAVLTEDEK DLGVCVIDIG GGTTDIAVYM NGAIRHTSVI PAGGNLITKD LSKSLRTPLD AAEYIKIHYG VASCDTEGLG EMIEVPGVGD RTSRQVSSKV LAAIISARIQ EIFGVVLGEL QKSGFPKEVL NAGIVLTGGV SMMTGIVEFA EKIFDLPVRT GAPQEMGGLS DRVRTPRFST AIGLLHAACK LEGNLPQPEN GTVQEREGGG GLLARLKRWI ENNL // ID Q5F9W8_NEIG1 Unreviewed; 119 AA. AC Q5F9W8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89019.2}; GN ORFNames=NGO_0268 {ECO:0000313|EMBL:AAW89019.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89019.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89019.2; -; Genomic_DNA. DR EnsemblBacteria; AAW89019; AAW89019; NGO_0268. DR PATRIC; 20333505; VBINeiGon24812_0333. DR HOGENOM; HOG000218746; -. DR OMA; YLIPEMD; -. DR OrthoDB; EOG6WT8DD; -. DR BioCyc; NGON242231:GI2G-251-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 119 AA; 14142 MW; FDED459384D094C7 CRC64; MYFVDRTAAV LKPTARFLEW LKSTDENMPD LTIEQLRADC SVFLVPQFDE PEAVVSYFDE RYRQIFEAEL AGWDIDKDKW PQDMGLKAFW EFFDIEIHDM VLDMEEADLN ITPVFDNMM // ID Q5F942_NEIG1 Unreviewed; 594 AA. AC Q5F942; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692}; DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692}; GN ORFNames=NGO_0562 {ECO:0000313|EMBL:AAW89295.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89295.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89295.1; -; Genomic_DNA. DR RefSeq; WP_003700029.1; NC_002946.2. DR RefSeq; YP_207707.1; NC_002946.2. DR ProteinModelPortal; Q5F942; -. DR SMR; Q5F942; 2-82, 112-593. DR EnsemblBacteria; AAW89295; AAW89295; NGO_0562. DR GeneID; 3282471; -. DR KEGG; ngo:NGO0562; -. DR PATRIC; 20334188; VBINeiGon24812_0666. DR HOGENOM; HOG000276708; -. DR KO; K00382; -. DR OMA; YTSPEWA; -. DR OrthoDB; EOG6QCD6D; -. DR BioCyc; NGON242231:GI2G-535-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; 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 Redox-active center {ECO:0000256|RuleBase:RU003692}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 3 77 Lipoyl-binding. FT {ECO:0000259|PROSITE:PS50968}. SQ SEQUENCE 594 AA; 61794 MW; 35277D7C5E60FABE CRC64; MALVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA EVAGVIKEVK VKVGDKISEG GLIVVVEAEG AAAAPKAEAA AAPAQEAPKA AAPAPQAAQF GGAADAEYDV VVLGGGPGGY SAAFAAADEG LKVAIVERYK TLGGVCLNVG CIPSKALLHN AAVIDEVRHL AANGIKYPKP 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 ALGVCTDLPP QKKK // ID Q5F7U7_NEIG1 Unreviewed; 105 AA. AC Q5F7U7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89740.1}; GN ORFNames=NGO_1070 {ECO:0000313|EMBL:AAW89740.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89740.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89740.1; -; Genomic_DNA. DR RefSeq; WP_002215112.1; NC_002946.2. DR RefSeq; YP_208152.1; NC_002946.2. DR EnsemblBacteria; AAW89740; AAW89740; NGO_1070. DR GeneID; 3281529; -. DR KEGG; ngo:NGO1070; -. DR PATRIC; 20335378; VBINeiGon24812_1255. DR OrthoDB; EOG67T5NK; -. DR BioCyc; NGON242231:GI2G-985-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 105 AA; 12256 MW; 0D0D3EF73BC92A6A CRC64; MKKNIFHNVS LYEIIFSDNG NTLTLSFTDT IEGNYFGYIK CSNILNFKLD TNNFVDYEDK EDSLFPLFIP EIELYKYQFY SEIIIDVGII IKISAETINF EPLGK // ID Q5F737_NEIG1 Unreviewed; 188 AA. AC Q5F737; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90000.1}; GN ORFNames=NGO_1350 {ECO:0000313|EMBL:AAW90000.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90000.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90000.1; -; Genomic_DNA. DR ProteinModelPortal; Q5F737; -. DR DNASU; 3282055; -. DR EnsemblBacteria; AAW90000; AAW90000; NGO_1350. DR PATRIC; 20336079; VBINeiGon24812_1589. DR OrthoDB; EOG6384M8; -. DR BioCyc; NGON242231:GI2G-1264-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 188 AA; 20443 MW; 3D30CC8D1A7BD89A CRC64; MLPHSGRMVL IDRITRYGDD FVEAGAQVKP DHILLAGGML PYTAFIELMA QAVGAYAGIQ ARKNARPVRL GFLPGTRKLE IFAQSVPVGT HLPATAHMSI QDAGVWACPT ANCVGRMRRK LRPEHSFQTA FWHAPHSTCT APNTMTEQLT PSEQAHIRRT TMTETVLITG SNRGIGKAAA LGFGGRRL // ID Q5F6J0_NEIG1 Unreviewed; 83 AA. AC Q5F6J0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90197.1}; GN ORFNames=NGO_1564 {ECO:0000313|EMBL:AAW90197.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90197.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90197.1; -; Genomic_DNA. DR RefSeq; WP_003689481.1; NC_002946.2. DR RefSeq; YP_208609.1; NC_002946.2. DR EnsemblBacteria; AAW90197; AAW90197; NGO_1564. DR GeneID; 3281473; -. DR KEGG; ngo:NGO1564; -. DR PATRIC; 20336636; VBINeiGon24812_1864. DR BioCyc; NGON242231:GI2G-1465-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 83 AA; 9404 MW; 1A72A35FFD00B646 CRC64; MDIFRESRPF CATGCPTPTS GSAFHHRRRR YGQDRIGRAF LTMHRILDKE NQIHTDMALA LPAVVKDAVA IWADMDTLDR CSG // ID Q5F993_NEIG1 Unreviewed; 199 AA. AC Q5F993; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89244.1}; GN ORFNames=NGO_0506 {ECO:0000313|EMBL:AAW89244.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89244.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89244.1; -; Genomic_DNA. DR RefSeq; WP_003692874.1; NC_002946.2. DR RefSeq; YP_207656.1; NC_002946.2. DR EnsemblBacteria; AAW89244; AAW89244; NGO_0506. DR GeneID; 3282943; -. DR KEGG; ngo:NGO0506; -. DR PATRIC; 20334054; VBINeiGon24812_0599. DR HOGENOM; HOG000057733; -. DR OMA; RCRFKDD; -. DR OrthoDB; EOG6J1DCB; -. DR BioCyc; NGON242231:GI2G-484-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR011740; DUF2460. DR Pfam; PF09343; DUF2460; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 199 AA; 22182 MW; 94A0AA93768BC196 CRC64; MGNAVFPEFP GLKWGRKKTA VWSTGTQKSA SGREFRTAYY TYPQWRFSLS FEVLRTKASV NELEKLAGFF NARKGSFESF LYEDPADNAV TDQPVGNTVQ GVARYQLVRS MGGFIEPVSA VKERPAVKVG GTALAYGRDY TVTDKGVLVF NTPQPPGRPI TWTGGFYFRV RFTSDTVDFE NVLGSLWAAK KIEFTSVKL // ID Q5FAG3_NEIG1 Unreviewed; 166 AA. AC Q5FAG3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 64. DE SubName: Full=MFS transporter {ECO:0000313|EMBL:AAW88824.1}; GN ORFNames=NGO_0059 {ECO:0000313|EMBL:AAW88824.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88824.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88824.1; -; Genomic_DNA. DR RefSeq; WP_003687298.1; NC_002946.2. DR RefSeq; YP_207236.1; NC_002946.2. DR ProteinModelPortal; Q5FAG3; -. DR EnsemblBacteria; AAW88824; AAW88824; NGO_0059. DR GeneID; 3282327; -. DR KEGG; ngo:NGO0059; -. DR PATRIC; 20332968; VBINeiGon24812_0068. DR HOGENOM; HOG000115783; -. DR KO; K00484; -. DR OMA; MAREWHE; -. DR OrthoDB; EOG6T1WSH; -. DR BioCyc; NGON242231:GI2G-53-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 16 164 Flavin_Reduct. FT {ECO:0000259|SMART:SM00903}. SQ SEQUENCE 166 AA; 18401 MW; E9DEFB7D417FEDC4 CRC64; MADLQKTFQT SFRDAMASCA AGVHVITTDG AAGRYGITMT AVAPVTDEPP TVMLCINRSA RIIPILSENG SLCINMLADE HQDVAEHFAG LTGLSPEERF AYHIWHRGKT GQLEIEGALA HLHGHIVGKH EIGTHFVFYV RLDEIKNCGC KRPALLYFRR QFRPLD // ID Q5F4X0_NEIG1 Unreviewed; 166 AA. AC Q5F4X0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90767.1}; GN ORFNames=NGO_2174 {ECO:0000313|EMBL:AAW90767.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90767.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90767.1; -; Genomic_DNA. DR RefSeq; WP_010951421.1; NC_002946.2. DR RefSeq; YP_209179.1; NC_002946.2. DR DNASU; 3282751; -. DR EnsemblBacteria; AAW90767; AAW90767; NGO_2174. DR GeneID; 3282751; -. DR KEGG; ngo:NGO2174; -. DR PATRIC; 20338212; VBINeiGon24812_2628. DR HOGENOM; HOG000258049; -. DR KO; K07040; -. DR OMA; SANQDKP; -. DR OrthoDB; EOG61046G; -. DR BioCyc; NGON242231:GI2G-2061-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR003772; DUF177. DR Pfam; PF02620; DUF177; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 166 AA; 18799 MW; F94A41B9783F3539 CRC64; MSDPNLIDPE IFAAERQNLQ GSFLLEELDE RVSLHDYPAD RRNKISFTLT GGRDRLQRLF LDLNVKADMP LICQRCIKPM PFMLDESSRI ILFSDEESLD ESMLADEELE GILIEKELDV RALVEDQILM SLPFSPRHGH CGNTLPESAN QDKPNPFAVL AGLKSS // ID Q5F9F2_NEIG1 Unreviewed; 508 AA. AC Q5F9F2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 69. 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 ORFNames=NGO_0444 {ECO:0000313|EMBL:AAW89185.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89185.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89185.1; -; Genomic_DNA. DR RefSeq; WP_003687904.1; NC_002946.2. DR RefSeq; YP_207597.1; NC_002946.2. DR ProteinModelPortal; Q5F9F2; -. DR SMR; Q5F9F2; 2-508. DR EnsemblBacteria; AAW89185; AAW89185; NGO_0444. DR GeneID; 3281086; -. DR KEGG; ngo:NGO0444; -. DR PATRIC; 20333914; VBINeiGon24812_0531. DR HOGENOM; HOG000046975; -. DR KO; K01754; -. DR OMA; DEVCAAM; -. DR OrthoDB; EOG6ZSP7D; -. DR BioCyc; NGON242231:GI2G-423-MONOMER; -. DR UniPathway; UPA00047; UER00054. DR Proteomes; UP000000535; 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:UP000000535}; KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012}; KW Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:AAW89185.1}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 334 405 ACT-like. {ECO:0000259|PROSITE:PS51672}. FT DOMAIN 428 499 ACT-like. {ECO:0000259|PROSITE:PS51672}. SQ SEQUENCE 508 AA; 55033 MW; 1C030666B680DD17 CRC64; MNTPLPYSDY LIRILTASVY DVAVETPLEP ARSLSVRLKN NILLKREDLQ PVFSFKIRGA YNKMSKLPKD ALACGVIAAS AGNHAQGVAL SAQRLGCRAV IVMPETTPKI KVDAVKSRGG EVVLRGVSYN DAYDYAMELA EQEGLTYIAP FDDPDVIAGQ GTVGMEIVSQ HPDPIRAVFV PIGGGGLAAG VAAFIKQVRP EIKVIGVQTN DSCCMKQSVE AGEIVHLKDV GLFSDGTAVK VVGNGTFRLC KELLDEIITV DTDAVCGAVK DIFDDTRSIT EPAGALALAG LKAYIAREGA ENQTLIAVTS GANMNFHRLR HVSERSELGE GNEGIFAVTI PEERGSFLKF VNILGNRNIT EFNYRYGGDE KAHIFVGLQA AGPQDLAVIG SRLDEAGLPN VDLTNNEIAK IHIRYMVGGR TDKVGHERLV SFEFPERPGA LARFLNHMQG GWNITLFHYR NHGADYGRIL VGIDVPPHDA AAFDGFLESL GYSYHEETQN AAYKLFLA // ID Q5F660_NEIG1 Unreviewed; 303 AA. AC Q5F660; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 70. DE SubName: Full=LysR family transcriptional regulator {ECO:0000313|EMBL:AAW90327.1}; GN ORFNames=NGO_1706 {ECO:0000313|EMBL:AAW90327.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90327.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW90327.1; -; Genomic_DNA. DR RefSeq; WP_003689884.1; NC_002946.2. DR RefSeq; YP_208739.1; NC_002946.2. DR ProteinModelPortal; Q5F660; -. DR DNASU; 3281159; -. DR EnsemblBacteria; AAW90327; AAW90327; NGO_1706. DR GeneID; 3281159; -. DR KEGG; ngo:NGO1706; -. DR PATRIC; 20337004; VBINeiGon24812_2042. DR HOGENOM; HOG000233519; -. DR OMA; CANSETL; -. DR OrthoDB; EOG6Q8J00; -. DR BioCyc; NGON242231:GI2G-1602-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00523937}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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; 33687 MW; 8155175933BCFB83 CRC64; MDTLFSLKVF RQVVQSGGFT RAADALGIST AMASKHVSHL ENTVQAKLLH HNSRNLSLTE AGEEYYRQCS YALDTLDDAA QKAAGGTEKP QGLLRVTMPL WFAGSQICNW LAEYRERYPE VALELILDNR HVDLIAEGVD LALRVSQTLS PSLIARPLAE IEFALLASPD FLRRNGVPET PEEVAGLPAV LPTYTNQQKL DLTRKSDGKK YRLELTPVIR TDNTLMMREM IKAGACIGYQ PLWAAEHDLR CGPLVRLLPG YAVPTDRLNA VYADRAFLSA KVRSFIDFLN EKIASRKGCR NAV // ID Q5FAG9_NEIG1 Unreviewed; 377 AA. AC Q5FAG9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209}; DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209}; DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209}; GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209}; GN ORFNames=NGO_0053 {ECO:0000313|EMBL:AAW88818.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88818.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP- CC Rule:MF_01209}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|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; AE004969; AAW88818.1; -; Genomic_DNA. DR RefSeq; WP_010950981.1; NC_002946.2. DR RefSeq; YP_207230.1; NC_002946.2. DR ProteinModelPortal; Q5FAG9; -. DR SMR; Q5FAG9; 5-368. DR EnsemblBacteria; AAW88818; AAW88818; NGO_0053. DR GeneID; 3282335; -. DR KEGG; ngo:NGO0053; -. DR PATRIC; 20332946; VBINeiGon24812_0058. DR HOGENOM; HOG000038087; -. DR KO; K01956; -. DR OMA; TNAHIGN; -. DR OrthoDB; EOG61ZTH6; -. DR BioCyc; NGON242231:GI2G-46-MONOMER; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000535; 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 {ECO:0000256|HAMAP-Rule:MF_01209}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 190 377 Glutamine amidotransferase type-1. FT {ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000259|PROSITE:PS51273}. FT REGION 1 186 CPSase. {ECO:0000256|HAMAP- FT Rule:MF_01209}. FT ACT_SITE 266 266 Nucleophile. {ECO:0000256|HAMAP- FT Rule:MF_01209}. FT ACT_SITE 350 350 {ECO:0000256|HAMAP-Rule:MF_01209}. FT ACT_SITE 352 352 {ECO:0000256|HAMAP-Rule:MF_01209}. SQ SEQUENCE 377 AA; 40622 MW; CB6924E7835FBAFC CRC64; MNTPALLVLA DGSVFHGTSI GYEGSASGEV VFNTSMTGYQ EILTDPSYCK QIVTLTYPHI GNTGTNAEDE ESRSVYAAGL IIRDLPLLHS SFRASESLHD YLVRNETVAI ADIDTRRLTM LLREKGAQGG AILTGADATV EKAQELIAAF GSMVGKDLAK EVSCTETYEW TEGEWELGKG FVTPDKQPYH VVAYDFGVKT NILRMLASRG CRLTVVPAQT SAEDVLALNP DGVFLSNGPG DPEPCTYAIE AVQKLMESGK PIFGICLGHQ LISLAIGAKT LKMRFSHHGA NHPVQDLDSG KVVITSQNHG FAVDADTLPA NARITHKSLF DNTLQGIELT DKPVFCFQGH PEASPGPQDV GYLFDKFIGN MKAAKQA // ID Q5F8R2_NEIG1 Unreviewed; 280 AA. AC Q5F8R2; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89425.1}; GN ORFNames=NGO_0701 {ECO:0000313|EMBL:AAW89425.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89425.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89425.1; -; Genomic_DNA. DR RefSeq; WP_003688774.1; NC_002946.2. DR RefSeq; YP_207837.1; NC_002946.2. DR EnsemblBacteria; AAW89425; AAW89425; NGO_0701. DR GeneID; 3281809; -. DR KEGG; ngo:NGO0701; -. DR PATRIC; 20334512; VBINeiGon24812_0828. DR HOGENOM; HOG000270329; -. DR OMA; LLYGIEQ; -. DR OrthoDB; EOG6SFP8T; -. DR BioCyc; NGON242231:GI2G-665-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 280 AA; 32738 MW; 442BDA9C2F79EB1C CRC64; MNFVLAKITC KKDLVKILSD DHIFPDFSYE NLNFITYNYD YNLDDDTWFQ IENLKNQDFC PKFLDNSNLF DSKMFSEIKK EEINIEKLKY LVSCTNDALF FQKITSSLLL KKKHLLTICG NGAKLCEPQD LLVIKDIPDA VYIIKDDKLI FRTLSSISNI FKGIEDLYRE ATNTEVQQFL ESDFIDLKED FLSEKVSIPN RKRIALVQDR LNNMTLDQRQ ELLNYLAEYN NNILKFNADG SRVEISTDVQ LKHLLYGIDE RYYTTALGKE KRLANSVQPI // ID Q5F741_NEIG1 Unreviewed; 171 AA. AC Q5F741; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89996.1}; GN ORFNames=NGO_1346 {ECO:0000313|EMBL:AAW89996.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89996.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89996.1; -; Genomic_DNA. DR RefSeq; WP_003691689.1; NC_002946.2. DR RefSeq; YP_208408.1; NC_002946.2. DR EnsemblBacteria; AAW89996; AAW89996; NGO_1346. DR GeneID; 3282513; -. DR KEGG; ngo:NGO1346; -. DR PATRIC; 20336065; VBINeiGon24812_1582. DR HOGENOM; HOG000219075; -. DR OMA; NAVYFGM; -. DR OrthoDB; EOG6M3PD1; -. DR BioCyc; NGON242231:GI2G-1260-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR018697; DUF2199. DR Pfam; PF09965; DUF2199; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 171 AA; 19363 MW; FD3291935B663D36 CRC64; MHTCTSCGEK HEDMPATGFT APYPYNQLSE EERIAYQAEC DSDFCIIRYS DQTDRFIRAA LPIPIIGHQE TLEYGVWVSV SEKSFNDYQS RFYDNPENAV YFGMICNRLP PYETDTFGLH CNVVTQSDNQ RPLLQLHQSG GHPPVRDFYH GMGYAEAQAR IGAVSESDCS G // ID Q5F525_NEIG1 Unreviewed; 624 AA. AC Q5F525; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 66. DE SubName: Full=Aminobenzoate synthetase {ECO:0000313|EMBL:AAW90712.2}; GN ORFNames=NGO_2112 {ECO:0000313|EMBL:AAW90712.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90712.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90712.2; -; Genomic_DNA. DR ProteinModelPortal; Q5F525; -. DR EnsemblBacteria; AAW90712; AAW90712; NGO_2112. DR PATRIC; 20338065; VBINeiGon24812_2555. DR HOGENOM; HOG000025145; -. DR OMA; YQVNLTM; -. DR OrthoDB; EOG6D5G6B; -. DR BioCyc; NGON242231:GI2G-2006-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.60.120.10; -; 2. 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; 2. DR SUPFAM; SSF56752; SSF56752; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 109 345 Chorismate_bind. FT {ECO:0000259|Pfam:PF00425}. SQ SEQUENCE 624 AA; 68807 MW; 6DD50B62AC664EFA CRC64; MPYFALFDDA VSRRAKLYQN HVESRFFRPE ELDALDGALQ SGWQKGLHSV LFADYEFGLP LMGMESERGG NIALHWFADC ADTDAESWLA RHSDGLPAGI STPQSSVSET DYLDRIRQIH EAIRRGDTYQ INYTTRLHLQ AYGNPVSLYR RLRQPVPYAV LSHLPDEAGQ SAWTLCFSPE LFLNIASDGT ISTEPMKGTA PILGDGQDER RAAELQTDPK NRAENVMIVD LLRNDLGKIA QTGKVCVPEP FKVSRFGSVW QMTSTIRAQA LPDTSFADTL RAAFPCGSIT GAPKKMSMQI IESLETEARG LYTGSIGYLN PCSGGLGFEG AFNVVIRTLS LKPVSDGIVS GIGGTDSNAQ ARTAGQGGET PHPFEANPPY RGVYGVGSGI VIDSDPAAEY RECGWKARFL NELRPDFGIF ETLRAENRQC ALLDRHLCRL KTSAQALNLP LPDGCENQIK QYIADLPDGA FRIKALLASD GISLSHAVLN RLTDKQRVII SPTILPAQNY LRRFKTTHRA IFDQAWQTAE TQGAFDSLFF NSDGILLEGG RSNVFVKHRG QWLTPSLDLD ILNGIMRQAV SDEPQKYLHT NQVIETHITQ KTLQGAEEIR LSNALRGVFA AVLA // ID Q5F8L0_NEIG1 Unreviewed; 46 AA. AC Q5F8L0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW89477.1}; GN ORFNames=NGO_0762 {ECO:0000313|EMBL:AAW89477.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89477.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89477.1; -; Genomic_DNA. DR RefSeq; WP_003691201.1; NC_002946.2. DR RefSeq; YP_207889.1; NC_002946.2. DR EnsemblBacteria; AAW89477; AAW89477; NGO_0762. DR GeneID; 3282474; -. DR KEGG; ngo:NGO0762; -. DR PATRIC; 20334672; VBINeiGon24812_0908. DR BioCyc; NGON242231:GI2G-717-MONOMER; -. DR Proteomes; UP000000535; Chromosome. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 46 AA; 5098 MW; 53B9D7505869BBBA CRC64; MDYSGYGGGC FKTRPGCRLQ NFGLRLRLRG LPARNTQTLS HNLAAE // ID Q5FAD8_NEIG1 Unreviewed; 473 AA. AC Q5FAD8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 50. DE SubName: Full=Polysaccharide biosynthesis family protein {ECO:0000313|EMBL:AAW88849.1}; GN ORFNames=NGO_0088 {ECO:0000313|EMBL:AAW88849.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW88849.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW88849.1; -; Genomic_DNA. DR RefSeq; WP_003704927.1; NC_002946.2. DR RefSeq; YP_207261.1; NC_002946.2. DR EnsemblBacteria; AAW88849; AAW88849; NGO_0088. DR GeneID; 3282288; -. DR KEGG; ngo:NGO0088; -. DR PATRIC; 20333063; VBINeiGon24812_0115. DR HOGENOM; HOG000218779; -. DR OMA; LFCTLVE; -. DR OrthoDB; EOG6R87BG; -. DR BioCyc; NGON242231:GI2G-78-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; 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}. FT TRANSMEM 412 429 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 473 AA; 50922 MW; B0B5403989DBC4AA CRC64; MDTKEILGYA AGSIGSAVLA VIILPLLSWY FPADDIGRIV LMQTAAGLTV SVLCLGLDQA YVREYYAAAD KDTLFKTLFL PPLLFSAAIA ALLLSRPSLP SEILFSLDDA AAGIGLVLFE LSFLPIRFLL LVLRMEGRAL AFSSAQLVPK LAILLLLPLT VGLLHFPANT SVLTAVYALA NLAAAAFLLF QNRCRLKAVR RAPFSPAVLH RGLRYGIPLA LSSLAYWGLA SADRLFLKKY AGLEQLGVYS MGISFGGAAL LLQSIFSTVW TPYIFRAIEE NATPARLSAT AESAAALLAS ALCLTGIFSP LASLLLPENY AAVRFTVVSC MLPPLFYTLT EISGIGLNVV RKTRPIALAT LGALAANLLL LGLAVPSGGT RGAAVACAAS FWLFFVFKTE SSCRLWQPLK RLPLYMHTLF CLASSAAYTC FGTPANYPLF AGVWAAYLAG CILRHRKNLH KLFHYLKKQG FPL // ID Q5F7H0_NEIG1 Unreviewed; 189 AA. AC Q5F7H0; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 2. DT 17-FEB-2016, entry version 52. DE SubName: Full=Restriction endonuclease {ECO:0000313|EMBL:AAW89867.2}; GN ORFNames=NGO_1208 {ECO:0000313|EMBL:AAW89867.2}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89867.2, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89867.2; -; Genomic_DNA. DR REBASE; 1325; NgoAIII. DR EnsemblBacteria; AAW89867; AAW89867; NGO_1208. DR HOGENOM; HOG000005537; -. DR OMA; LDGFGNH; -. DR OrthoDB; EOG69PQ4V; -. DR BioCyc; NGON242231:GI2G-1119-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR018575; Restrct_endonuc_II_Eco29kI. DR Pfam; PF09517; RE_Eco29kI; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Endonuclease {ECO:0000313|EMBL:AAW89867.2}; KW Hydrolase {ECO:0000313|EMBL:AAW89867.2}; KW Nuclease {ECO:0000313|EMBL:AAW89867.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 189 AA; 21475 MW; 2C74BC18A1BDC41E CRC64; MRFFHGTPVH TLPPPKQFKG AGVYAIYYIG NNPLYKQYAD WNRLSYNAPI YVGKAVPKGW RQARNSDNAL NQSTELFHRL KEHSRSIAAV SDLDPSDFMC RFVIFEGAGS DMIGTIEAAL IKLHKPLWNS CVDGFGNHDP GKGRYEQAKS DWDVLHSGRV WADRLNGIPN SYESILENIN THLEIIKRK // ID Q5F8X3_NEIG1 Unreviewed; 148 AA. AC Q5F8X3; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 17-FEB-2016, entry version 71. DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AAW89364.1}; GN ORFNames=NGO_0637 {ECO:0000313|EMBL:AAW89364.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89364.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains HTH rrf2-type DNA-binding domain. CC {ECO:0000256|SAAS:SAAS00151869}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004969; AAW89364.1; -; Genomic_DNA. DR RefSeq; WP_003688879.1; NC_002946.2. DR RefSeq; YP_207776.1; NC_002946.2. DR ProteinModelPortal; Q5F8X3; -. DR EnsemblBacteria; AAW89364; AAW89364; NGO_0637. DR GeneID; 3281388; -. DR KEGG; ngo:NGO0637; -. DR PATRIC; 20334358; VBINeiGon24812_0751. DR HOGENOM; HOG000249812; -. DR KO; K13643; -. DR OMA; MTHDLWS; -. DR OrthoDB; EOG63FW56; -. DR BioCyc; NGON242231:GI2G-604-MONOMER; -. DR Proteomes; UP000000535; 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 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW DNA-binding {ECO:0000256|SAAS:SAAS00448026}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 148 AA; 15999 MW; 1C2F2B665163A41B CRC64; MRLTTKGRFA VTAMLDLAMN AQTGAVKLSA ISERQNISLS YLEQLFGKLR RAGLVESLRG PGGGYILAAP PAQINIAQII SAAEDRLDAT QCGSKANCHH GAPCLTHDLW ENLNKTINDY LGSVTLQSII EQKNNGDGSR VVQFTHIH // ID Q5F700_NEIG1 Unreviewed; 107 AA. AC Q5F700; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAW90037.1}; GN ORFNames=NGO_1389 {ECO:0000313|EMBL:AAW90037.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90037.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90037.1; -; Genomic_DNA. DR RefSeq; WP_003695639.1; NC_002946.2. DR RefSeq; YP_208449.1; NC_002946.2. DR ProteinModelPortal; Q5F700; -. DR EnsemblBacteria; AAW90037; AAW90037; NGO_1389. DR GeneID; 3281152; -. DR KEGG; ngo:NGO1389; -. DR PATRIC; 20336171; VBINeiGon24812_1634. DR HOGENOM; HOG000220764; -. DR OMA; MIVDEKS; -. DR OrthoDB; EOG6091GB; -. DR BioCyc; NGON242231:GI2G-1302-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR Gene3D; 3.30.70.970; -; 1. DR InterPro; IPR009671; RraB_dom. DR Pfam; PF06877; RraB; 1. DR SUPFAM; SSF89946; SSF89946; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 103 RraB. {ECO:0000259|Pfam:PF06877}. SQ SEQUENCE 107 AA; 12213 MW; AF454D27B299F843 CRC64; MIIDEKSTSD VLKQYQELGF DLTKPMIIEF FIGGSQKNLQ SIESQLISYR QDFQISIEQD EFGEMWTCYC SVNIVPSLEN ILAIETTLFG IAQKNDCNYE GFGSYGN // ID Q5F570_NEIG1 Unreviewed; 421 AA. AC Q5F570; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920}; GN ORFNames=NGO_2060 {ECO:0000313|EMBL:AAW90667.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90667.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_00920}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00920}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_00920}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000256|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; AE004969; AAW90667.1; -; Genomic_DNA. DR RefSeq; WP_010951395.1; NC_002946.2. DR RefSeq; YP_209079.1; NC_002946.2. DR ProteinModelPortal; Q5F570; -. DR SMR; Q5F570; 128-420. DR EnsemblBacteria; AAW90667; AAW90667; NGO_2060. DR GeneID; 3282736; -. DR KEGG; ngo:NGO2060; -. DR PATRIC; 20337921; VBINeiGon24812_2483. DR HOGENOM; HOG000036278; -. DR KO; K03110; -. DR OMA; ALFIHEE; -. DR OrthoDB; EOG62K1ZH; -. DR BioCyc; NGON242231:GI2G-1961-MONOMER; -. DR Proteomes; UP000000535; 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:0051301; P:cell division; IEA:UniProtKB-KW. 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 cycle {ECO:0000313|EMBL:AAW90667.1}; KW Cell division {ECO:0000313|EMBL:AAW90667.1}; KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00920}; KW Receptor {ECO:0000256|HAMAP-Rule:MF_00920}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 394 407 SRP54. {ECO:0000259|PROSITE:PS00300}. FT NP_BIND 228 235 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 309 313 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. FT NP_BIND 373 376 GTP. {ECO:0000256|HAMAP-Rule:MF_00920}. SQ SEQUENCE 421 AA; 44759 MW; F7FCA674F4E94E9C CRC64; MFSFFRRKKK QETPALEEAQ VQETAAKVES EVAQIVGNIK EDVESLAESV KGRAESAVET VSGAVEQVKE TVAEMPSEAG EAAEKAVERV ESAKEAVAET VGEAVGQVQE AVATTEEHKL GWAARLKQGL AKSRDKMAKS LAGVFGGGQI GEDLYEELET VLITGDMGME ATEYLMKDVR GRVSLKGLKD GNELRGALKE ALYDLIKPLE KPLVLPETKE PFVIMLAGIN GAGKTTSIGK LAKYFQAQGK SVLLAAGDTF RAAAREQLQA WGGRNNVTVI SQTTGDSAAV CFDAVQAAKA RGIDIVLADT AGRLPTQLHL MEEIKKVKRV LQKAIPGAPH EIIVVLDANI GQNAVNQVKA FDDALGLTGL IVTKLDGTAK GGILAALASD RPVPVRYIGV GEGIDDLRPF DARAFVDALL D // ID Q5F8M7_NEIG1 Unreviewed; 707 AA. AC Q5F8M7; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 79. DE SubName: Full=DNA polymerase III subunits gamma and tau {ECO:0000313|EMBL:AAW89460.1}; DE EC=2.7.7.7 {ECO:0000313|EMBL:AAW89460.1}; GN ORFNames=NGO_0743 {ECO:0000313|EMBL:AAW89460.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89460.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89460.1; -; Genomic_DNA. DR RefSeq; WP_003695312.1; NC_002946.2. DR RefSeq; YP_207872.1; NC_002946.2. DR ProteinModelPortal; Q5F8M7; -. DR SMR; Q5F8M7; 3-361. DR EnsemblBacteria; AAW89460; AAW89460; NGO_0743. DR GeneID; 3281850; -. DR KEGG; ngo:NGO0743; -. DR PATRIC; 20334626; VBINeiGon24812_0885. DR HOGENOM; HOG000083934; -. DR KO; K02343; -. DR OMA; TEDWRDE; -. DR OrthoDB; EOG6WQD76; -. DR BioCyc; NGON242231:GI2G-700-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Nucleotidyltransferase {ECO:0000313|EMBL:AAW89460.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Transferase {ECO:0000313|EMBL:AAW89460.1}. FT DOMAIN 37 179 AAA. {ECO:0000259|SMART:SM00382}. SQ SEQUENCE 707 AA; 76083 MW; 234F013552F97756 CRC64; MAYQVLARKW RPKTFSDLVG QEHVVKALQN ALDEGRLHHA YLLTGTRGVG KTTIARILAK SLNCENAQHG EPCGVCQSCT QIDAGRYVDL LEIDAASNTG IDNIREVLEN AQYAPTAGKY KVYIIDEVHM LSKSAFNAML KTLEEPPEHV KFILATTDPH KVPVTVLSRC LQFVLRNMTA QQVADHLAHV LDSEKIAYDP PALQLLGRAA AGSMRDALSL LDQAIALGSG KVAENDVRQM IGAVDKQYLY ELLTGIVNQD GEALLAKAQE MAACAVGFDN ALGELAILLQ QLALIQAVPS ALAHDDPDSD ILHRLAQTIS GEQIQLYYQI AVHGKRDLGL APDEYAGFMM TLLRMLAFAP LAAASCDANA VIENTELQSP SAQTAEKETA AKKPQPRPEA DAAQTPVQTA SAAAMPSEGK TAGPVSHQEN NDVPPWEDAP DKTETAAGTA RTSAKSIQTA SEAETPPENQ VSKNKAADNE TEASLSEVPS ENPIQATPND EAVETETFAH EAPAEPFYGF PDNDCPPEDG VEIPPPDWAN VLPADTAGGG TDEEAEAGGI GGNNTPSAPP PEFSTENWAA IVRHFARKLG AAQMPAQHSA WTEYRSDTGL MVLAMTAEAR ATADKKRLDK IRDTLAQAYG LQLTLQTEDW RDEAGRETPA MQDKRVQAED RQKAQALLEA DPAAQKILQA FGAQWQPESL ELAANRP // ID Q5F6I8_NEIG1 Unreviewed; 312 AA. AC Q5F6I8; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AAW90199.1}; GN ORFNames=NGO_1566 {ECO:0000313|EMBL:AAW90199.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90199.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90199.1; -; Genomic_DNA. DR RefSeq; WP_003689486.1; NC_002946.2. DR RefSeq; YP_208611.1; NC_002946.2. DR ProteinModelPortal; Q5F6I8; -. DR DNASU; 3281359; -. DR EnsemblBacteria; AAW90199; AAW90199; NGO_1566. DR GeneID; 3281359; -. DR KEGG; ngo:NGO1566; -. DR PATRIC; 20336642; VBINeiGon24812_1867. DR HOGENOM; HOG000219101; -. DR OMA; GHRTLQS; -. DR OrthoDB; EOG62RS8R; -. DR BioCyc; NGON242231:GI2G-1467-MONOMER; -. DR Proteomes; UP000000535; 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:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 312 AA; 35417 MW; F8AFE7C6143624CC CRC64; MDAYPEAEAP LQSIVELVPV LIAVTDGGLR VLTVAQGTLL PNGPLSPLRN SLQAGVKLWV AKQTSQPMGY VEQLYTFVDT HRRNEHGMPV LYVSYLGLVR EAADSILHPD AKWQDCYGYF PWEDLRTDGG QRDAVVSRLR IWANSADTEE VRQKRLKHIH LCWGVEPENW SEEYVLQRYE MLYESGLIAE AAEPQANFDF ALTGQTMRHD HRRVLATALS RLRAKIKYRP VIFELMPPGF TLLQLQNSVE AISGRLLHKQ NFRRQIQQQN LIEPSDTGVS GSKGRPAQLY RFRDNVLSDR LISDIGLPLG SR // ID Q5F8Z6_NEIG1 Unreviewed; 759 AA. AC Q5F8Z6; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 16-MAR-2016, entry version 77. DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410}; DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410}; GN ORFNames=NGO_0614 {ECO:0000313|EMBL:AAW89341.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89341.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89341.1; -; Genomic_DNA. DR RefSeq; WP_003702805.1; NC_002946.2. DR RefSeq; YP_207753.1; NC_002946.2. DR ProteinModelPortal; Q5F8Z6; -. DR SMR; Q5F8Z6; 7-739. DR EnsemblBacteria; AAW89341; AAW89341; NGO_0614. DR GeneID; 3281267; -. DR KEGG; ngo:NGO0614; -. DR PATRIC; 20334310; VBINeiGon24812_0727. DR HOGENOM; HOG000278076; -. DR KO; K00525; -. DR OMA; YELLWQM; -. DR OrthoDB; EOG6J48HC; -. DR BioCyc; NGON242231:GI2G-581-MONOMER; -. DR UniPathway; UPA00326; -. DR Proteomes; UP000000535; 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:UP000000535}; KW DNA replication {ECO:0000256|RuleBase:RU003410}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00511196}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003410, KW ECO:0000313|EMBL:AAW89341.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. FT DOMAIN 7 97 ATP-cone. {ECO:0000259|PROSITE:PS51161}. SQ SEQUENCE 759 AA; 85169 MW; B52B86AA3F7C5D93 CRC64; MNTPTDLKVT KRDGRLEAID LDKIHRVVTW AAEGLENVSV SQVELKSHIQ FYNGIRTDDI HETIIKAAAD LISEDTPDYQ YLAARLAIFH LRKIAYGEYE PPHLYNHVKK LTDAGKYDRH ILEDYSREEF DELNAYIDHE RDMSFSYAAV KQLEGKYLVQ NRVTRQIYET PQFLYVLVAM CLFSKYPKEA RLDYVKRFYD AVSTFKVSLP TPIMSGVRTP TRQFSSCVLI ECDDSLDSIN ATTSAIVKYV SQRAGIGINA GRIRGLDSEI RGGEARHTGC IPFFKMFQAA VKSCSQGGVR GGAATLFYPL WHIEAESLLV LKNNRGVEDN RIRQLDYGVQ INRLLYTRLI KGGNITLFSP NEVSGLYEAF FADQDEFERL YTKYEQDPNI RKRIIPAADL FSTLMQERAG TGRIYIQNVD HCNTHSPFDP RVAPVHQSNL CMEIALPTKP LDNINDPDGE IALCTLSAFN LGALNSLDEL EGLADLTVRA LDALLDYQGY PVEAARTSTM DRRSLGIGVI NYAYYLAKNG VRYSDGSALG LTHRTFEAIQ YYLLKASANL AKEYGACTLF NQTVYSQGKL PIDTYKKDLD AVCGEPLHYD WESLRADIVK YGLRNSTLTA LMPSETSSQI ANATNGIEPP RGLVTVKASK DGILKQVVPE FETLKNAYET LWQLPGNEGY LKLVGVMQKF VDQAISANTA YDPGKFEGNK VSMKQMLKDL LTAYKYGVKT LYYHNTRDGA DDTQTDIQDD GCAGGACKI // ID Q5F537_NEIG1 Unreviewed; 56 AA. AC Q5F537; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 20-JAN-2016, entry version 45. DE SubName: Full=Prokaryotic lipo-attachment site family protein {ECO:0000313|EMBL:AAW90700.1}; GN ORFNames=NGO_2099 {ECO:0000313|EMBL:AAW90700.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW90700.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW90700.1; -; Genomic_DNA. DR RefSeq; WP_003687071.1; NC_002946.2. DR RefSeq; YP_209112.1; NC_002946.2. DR EnsemblBacteria; AAW90700; AAW90700; NGO_2099. DR GeneID; 3282818; -. DR KEGG; ngo:NGO2099; -. DR PATRIC; 20338035; VBINeiGon24812_2540. DR HOGENOM; HOG000218735; -. DR OMA; ACGYKGG; -. DR OrthoDB; EOG6J752D; -. DR BioCyc; NGON242231:GI2G-1994-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR032831; LPAM_2. DR Pfam; PF13627; LPAM_2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}. SQ SEQUENCE 56 AA; 5890 MW; E8E7E956B765D6A0 CRC64; MKYGVFFAAA TALLLSACGY KGGLYLPKEG DTARFGVIQT GLQLQGKPQS APPTQK // ID Q5F7U9_NEIG1 Unreviewed; 468 AA. AC Q5F7U9; DT 15-MAR-2005, integrated into UniProtKB/TrEMBL. DT 15-MAR-2005, sequence version 1. DT 09-DEC-2015, entry version 50. DE SubName: Full=Septum formation inhibitor Maf {ECO:0000313|EMBL:AAW89738.1}; GN ORFNames=NGO_1068 {ECO:0000313|EMBL:AAW89738.1}; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89738.1, ECO:0000313|Proteomes:UP000000535}; RN [1] {ECO:0000313|Proteomes:UP000000535} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535}; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) 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; AE004969; AAW89738.1; -; Genomic_DNA. DR RefSeq; WP_010951171.1; NC_002946.2. DR RefSeq; YP_208150.1; NC_002946.2. DR EnsemblBacteria; AAW89738; AAW89738; NGO_1068. DR GeneID; 3281798; -. DR KEGG; ngo:NGO1068; -. DR PATRIC; 20335370; VBINeiGon24812_1251. DR HOGENOM; HOG000218708; -. DR OMA; MKLSIQK; -. DR OrthoDB; EOG6FFS2K; -. DR BioCyc; NGON242231:GI2G-983-MONOMER; -. DR Proteomes; UP000000535; Chromosome. DR InterPro; IPR008106; Adhesin_MafB. DR Pfam; PF06255; DUF1020; 1. DR PRINTS; PR01732; ADHESINMAFB. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000535}; KW Reference proteome {ECO:0000313|Proteomes:UP000000535}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 468 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004256059. SQ SEQUENCE 468 AA; 50734 MW; B464174C27932D17 CRC64; MNLPIQKFMM LFAAAISLLQ IPISHANGLD ARLRDDMQAK HYEPGGKYHL FGNARGSVKN RVCAVQTFDA TAVGPILPIT HERTGFEGVI GYETHFSGHG HEVHSPFDNH DSKSTSDFSG GVDGGFTVYQ LHRTGSEIHP EDGYDGPQGG GYPPPGGARD IYSYHIKGTS TKTKINTVPQ APFSDRWLKE NAGAASGFLS RADEAGKLIW ENDPDKNWRA NRMDDIRGIV QGAVNPFLTG FQGLGVGAIT DSAVSPVTYA AARKTLQGIH NLGNLSPEAQ LAAATALQDS AFAVKDSINS ARQWADAHPN ITATAQTALA VTEAATTVWG GKKVELNPAK WDWVKNTGYK KPAARHMQTV DGEMAGGNKP LESKNTVTTN NFFENTGYTE KVLRQASNGD YHGFPQSVDA FSENGTVIQI VGGDNIVRHK LYIPGSYKGK DGNFEYIREA DGKINHRLFV PNQQLPEK //